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Journal Articles

Small-number effects limit chromosome segregation synchrony

Andreas Boland
Journal: Journal of Cell Biology
J Cell Biol (2026) 225 (7): e202605017.
https://doi.org/10.1083/jcb.202605017
Published: 23 June 2026
View article titled, Small-number effects limit chromosome segregation synchrony
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Journal Articles

When neuroligin-2 sticks around, astrocytes take shape

Sneha Ray, Aakanksha Singhvi
Journal: Journal of Cell Biology
J Cell Biol (2026) 225 (7): e202606021.
https://doi.org/10.1083/jcb.202606021
Published: 18 June 2026
View article titled, When neuroligin-2 sticks around, astrocytes take shape
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Images
A multi-panel diagram illustrating the role of Nedd4l in astrocyte morphogenesis through the interaction with neuroligins.

NLs are functionally diverse, and astrocytic NL2 is ubiquitinated by Nedd4l...

in When neuroligin-2 sticks around, astrocytes take shape > Journal of Cell Biology
Published: 18 June 2026
Figure 1. NLs are functionally diverse, and astrocytic NL2 is ubiquitinated by Nedd4l for proper astrocyte morphogenesis. (A) The authors used in vivo BioID to identify the interactomes for astrocyte NL1–3 and neuronal NL2. (B) In wild-type More about this image found in NLs are functionally diverse, and astrocytic NL2 is ubiquitinated by Nedd4l...
Journal Articles

Redox-dependent S-glutathionylation of Aurora-A kinase by Gstp promotes postsynaptic maturation

Shuji Wakatsuki, Akiko Yumoto, Takehiro Suzuki, Naoshi Dohmae, Toshiyuki Araki
Journal: Journal of Cell Biology
J Cell Biol (2026) 225 (8): e202509200.
https://doi.org/10.1083/jcb.202509200
Published: 12 June 2026
View article titled, Redox-dependent S-glutathionylation of Aurora-A kinase by Gstp promotes postsynaptic maturation
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Includes: Supplementary data
Journal Articles

Met-Vision reveals coexisting energetic states in tissue macrophages redistributed by inflammation

Adriana Lecourieux, Margot Bardou, Zacarias Garcia, Philippe Bousso
Journal: Journal of Cell Biology
J Cell Biol (2026) 225 (8): e202603170.
https://doi.org/10.1083/jcb.202603170
Published: 12 June 2026
View article titled, Met-Vision reveals coexisting energetic states in tissue macrophages redistributed by inflammation
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Journal Articles

Fibroblast depletion reveals mammalian epithelial resilience across neonatal and adult stages

Isabella M. Gaeta, Shuangshuang Du, Clémentine Villeneuve, David G. Gonzalez, Catherine Matte-Martone, Smirthy Ganesan, Deandra Simpson, Hilldana Tibebu, Jessica L. Moore, Chen Yuan Kam, Sara Gallini, Haoyang Wei, Fabien Bertillot, Dagmar Zeuschner, Lauren E. Gonzalez, Ushnish Rana, Kaelyn D. Sumigray, Sara A. Wickström, Valentina Greco
Journal: Journal of Cell Biology
J Cell Biol (2026) 225 (8): e202507165.
https://doi.org/10.1083/jcb.202507165
Published: 12 June 2026
View article titled, Fibroblast depletion reveals mammalian epithelial resilience across neonatal and adult stages
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Images
Aurora-A is specifically activated and glutathionylated at the PSD during the peak window of synaptogenesis. (A–C) Developmental profile of Aurora-A modification in the murine brain. (A and B) PSD fractions were prepared from murine cerebral cortex at the indicated postnatal days. Representative immunoblots of PSD fractions (A) and immunoprecipitates (IP) of total Aurora-A (B) are shown. β-Actin serves as a loading control for lysates. (C) Densitometric quantification of T288-phosphorylated and -glutathionylated Aurora-A levels, normalized to total Aurora-A, and shown relative to P0 (mean ± SEM, n = 3 animals per time point). The data reveal a marked increase in both modifications during the peak phase of synaptogenesis (P14). Statistical significance (**P < 0.01; ****P < 0.0001; n.s., P > 0.05) was determined by one-way ANOVA followed by Tukey’s multiple comparisons test. (D–F) Recapitulation of the synaptogenic activation program in primary neurons. (D and F) Whole-cell lysates and PSD fractions from cultured cortical neurons were analyzed at the indicated DIV. Representative immunoblots (D) and immunoprecipitates of total Aurora-A (E) confirm the temporal increase in Aurora-A modifications. (F) Quantified levels of T288-phosphorylated and -glutathionylated Aurora-A relative to DIV7 (mean ± SEM, n = 3 independent experiments). Consistent with the in vivo data, modification levels surge during the period of active synapse formation (DIV 7–14). Statistical significance (*P < 0.05; ***P < 0.001; ****P < 0.0001) was determined by one-way ANOVA followed by Tukey’s multiple comparisons test. (G) Spatial localization of active Aurora-A at the postsynaptic site. Representative photomicrographs of cultured cortical neurons (DIV14) immunostained for total Aurora-A or phosphorylated Aurora-A (pT288; red), MAP2 (blue), and PSD95 (green). Merged images highlight the overlap between Aurora-A and the postsynaptic marker PSD95 (yellow). Quantitative analysis demonstrates that 64.2 ± 4.4% and 42.3 ± 2.7% of PSD95-positive puncta exhibit immunoreactivity for total and active Aurora-A, respectively. Scale bar, 10 μm. Data were pooled from 30 neurons from five independent cultures. Source data are available for this figure: SourceData F1.

Aurora-A is specifically activated and glutathionylated at the PSD during t...

in Redox-dependent S-glutathionylation of Aurora-A kinase by Gstp promotes postsynaptic maturation > Journal of Cell Biology
Published: 12 June 2026
Figure 1. Aurora-A is specifically activated and glutathionylated at the PSD during the peak window of synaptogenesis. (A–C) Developmental profile of Aurora-A modification in the murine brain. (A and B) PSD fractions were prepared from murine More about this image found in Aurora-A is specifically activated and glutathionylated at the PSD during t...
Images
C290 glutathionylation promotes Aurora-A dimerization and autophosphorylation. (A) Cortical neurons from murine E14 embryos were cultured for the indicated number of DIV following adenoviral infection. Representative immunoblots show expression of the indicated molecules, confirming WT and C290A mutant HA-tagged Aurora-A. β-Actin serves as a loading control. (B) Quantification of the postsynaptic marker PSD95, normalized to β-actin, and expressed relative to WT Aurora-A–transfected controls at DIV7 (mean ± SEM, n = 5), demonstrating progressive synapse formation over the culture period. Significant differences from the control (***P < 0.001; ****P < 0.0001) were determined by two-way ANOVA with Sidak’s post hoc test. (C and D) Detection of free thiol groups in HA-Aurora-A using PEG-PCMal. Cultured cortical neurons expressing HA-tagged WT or C290A Aurora-A were lysed with RIPA buffer containing 1 mM PEG-PCMal at 37°C for 30 min at the indicated DIV. HA-Aurora-A was purified, separated by SDS-PAGE, and the gels were irradiated with 302 nm ultraviolet light to cleave the PEG chains. Proteins were transferred to polyvinylidene fluoride membranes and probed with anti-HA antibody. Representative immunoblots (C) showing PEG modification of the free thiol at C290 in WT Aurora-A, resulting in a ∼5 kDa upward shift per labeled thiol, whereas no shift was observed in C290A Aurora-A. PEG-modified bands showing the upward shift are indicated by the filled triangle, while non-modified bands are indicated by the open triangle. These data indicate that the C290 residue of Aurora-A undergoes extensive posttranslational modification specifically during the peak period of synaptogenesis. (D) Quantification of PEG-modified bands (indicated by the filled triangle in C), normalized to β-actin, and expressed relative to WT Aurora-A–transfected controls at DIV7 (mean ± SEM, n = 5). Significant differences from the control (***P < 0.001; ****P < 0.0001) were determined by two-way ANOVA with Sidak’s post hoc test. (E) Immunoblot confirming the expression of WT and C290A mutant HA-tagged Aurora-A in cultured cortical neurons 10 days postadenoviral infection. β-Actin serves as a loading control. (F) Immunoprecipitation (IP) with anti-HA antibody followed by non-reducing immunoblotting reveals glutathionylated Aurora-A and Aurora-A dimers (detected by anti-HA and anti-pT288 antibodies) in neurons expressing WT Aurora-A. These signals are absent in neurons expressing the C290A mutant. Open triangle indicates the dimeric form of Aurora-A detected under nonreducing conditions. (G) Quantification of dimerized (nonreducing blot), glutathionylated (nonreducing blot), and pT288 (reducing blot) Aurora-A expression levels, normalized to β-actin, and expressed relative to mock-transfected controls (mean ± SEM, n = 5). For each parameter, differences between control and treated groups (***P < 0.001) were analyzed using unpaired two-tailed Welch’s t tests with Holm’s correction for multiple comparisons. Source data are available for this figure: SourceData F2.

C290 glutathionylation promotes Aurora-A dimerization and autophosphorylati...

in Redox-dependent S-glutathionylation of Aurora-A kinase by Gstp promotes postsynaptic maturation > Journal of Cell Biology
Published: 12 June 2026
Figure 2. C290 glutathionylation promotes Aurora-A dimerization and autophosphorylation. (A) Cortical neurons from murine E14 embryos were cultured for the indicated number of DIV following adenoviral infection. Representative immunoblots show More about this image found in C290 glutathionylation promotes Aurora-A dimerization and autophosphorylati...
Images
Gstp-mediated glutathionylation of Aurora-A is required for synaptogenesis. (A) RT-qPCR screening of 18 cytoplasmic Gst isoforms in cultured cortical neurons. Among the isoforms tested, Gstp1 and Gstp2 exhibited the highest fold-induction during synaptogenesis. Concurrent increases in the expression of synaptic marker genes (synapsin I, synaptophysin, PSD95, and GluA1) confirm progression of synaptic maturation. (B–D) Suppression of Gstp expression inhibits Aurora-A glutathionylation and T288 phosphorylation. Cortical neurons from murine E14 embryos were cultured and infected at DIV5 with lentiviral vectors expressing the indicated molecules. (B) Representative immunoblots showing expression of the indicated proteins. β-Actin serves as a loading control. (C) Quantification of each Gst isoform, normalized to β-actin and relative to mock-infected controls (mean ± SEM, n = 5). Significant differences from control levels (****P < 0.0001) were determined by one-way ANOVA followed by Tukey’s multiple comparisons test. Due to the lack of isoform-specific antibodies, the efficacy of Gstm7 knockdown was validated by RT-qPCR (Table S1), which confirmed that the magnitude of mRNA depletion was comparable with that of Gstp1/2. (D) Quantification of ERK phosphorylation (phospho-ERK/total ERK), presynaptic markers synapsin I and synaptophysin, and postsynaptic markers PSD95 and GluA1. All values are normalized to β-actin and relative to mock-infected controls (mean ± SEM, n = 5). Significant differences from control levels (***P < 0.001; ****P < 0.0001) were determined by one-way ANOVA followed by Tukey’s multiple comparisons test. (E) Representative immunoblot analysis of Aurora-A immunoprecipitates. (F) Quantification of glutathionylated and pT288 Aurora-A levels, normalized to β-actin and relative to mock-infected controls (mean ± SEM, n = 5). Significant differences from control levels (****P < 0.0001) were determined by one-way ANOVA followed by Tukey’s multiple comparisons test. (G and H) Gstp knockdown reduces synapse formation. (G) Representative images of cortical neurons (DIV14–16) infected with the indicated shRNA-expressing lentiviruses and double-immunostained for PSD95 and synapsin I. (H) Colocalization panels (bottom panels; black) represent double-positive signals. Scale bar, 10 µm. Quantification shows the number of synapses per 10 µm of dendritic length. Significant differences from the control (*P < 0.05) were determined by one-way ANOVA with Tukey’s post hoc test. Source data are available for this figure: SourceData F3.

Gstp-mediated glutathionylation of Aurora-A is required for synaptogenesis....

in Redox-dependent S-glutathionylation of Aurora-A kinase by Gstp promotes postsynaptic maturation > Journal of Cell Biology
Published: 12 June 2026
Figure 3. Gstp-mediated glutathionylation of Aurora-A is required for synaptogenesis. (A) RT-qPCR screening of 18 cytoplasmic Gst isoforms in cultured cortical neurons. Among the isoforms tested, Gstp1 and Gstp2 exhibited the highest More about this image found in Gstp-mediated glutathionylation of Aurora-A is required for synaptogenesis....
Images
Co-enrichment of Aurora-A and Gstp at the PSD in the mouse brain. (A) Representative immunoblots of biochemical fractions prepared from P14 murine brain lysates. Whole-brain lysate, synaptosome, and detergent-extracted PSD fractions were analyzed with the indicated antibodies. (B) Enrichment index of Aurora-A and Gst isoforms in the PSD fraction. The enrichment index was calculated by dividing the PSD–to–whole-brain lysate ratio of each target protein by the corresponding GAPDH ratio. A value of 1.0 indicates a distribution equivalent to that of GAPDH. PSD95 and synapsin I are shown as positive controls for PSD sequestration but were excluded from the statistical analysis of the Gst/Aurora-A group to maintain variance homogeneity. Significant enrichment of Aurora-A, Gstp1, and Gstp2 was determined by comparing their indices with that of the cytoplasmic isoform Gstm5 (mean ± SEM, n = 3; *P < 0.05; ****P < 0.0001 by one-way ANOVA with Tukey’s post hoc test). (C) Gst-specific activity in biochemical fractions. Activity was measured using CDNB as a substrate and expressed as milliunits per milligram of protein (mU/mg protein). The significant enrichment of enzymatic activity in the PSD fraction confirms the functional presence of Gst isoforms at the postsynaptic scaffold. Significant differences from control levels (*P < 0.05; **P < 0.01) were determined by one-way ANOVA with Tukey’s post hoc test. (D) Representative immunoblot analysis of Aurora-A immunoprecipitates (IP) from the indicated fractions, demonstrating the physical association and modification status of the kinase. (E) Quantification of S-glutathionylated and pT288 Aurora-A levels. Values were normalized to total Aurora-A and expressed relative to levels in total brain lysates (mean ± SEM, n = 5). Significant differences from control levels (**P < 0.01; ***P < 0.001; ****P < 0.0001) were determined by one-way ANOVA followed by Tukey’s multiple comparisons test. Source data are available for this figure: SourceData F4.

Co-enrichment of Aurora-A and Gstp at the PSD in the mouse brain . (A) Re...

in Redox-dependent S-glutathionylation of Aurora-A kinase by Gstp promotes postsynaptic maturation > Journal of Cell Biology
Published: 12 June 2026
Figure 4. Co-enrichment of Aurora-A and Gstp at the PSD in the mouse brain . (A) Representative immunoblots of biochemical fractions prepared from P14 murine brain lysates. Whole-brain lysate, synaptosome, and detergent-extracted PSD fractions More about this image found in Co-enrichment of Aurora-A and Gstp at the PSD in the mouse brain . (A) Re...
Images
C290 glutathionylation potentiates Aurora-A kinase activity. (A–C) In vitro glutathionylation promotes T288 autophosphorylation and enhances the kinase activity of WT Aurora-A, but not of the C290A mutant. Purified recombinant HA-tagged WT or C290A mutant Aurora-A proteins were subjected to in vitro glutathionylation with oxidized glutathione (GSSG, 10 mM) for 30 min. (A) Immunoblot analysis under nonreducing conditions confirms glutathionylation of WT Aurora-A. Robust T288 autophosphorylation is observed in the presence of GSSG. Total protein loading was confirmed by immunoblotting for total Aurora-A. Glutathione induces dimerization and subsequent autophosphorylation of WT Aurora-A in vitro. Open triangle indicates the dimeric form of Aurora-A detected under nonreducing conditions. (B) Quantification of dimerized, glutathionylated, and pT288 Aurora-A protein levels, normalized to total Aurora-A, and expressed relative to the untreated control (without GSSG) (mean ± SEM, n = 5). Significant differences from the control (****P < 0.0001) were determined by one-way ANOVA followed by Tukey’s multiple comparisons test. IP, immunoprecipitation. (C) Kinase activity of glutathionylated proteins was assessed by a luminescence-based ADP assay. Glutathionylation significantly enhances the kinase activity of WT Aurora-A, whereas the glutathionylation-resistant C290A mutant shows no response. Notably, in the absence of GSSG, the basal kinase activity of the C290A mutant is comparable with that of WT Aurora-A, indicating that the C290A mutation specifically abolishes the redox-responsive “gear-up” without affecting intrinsic catalytic activity. Data are presented as mean ± SEM (n = 5). Statistical significance was assessed using two-way ANOVA (factors: genotype and treatment), followed by Sidak’s multiple comparisons test (*P < 0.05; **P < 0.01). Source data are available for this figure: SourceData F5.

C290 glutathionylation potentiates Aurora-A kinase activity. (A–C) In vitr...

in Redox-dependent S-glutathionylation of Aurora-A kinase by Gstp promotes postsynaptic maturation > Journal of Cell Biology
Published: 12 June 2026
Figure 5. C290 glutathionylation potentiates Aurora-A kinase activity. (A–C) In vitro glutathionylation promotes T288 autophosphorylation and enhances the kinase activity of WT Aurora-A, but not of the C290A mutant. Purified recombinant More about this image found in C290 glutathionylation potentiates Aurora-A kinase activity. (A–C) In vitr...
Images
Redox-mediated potentiation of Aurora-A at C290 is required for Aurora-A to reach the full functional threshold for synapse assembly. Cortical neurons from murine E14 embryos were cultured and infected with adenovirus vectors expressing the indicated molecules after 5 days. (A and B) Gain-of-function analysis under overexpression conditions. (A) Representative immunoblots for the expression of the indicated molecules. β-Actin serves as a loading control. (B) Quantification of Erk phosphorylation (phospho-Erk/total Erk) and synaptic markers (synapsin I, synaptophysin, PSD95, and GluA1). All values are normalized to β-actin and relative to mock-transfected controls (mean ± SEM, n = 5). Statistical significance (*P < 0.05; **P < 0.01; ***P < 0.001; ****P < 0.0001; n.s., not significant, P > 0.05) was determined separately for each dataset using one-way ANOVA followed by Tukey’s multiple comparisons test. Pairwise comparisons among all indicated conditions were performed, and key comparisons relevant to the mechanistic interpretation (e.g., WT vs C290A) are shown. (C and D) Stoichiometry-dependent masking of the C290A deficit. (C) Representative photomicrographs of cultured cortical neurons (DIV14–16) immunostained for PSD95 (green) and synapsin I (red). Colocalization panels highlight double-positive puncta (bottom panels; black) identified as synapses (see Fig. S4, A and B). Scale bar, 10 μm. (D) Quantification of synapse density (synapse numbers per unit dendrite length). Statistical significance (*P < 0.05; ****P < 0.0001) was determined separately for each dataset using one-way ANOVA followed by Tukey’s multiple comparisons test. Pairwise comparisons among all indicated conditions were performed, and key comparisons relevant to the mechanistic interpretation are shown. Notably, the synaptogenic effect of the C290A mutant was significantly weaker than that of WT Aurora-A, although partial activity remained detectable under overexpression conditions. (E–H) Rescue of synapse formation defects in Aurora-A–depleted neurons. Endogenous Aurora-A was depleted using targeted shRNAs, and the neurons were then rescued with the indicated shRNA-resistant Aurora-A variants. (E) Representative immunoblots of the rescue experiments where endogenous Aurora-A was depleted by shRNA and replaced with the indicated variants. β-Actin serves as a loading control. (F) Densitometric quantification of the rescue efficiency. The analysis confirms that endogenous Aurora-A is effectively silenced and replaced by exogenous variants at near-physiological levels (∼1:1 stoichiometry), providing a sensitive platform to evaluate the C290 switch without the confounding effects of mass action. Significant differences from the control (*P < 0.05; **P < 0.01; ***P < 0.001; ****P < 0.0001) were determined by one-way ANOVA followed by Tukey’s multiple comparisons test. (G) Representative images of Aurora-A–depleted neurons rescued with the indicated variants. Merged panels show PSD95 (green) and synapsin I (red) colocalization; black masks in the bottom panels represent identified synaptic puncta. Scale bar, 10 μm. (H) Quantification of synapse density. In contrast to the full rescue observed with WT and T288D, the C290A mutant fails to sustain the robust synaptogenic program required for full maturation, acting as a functional hypomorph under physiological conditions. Significant differences (*P < 0.05; **P < 0.01) were determined by one-way ANOVA with Tukey’s post hoc test. Source data are available for this figure: SourceData F6.

Redox-mediated potentiation of Aurora-A at C290 is required for Aurora-A to...

in Redox-dependent S-glutathionylation of Aurora-A kinase by Gstp promotes postsynaptic maturation > Journal of Cell Biology
Published: 12 June 2026
Figure 6. Redox-mediated potentiation of Aurora-A at C290 is required for Aurora-A to reach the full functional threshold for synapse assembly. Cortical neurons from murine E14 embryos were cultured and infected with adenovirus vectors More about this image found in Redox-mediated potentiation of Aurora-A at C290 is required for Aurora-A to...
Images
Constitutively active Aurora-A rescues synaptogenesis defects caused by Gstp knockdown. Aurora-A T288D restores synaptic marker expression in Gstp-deficient neurons. (A) Representative immunoblots of the indicated proteins. Cortical neurons were co-transfected with shRNAs targeting Gstp1/2 and the HA-tagged Aurora-A T288D mutant. Gstp knockdown, T288D mutant expression, phosphorylated ERK, and various synaptic markers were analyzed. β-Actin serves as a loading control. (B) Quantification of ERK phosphorylation (phospho-ERK/total ERK), presynaptic markers synapsin I and synaptophysin, and postsynaptic markers PSD95 and GluA1. All values are normalized to β-actin and relative to mock-transfected controls (mean ± SEM, n = 3). Significant differences from the control (*P < 0.05; **P < 0.01; ***P < 0.001; ****P < 0.0001; n.s., not significant, P > 0.05) were determined by one-way ANOVA followed by Tukey’s multiple comparisons test. (C and D) The Aurora-A T288D mutant compensates for the loss of Gstp in synapse formation. Representative images (C) of cortical neurons (DIV14–16) expressing Gstp1/2 shRNAs and the Aurora-A T288D mutant, double-immunostained for PSD95 and synapsin I. Colocalization panels show synaptic puncta (bottom panels; black) as double-positive signals (see Fig. S4, A and B). Scale bar, 10 μm. Quantification shows the number of synapses per unit dendritic length in D. Significant differences (**P <0.01; n.s., not significant, P > 0.05) were determined by one-way ANOVA with Tukey’s post hoc test for all possible pairs, including the comparison between shControl and shGstp + T288D. Note that the reduction in synapse formation induced by Gstp knockdown is significantly rescued by expression of the Aurora-A T288D mutant, returning to levels comparable with those of the control (P > 0.05, shControl vs shGstp + T288D). Source data are available for this figure: SourceData F7.

Constitutively active Aurora-A rescues synaptogenesis defects caused by ...

in Redox-dependent S-glutathionylation of Aurora-A kinase by Gstp promotes postsynaptic maturation > Journal of Cell Biology
Published: 12 June 2026
Figure 7. Constitutively active Aurora-A rescues synaptogenesis defects caused by Gstp knockdown. Aurora-A T288D restores synaptic marker expression in Gstp-deficient neurons. (A) Representative immunoblots of the indicated proteins. Cortical More about this image found in Constitutively active Aurora-A rescues synaptogenesis defects caused by ...
Images
Human GSTP1 enhances synaptogenesis via Aurora-A activation. Overexpression of hGSTP1 promotes synaptic marker expression. (A) Representative immunoblots of the indicated proteins. Cortical neurons were co-electroporated with plasmids expressing HA-tagged Aurora-A C290A mutant and Myc-tagged hGSTP1. Expression of hGSTP1 and the T288D mutant, as well as levels of phosphorylated ERK and various synaptic markers, were analyzed. β-Actin serves as a loading control. (B) Quantification of ERK phosphorylation (phospho-ERK/total ERK), presynaptic markers synapsin I and synaptophysin, and postsynaptic markers PSD95 and GluA1. All values are normalized to β-actin and relative to mock-transfected controls without GSTP1 expression (mean ± SEM, n = 3). Significant differences from the control (*P < 0.05; **P < 0.01; ****P < 0.0001; n.s., not significant, P > 0.05) were determined by one-way ANOVA followed by Tukey’s multiple comparisons test. (C and D) Expression of hGSTP1 upregulates synapse formation. Representative images (C) of cortical neurons (DIV14–16) electroporated with HA-tagged Aurora-A C290A mutant and Myc-tagged hGSTP1, double-immunostained for PSD95 and synapsin I. Colocalization panels show synaptic puncta (bottom panels; black) as double-positive signals (see Fig. S4, A and B). Scale bar, 10 μm. Quantification shows the number of synapses per unit dendritic length in D. Significant differences (*P < 0.05; **P < 0.01; n.s., not significant, P > 0.05) were determined by one-way ANOVA followed by Tukey’s post hoc test for all pairwise comparisons, including those between mock-transfected controls, GSTP1 alone, Aurora-A C290A alone, and the combination of GSTP1 and Aurora-A C290A. Note that while the Aurora-A C290A mutant itself promotes synapse formation, this effect is not further augmented by co-expression of GSTP1 (P > 0.05, Aurora-A C290A vs Aurora-A C290A + GSTP1). Source data are available for this figure: SourceData F8.

Human GSTP1 enhances synaptogenesis via Aurora-A activatio...

in Redox-dependent S-glutathionylation of Aurora-A kinase by Gstp promotes postsynaptic maturation > Journal of Cell Biology
Published: 12 June 2026
Figure 8. Human GSTP1 enhances synaptogenesis via Aurora-A activation. Overexpression of hGSTP1 promotes synaptic marker expression. (A) Representative immunoblots of the indicated proteins. Cortical neurons were co-electroporated with More about this image found in Human GSTP1 enhances synaptogenesis via Aurora-A activatio...
Images
Redox-dependent regulation of Aurora-A glutathionylation and synaptogenesis. Impact of redox reagents on synaptic marker expression. (A) Representative immunoblots for the indicated proteins, confirming the effects of the oxidant H2O2, the general antioxidant N-acetylcysteine (NAC), and the mitochondria-targeted antioxidant mito-TEMPO. β-Actin serves as a loading control. (B) Quantification of ERK phosphorylation (phospho-ERK/total ERK), presynaptic markers synapsin I and synaptophysin, and postsynaptic markers PSD95 and GluA1. All values are normalized to β-actin and relative to mock-treated controls (mean ± SEM, n = 3). Significant differences from the control (*P < 0.05; **P < 0.01; ****P < 0.0001) were determined by one-way ANOVA followed by Tukey’s multiple comparisons test. (C and D) ROS-induced Aurora-A glutathionylation and activation. (C) Representative immunoblot analysis of Aurora-A immunoprecipitates. (D) Quantification of glutathionylated and pT288 Aurora-A levels, normalized to total Aurora-A and relative to control levels (mean ± SEM, n = 3). Significant differences from the control (*P < 0.05; ***P < 0.001; ****P < 0.0001; n.s., not significant, P > 0.05) were determined by one-way ANOVA followed by Tukey’s multiple comparisons test. (E and F) Synaptogenesis is regulated by non-mitochondrial ROS. Representative images (E) of cortical neurons (DIV14–16) treated with the indicated drugs and double-immunostained for PSD95 and synapsin I. Colocalization panels show synaptic puncta (bottom panels; black) as double-positive signals (see Fig. S4, A and B). Scale bar, 10 μm. Quantification shows the number of synapses per unit dendritic length in F. Significant differences (**P < 0.01; n.s., not significant, P > 0.05) were determined by one-way ANOVA with Tukey’s post hoc test. Notably, while the oxidant H2O2 promotes synapse formation and the general antioxidant NAC inhibits it, the mitochondrial-specific scavenger mito-TEMPO has no significant effect, indicating that ROS from sources other than mitochondria regulate this process. Source data are available for this figure: SourceData F9.

Redox-dependent regulation of Aurora-A glutathionylation and synaptogenesis...

in Redox-dependent S-glutathionylation of Aurora-A kinase by Gstp promotes postsynaptic maturation > Journal of Cell Biology
Published: 12 June 2026
Figure 9. Redox-dependent regulation of Aurora-A glutathionylation and synaptogenesis. Impact of redox reagents on synaptic marker expression. (A) Representative immunoblots for the indicated proteins, confirming the effects of the oxidant H2O More about this image found in Redox-dependent regulation of Aurora-A glutathionylation and synaptogenesis...
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Gstp acts as a kinetic facilitator to ensure efficient redox-dependent Aurora-A activation. (A and B) H2O2 treatment partially restores synaptic marker expression in Gstp-deficient neurons. (A) Representative immunoblots for the indicated proteins. Cortical neurons were transfected with shRNAs targeting Gstp1/2. Gstp knockdown, phosphorylated ERK, and various synaptic markers, were analyzed. β-Actin serves as a loading control. (B) Quantification of ERK phosphorylation (phospho-ERK/total ERK), presynaptic markers synapsin I and synaptophysin, and postsynaptic markers PSD95 and GluA1. All values are normalized to β-actin and relative to mock-transfected controls (mean ± SEM, n = 3). Significant differences from the control (*P < 0.05; **P < 0.01; ***P < 0.001; n.s., not significant, P > 0.05) were determined by one-way ANOVA followed by Tukey’s multiple comparisons test. (C) Representative immunoblot analysis of Aurora-A immunoprecipitates (IP) from the indicated fractions, demonstrating the physical association and modification status of the kinase. (D) Quantification of S-glutathionylated and pT288 Aurora-A levels. Values were normalized to total Aurora-A and expressed relative to the control levels (mean ± SEM, n = 5). Significant differences from control levels (****P < 0.0001; n.s., not significant, P > 0.05) were determined by one-way ANOVA followed by Tukey’s multiple comparisons test. (E and F) H2O2 treatment effectively compensates for the loss of Gstp in synapse formation. Representative images of cortical neurons (DIV14–16) expressing Gstp1/2 shRNAs and double-immunostained for PSD95 and synapsin I. Colocalization panels (bottom panels; black) display double-positive signals (see Fig. S4, A and B). Scale bar, 10 μm. Quantification shows the number of synapses per 10 µm of dendritic length. Significant differences (**P < 0.01; ****P < 0.0001; n.s., not significant, P > 0.05) were determined by one-way ANOVA with Tukey’s post hoc test. Notably, the reduction in synapse formation induced by Gstp knockdown was significantly rescued by H2O2 treatment, returning to levels comparable with those of the control (P > 0.05, shControl vs shGstp + H2O2). This result demonstrates that while nonenzymatic glutathionylation can occur under elevated oxidative conditions, Gstp is required as the essential catalytic facilitator to ensure efficient Aurora-A activation under physiological redox environments. (G) Working model for Gstp-mediated kinetic modulation of postsynaptic maturation. (Upper) Gstp functions as a catalytic regulator by lowering the activation energy barrier (Ea) for site-specific glutathionylation of Aurora-A at C290. This enzymatic catalysis ensures that physiological ROS levels are sufficient to transition the kinase from an inactive state to a primed state. (Lower) In this kinetic regulatory process, Gstp acts as a signal integrator, converting stochastic redox fluctuations into a discrete, committed signal at C290 of Aurora-A. This site-specific modification represents a kinetic priming event, a mechanistic prerequisite for subsequent dimerization and autophosphorylation at T288. Only after this sequential signaling hierarchy of priming and catalytic activation does Aurora-A achieve full catalytic activity to drive the downstream Aurora-A–Mvp–ERK signaling axis, ultimately orchestrating the localized translation of synaptic proteins required for synaptogenesis. Source data are available for this figure: SourceData F10.

Gstp acts as a kinetic facilitator to ensure efficient redox-dependent Auro...

in Redox-dependent S-glutathionylation of Aurora-A kinase by Gstp promotes postsynaptic maturation > Journal of Cell Biology
Published: 12 June 2026
Figure 10. Gstp acts as a kinetic facilitator to ensure efficient redox-dependent Aurora-A activation. ( A and B) H2O2 treatment partially restores synaptic marker expression in Gstp-deficient neurons. (A) Representative immunoblots for the More about this image found in Gstp acts as a kinetic facilitator to ensure efficient redox-dependent Auro...
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A multi-panel image depicts macrophage energy metabolism analysis.

Met-Vision, an imaging-based automated pipeline to profile energy metabolis...

in Met-Vision reveals coexisting energetic states in tissue macrophages redistributed by inflammation > Journal of Cell Biology
Published: 12 June 2026
Figure 1. Met-Vision, an imaging-based automated pipeline to profile energy metabolism at the single-cell level. (A) Principle for Met-Vision analyses. Macrophages isolated from SPICY mice expressing the PercevalHR fluorescent reporter for More about this image found in Met-Vision, an imaging-based automated pipeline to profile energy metabolis...
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A two-part image depicts macrophage energy metabolism profiles.

Met-Vision identifies and classifies distinct energy metabolism profiles in...

in Met-Vision reveals coexisting energetic states in tissue macrophages redistributed by inflammation > Journal of Cell Biology
Published: 12 June 2026
Figure 2. Met-Vision identifies and classifies distinct energy metabolism profiles in macrophages. (A) Scheme illustrating the main steps to establish a classifier for macrophage energy metabolic profiles. The dataset (n = 879 macrophages) More about this image found in Met-Vision identifies and classifies distinct energy metabolism profiles in...
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A multi-part image depicts macrophage metabolic profiles under different conditions.

Distinct macrophage metabolic profiles coexist at steady state and are reco...

in Met-Vision reveals coexisting energetic states in tissue macrophages redistributed by inflammation > Journal of Cell Biology
Published: 12 June 2026
Figure 3. Distinct macrophage metabolic profiles coexist at steady state and are reconfigured upon inflammation. (A and B) Distribution of the four metabolic profiles (Ox-high, Ox-med, Ox-low, and Ox-null) in (A) BMDMs treated or not with More about this image found in Distinct macrophage metabolic profiles coexist at steady state and are reco...

in Met-Vision reveals coexisting energetic states in tissue macrophages redistributed by inflammation > Journal of Cell Biology
Published: 12 June 2026
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