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In Focus

Two studies investigate how cells regulate the formation of autophagosomes.

People & Ideas

Hetzer investigates how the nuclear envelope and nuclear pores organize chromatin and regulate gene expression.



Cyclin A outcompetes inhibitory spindle assembly checkpoint proteins for binding to the APC/C ubiquitin ligase coactivator Cdc20 to promote its self-destruction even when the checkpoint is active (see also a paper from van Zon et al., in this issue).

Generation of PI3P in the normally PI3P-deficient ER membrane makes the organelle a platform for autophagosome formation.

Blocking autophagy protects the apoptosis inhibitor dBruce from destruction and promotes nurse cell survival in developing egg chambers.

PKA puts the brakes on autophagy by inhibiting LC3 recruitment to autophagosomes.

A screen for GFP-tagged yeast proteins that can assemble into visible structures reveals four new filamentous structures in the cytoplasm formed by metabolic enzymes and translation factors.

A biosensor for the RhoA GTPase illustrates its activation patterns in both the front and rear of migrating lymphocytes.

G protein–coupled receptors rely on the PDZ domain of SNX27 for endosomal recycling.


ERK8 prevents genome instability by blocking the association of the HDM2 E3 ubiquitin ligase with the genome-protecting protein PCNA.

Prior associations with the APC/C complex during prometaphase makes cyclin B1 a better substrate for the cell cycle–regulating ubiquitin ligase in metaphase (see also a related paper by Di Fiore et al. in this issue).

Passage of transcribed U snRNA precursors through Cajal bodies ensures that they are properly bound to the PHAX adaptor protein required for nuclear exit.

CryoET shows the configuration of the ephemeral translationally inactive 100S ribosomal dimer.

Phospholipid binding leads to accelerated assembly of the bacterial SRP receptor FtsY and SRP, allowing cargo proteins to be delivered to target membranes more efficiently.

The ubiquitin-like protein BAG-6 protects cells from newly synthesized misfolded proteins by tethering them to the proteasome.

p107, a member of the retinoblastoma susceptibility protein family, influences lipid metabolism in muscle and other tissues by repressing the PPAR-γ co-factor PGC-1α.

The activity of Rho GTPases in migrating cells is regulated by binding of myosin II to GEFs.

Quantitative ultrastructural analysis and proteomics detail CLIC structure, composition, and function.

In response to tissue stiffening, fibroblasts increase production of extracellular matrix while decreasing production of matrix-degrading enzymes and the fibrosis inhibitor prostaglandin E2.

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