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In early C. elegans embryos, the kinetochore-localized BUB- 1/BUB-3 complex promotes anaphase onset independently of its roles in spindle checkpoint signaling and chromosome alignment.
Bub3 and its kinetochore localization are required for the normal timing of anaphase onset and for normal binding of APC/C and Cdc20 in S. cerevisiae.
The myonuclear scaffold in Drosophila larval muscles exhibits both elastic features, contributed by the stretching capacity of MSP300/nesprin, and rigidity, provided by a perinuclear network of microtubules stabilized by Shot/spectraplakin and EB1.
Ltc1 is an ER-localized sterol transporter and a component of ER–mitochondria and ER–vacuole contacts
Cytological and biochemical analyses show that Ylr072w, here renamed Lipid transfer at contact site 1 (Ltc1), is a sterol transport protein localized to both ER–mitochondria and ER–vacuole contact sites in partnership with the organelle-specific components Tom70/81 and Vac8, respectively.
Msd1–Wdr8 are delivered by Pkl1 to mitotic spindle pole bodies, where the Msd1–Wdr8–Pkl1 complex anchors the minus ends of spindle microtubules and antagonizes the outward-pushing forces generated by Cut7/kinesin-5 in fission yeast.
Quantitative analyses of melanosome cargo localization and trafficking and of endosomal membrane dynamics in immortalized melanocytes from mouse Hermansky–Pudlak syndrome models show that BLOC-2 functions to specify the delivery of recycling endosomal cargo transport intermediates to maturing melanosomes.
Quantitative single-molecule receptor dimerization assays show dimerization of IFNAR1 and IFNAR2 upon IFN treatment, and reveal the limiting role of IFNAR1 binding affinity in complex assembly and the regulatory role of USP18.
Wnt ligands regulate Tkv expression to constrain Dpp activity in the Drosophila ovarian stem cell niche
Multiple Wnt ligands produced by cap cells regulate the expression of Tkv, which acts as a receptor sink to remove excess cap cell–expressed Dpp and to restrict niche-associated Dpp activity, in escort cells.
Multifocus microscopy combined with precise registration between fluorescently labeled mRNA, nuclear pore complexes, and chromatin reveals that β-actin mRNAs freely access the entire nucleus and most are within 0.5 µm of a nuclear pore.