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Self-assembly of VPS41 promotes sorting required for biogenesis of the regulated secretory pathway.

Authors: Asensio, CS  Sirkis, DW  Maas JW, JR  Egami, K  To, TL  Brodsky, FM  Shu, X  Cheng, Y  Edwards, RH 
Citation: Asensio CS, etal., Dev Cell. 2013 Nov 25;27(4):425-37. doi: 10.1016/j.devcel.2013.10.007. Epub 2013 Nov 7.
Pubmed: (View Article at PubMed) PMID:24210660
DOI: Full-text: DOI:10.1016/j.devcel.2013.10.007

The regulated release of polypeptides has a central role in physiology, behavior, and development, but the mechanisms responsible for production of the large dense core vesicles (LDCVs) capable of regulated release have remained poorly understood. Recent work has implicated cytosolic adaptor protein AP-3 in the recruitment of LDCV membrane proteins that confer regulated release. However, AP-3 in mammals has been considered to function in the endolysosomal pathway and in the biosynthetic pathway only in yeast. We now find that the mammalian homolog of yeast VPS41, a member of the homotypic fusion and vacuole protein sorting (HOPS) complex that delivers biosynthetic cargo to the endocytic pathway in yeast, promotes LDCV formation through a common mechanism with AP-3, indicating a conserved role for these proteins in the biosynthetic pathway. VPS41 also self-assembles into a lattice, suggesting that it acts as a coat protein for AP-3 in formation of the regulated secretory pathway.

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CRRD Object Information
CRRD ID: 10054072
Created: 2015-07-25
Species: All species
Last Modified: 2015-07-25
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.