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

Abstract:

: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.

journal_name

Dev Cell

journal_title

Developmental cell

authors

Asensio CS,Sirkis DW,Maas JW Jr,Egami K,To TL,Brodsky FM,Shu X,Cheng Y,Edwards RH

doi

10.1016/j.devcel.2013.10.007

subject

Has Abstract

pub_date

2013-11-25 00:00:00

pages

425-37

issue

4

eissn

1534-5807

issn

1878-1551

pii

S1534-5807(13)00604-7

journal_volume

27

pub_type

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