Sec24C/D-isoform-specific sorting of the preassembled ER-Golgi Q-SNARE complex.

Abstract:

:Secretory proteins are exported from the endoplasmic reticulum in COPII vesicles. SNARE proteins-core machinery for membrane fusion-are incorporated into COPII vesicles by direct interaction with Sec24. Here we report a novel mechanism for sorting of the ER-Golgi Q-SNAREs into COPII vesicles. Different mammalian Sec24 isoforms recruit either the R-SNARE Sec22b or the Q-SNAREs Syntaxin5, GS27, and Bet1. Syntaxin5 is the only Q-SNARE that directly interacts with Sec24C, requiring its "open" conformation. Mutation within the IxM cargo-binding site of Sec24C led to a drastic reduction in sorting of all three Q-SNAREs into COPII vesicles, implying their ER export as a preassembled complex. Analysis of immunoisolated COPII vesicles and intracellular localization of Sec24 isoforms indicate that all ER-Golgi SNAREs are present on the same vesicle. Combined with existing data, our findings yield a general concept of how Sec24 isoforms can recruit fusogenic SNARE subunits to keep them functionally apart and thus prime mammalian COPII vesicles for homotypic fusion.

journal_name

Mol Biol Cell

authors

Adolf F,Rhiel M,Reckmann I,Wieland FT

doi

10.1091/mbc.E16-04-0229

subject

Has Abstract

pub_date

2016-09-01 00:00:00

pages

2697-707

issue

17

eissn

1059-1524

issn

1939-4586

pii

mbc.E16-04-0229

journal_volume

27

pub_type

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