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Cargo crowding contributes to sorting stringency in COPII vesicles
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DOI：10.1083/jcb.201806038.png)
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摘要
En 中文
Accurate maintenance of organelle identity in the secretory pathway relies on retention and retrieval of resident proteins. In the endoplasmic reticulum (ER), secretory proteins are packaged into COPII vesicles that largely exclude ER residents and misfolded proteins by mechanisms that remain unresolved. Here we combined biochemistry and genetics with correlative light and electron microscopy (CLEM) to explore how selectivity is achieved. Our data suggest that vesicle occupancy contributes to ER retention: in the absence of abundant cargo, nonspecific bulk flow increases. We demonstrate that ER leakage is influenced by vesicle size and cargo occupancy: overexpressing an inert cargo protein or reducing vesicle size restores sorting stringency. We propose that cargo recruitment into vesicles creates a crowded lumen that drives selectivity. Retention of ER residents thus derives in part from the biophysical process of cargo enrichment into a constrained spherical membrane-bound carrier.
Keyword:
ENDOPLASMIC-RETICULUM STRESS
PLASMA-MEMBRANE ATPASE
ER EXIT SITES
PROTEIN-TRANSPORT
COAT PROTEINS
P24 PROTEINS
BULK FLOW
SEC24P
EXPORT
ORGANIZATION
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期刊
IF:
6.4
论文数:
1.2W
被引数:
5.7W
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Adaptation of endoplasmic reticulum exit sites to acute and chronic increases in cargo load.png)
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