期刊
EMBO JOURNAL
卷 34, 期 6, 页码 811-827出版社
WILEY
DOI: 10.15252/embj.201489032
关键词
COPII vesicle transport; intrinsic disorder; secretion; single particle electron microscopy
资金
- NIH [GM088151, GM086892]
- NSF [MCB1157824]
- American Cancer Society [123268-RSG-12-139-01-CSM]
- UW-Madison [BIR-9512577, S10 RR13790]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1157824] Funding Source: National Science Foundation
In mammalian cells, cargo-laden secretory vesicles leave the endoplasmic reticulum (ER) en route to ER-Golgi intermediate compartments (ERGIC) in a manner dependent on the COPII coat complex. We report here that COPII-coated transport carriers traverse a submicron, TFG (Trk-fused gene)-enriched zone at the ER/ERGIC interface. The architecture of TFG complexes as determined by three-dimensional electron microscopy reveals the formation of flexible, octameric cup-like structures, which are able to self-associate to generate larger polymers in vitro. In cells, loss of TFG function dramatically slows protein export from the ER and results in the accumulation of COPII-coated carriers throughout the cytoplasm. Additionally, the tight association between ER and ERGIC membranes is lost in the absence of TFG. We propose that TFG functions at the ER/ERGIC interface to locally concentrate COPII-coated transport carriers and link exit sites on the ER to ERGIC membranes. Our findings provide a new mechanism by which COPII-coated carriers are retained near their site of formation to facilitate rapid fusion with neighboring ERGIC membranes upon uncoating, thereby promoting interorganellar cargo transport.
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