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TitleTFG clusters COPII-coated transport carriers and promotes early secretory pathway organization.
Journal, issue, pagesEMBO J, Vol. 34, Issue 6, Page 811-827, Year 2015
Publish dateMar 12, 2015
AuthorsAdam Johnson / Nilakshee Bhattacharya / Michael Hanna / Janice G Pennington / Amber L Schuh / Lei Wang / Marisa S Otegui / Scott M Stagg / Anjon Audhya /
PubMed AbstractIn 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 ...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.
External linksEMBO J / PubMed:25586378 / PubMed Central
MethodsEM (single particle)
Resolution30.0 Å
Structure data

EMDB-6075:
Reconstruction of the N-terminal domain of C. elegans TFG
Method: EM (single particle) / Resolution: 30.0 Å

EMDB-6076:
Reconstruction of the N-terminal domain of human TFG
Method: EM (single particle) / Resolution: 30.0 Å

Source
  • Caenorhabditis elegans (invertebrata)
  • Homo sapiens (human)

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