TGF clusters COPII-coated transport carriers and promotes early secretory pathway organization
نویسندگان
چکیده
As you will see, the referees find your study interesting. However, they think that the current dataset does not sufficiently support your claims. They point out that additional data and information are needed and that alternative models on TFG functioning should be considered. Furthermore, technical concerns need to be addressed. Given the very constructive comments provided, I would like to invite you to submit a revised version of the manuscript, addressing all concerns of the referees. Please contact me in case of questions regarding the revision of your manuscript.
منابع مشابه
TFG clusters COPII-coated transport carriers and promotes early secretory pathway organization.
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 ...
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What is the first membrane fusion step in the secretory pathway? In mammals, transport vesicles coated with coat complex (COP) II deliver secretory cargo to vesicular tubular clusters (VTCs) that ferry cargo from endoplasmic reticulum exit sites to the Golgi stack. However, the precise origin of VTCs and the membrane fusion step(s) involved have remained experimentally intractable. Here, we doc...
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In eukaryotic cells, intracellular protein transport between the organelles of the secretory pathway is mediated by 50– 80 nm vesicular carriers that are released from a donor organelle and fuse with an appropriate acceptor organelle. The starting point of the secretory route is the endoplasmic reticulum (ER). Once correctly folded and assembled properly in the ER, secretory cargo proteins can ...
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Erv14p is a conserved integral membrane protein that traffics in COPII-coated vesicles and localizes to the early secretory pathway in yeast. Deletion of ERV14 causes a defect in polarized growth because Axl2p, a transmembrane secretory protein, accumulates in the endoplasmic reticulum and is not delivered to its site of function on the cell surface. Herein, we show that Erv14p is required for ...
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تاریخ انتشار 2014