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|Title:||p125A exists as part of the mammalian Sec13/Sec31 COPII subcomplex to facilitate ER-Golgi transport||Authors:||Ong, Y.S.
|Issue Date:||9-Aug-2010||Citation:||Ong, Y.S., Tang, B.L., Loo, L.S., Hong, W. (2010-08-09). p125A exists as part of the mammalian Sec13/Sec31 COPII subcomplex to facilitate ER-Golgi transport. Journal of Cell Biology 190 (3) : 331-345. ScholarBank@NUS Repository. https://doi.org/10.1083/jcb.201003005||Abstract:||Coat protein II (COPII)-mediated export from the endoplasmic reticulum (ER) involves sequential recruitment of COPII complex components, including the Sar1 GTPase, the Sec23/Sec24 subcomplex, and the Sec13/Sec31 subcomplex. p125A was originally identified as a Sec23A-interacting protein. Here we demonstrate that p125A also interacts with the C-terminal region of Sec31A. The Sec31A-interacting domain of p125A is between residues 260-600, and is therefore a distinct domain from that required for interaction with Sec23A. Gel filtration and immunodepletion studies suggest that the majority of cytosolic p125A exists as a ternary complex with the Sec13/Sec31A subcomplex, suggesting that Sec 13, Sec31A, and p125A exist in the cytosol primarily as preassembled Sec13/Sec31A/ p125A heterohexamers. Golgi morphology and protein export from the ER were affected in p125A-silenced cells. Our results suggest that p125A is part of the Sec13/ Sec31A subcomplex and facilitates ER export in mammalian cells. © 2010 Ong et al.||Source Title:||Journal of Cell Biology||URI:||http://scholarbank.nus.edu.sg/handle/10635/108484||ISSN:||00219525||DOI:||10.1083/jcb.201003005|
|Appears in Collections:||Staff Publications|
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