Coupling of ER exit to microtubules through direct interaction of COPII with dynactin

Watson, Peter Duncan ORCID: https://orcid.org/0000-0003-0250-7852, Forster, Rebecca, Palmer, Krysten J., Pepperkok, Rainer and Stephens, David J. 2004. Coupling of ER exit to microtubules through direct interaction of COPII with dynactin. Nature Cell Biology 7 , pp. 48-55. 10.1038/ncb1206

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Abstract

Transport of proteins from the endoplasmic reticulum (ER) to the Golgi is mediated by the sequential action of two coat complexes: COPII concentrates cargo for secretion at ER export sites, then COPI is subsequently recruited to nascent carriers and retrieves recycling proteins back to the ER. These carriers then move towards the Golgi along microtubules, driven by the dynein/dynactin complexes. Here we show that the Sec23p component of the COPII complex directly interacts with the dynactin complex through the carboxy-terminal cargo-binding domain of p150Glued. Functional assays, including measurements of the rate of recycling of COPII on the ER membrane and quantitative analyses of secretion, indicate that this interaction underlies functional coupling of ER export to microtubules. Together, our data suggest a mechanism by which membranes of the early secretory pathway can be linked to motors and microtubules for subsequent organization and movement to the Golgi apparatus.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Biosciences
Subjects:	Q Science > QH Natural history > QH301 Biology
ISSN:	1465-7392
Last Modified:	17 Oct 2022 08:48
URI:	https://orca.cardiff.ac.uk/id/eprint/1122

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