UMMS Affiliation

Program in Gene Function and Expression

Date

7-7-2014

Document Type

Article

Disciplines

Biochemistry | Cell Biology | Genetics and Genomics

Abstract

The coat protein II (COPII)-coated vesicular system transports newly synthesized secretory and membrane proteins from the endoplasmic reticulum (ER) to the Golgi complex. Recruitment of cargo into COPII vesicles requires an interaction of COPII proteins either with the cargo molecules directly or with cargo receptors for anterograde trafficking. We show that cytosolic phosphatidic acid phospholipase A1 (PAPLA1) interacts with COPII protein family members and is required for the transport of Rh1 (rhodopsin 1), an N-glycosylated G protein-coupled receptor (GPCR), from the ER to the Golgi complex. In papla1 mutants, in the absence of transport to the Golgi, Rh1 is aberrantly glycosylated and is mislocalized. These defects lead to decreased levels of the protein and decreased sensitivity of the photoreceptors to light. Several GPCRs, including other rhodopsins and Bride of sevenless, are similarly affected. Our findings show that a cytosolic protein is necessary for transit of selective transmembrane receptor cargo by the COPII coat for anterograde trafficking.

Rights and Permissions

Citation: Kunduri G, Yuan C, Parthibane V, Nyswaner KM, Kanwar R, Nagashima K, Britt SG, Mehta N, Kotu V, Porterfield M, Tiemeyer M, Dolph PJ, Acharya U, Acharya JK. Phosphatidic acid phospholipase A1 mediates ER-Golgi transit of a family of G protein-coupled receptors. J Cell Biol. 2014 Jul 7;206(1):79-95. doi:10.1083/jcb.201405020. Link to article on publisher's site

Comments

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

Related Resources

Link to Article in PubMed

 
 

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