A G protein-coupled receptor-like module regulates cellulose synthase secretion from the endomembrane system in Arabidopsis

Heather E. McFarlane*, Daniela Mutwil-Anderwald, Jana Verbančič, Kelsey L. Picard, Timothy E. Gookin, Anja Froehlich, David Chakravorty, Luisa M. Trindade, Jose M. Alonso, Sarah M. Assmann, Staffan Persson

*Corresponding author af dette arbejde

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Abstract

Cellulose is produced at the plasma membrane of plant cells by cellulose synthase (CESA) complexes (CSCs). CSCs are assembled in the endomembrane system and then trafficked to the plasma membrane. Because CESAs are only active in the plasma membrane, control of CSC secretion regulates cellulose synthesis. We identified members of a family of seven transmembrane domain-containing proteins (7TMs) that are important for cellulose production during cell wall integrity stress. 7TMs are often associated with guanine nucleotide-binding (G) protein signaling and we found that mutants affecting the Gβγ dimer phenocopied the 7tm mutants. Unexpectedly, the 7TMs localized to the Golgi/trans-Golgi network where they interacted with G protein components. Here, the 7TMs and Gβγ regulated CESA trafficking but did not affect general protein secretion. Our results outline how a G protein-coupled module regulates CESA trafficking and reveal that defects in this process lead to exacerbated responses to cell wall integrity stress.

OriginalsprogEngelsk
TidsskriftDevelopmental Cell
Vol/bind56
Udgave nummer10
Sider (fra-til)1484-1497
Antal sider14
ISSN1534-5807
DOI
StatusUdgivet - 2021

Bibliografisk note

Funding Information:
Live cell imaging was conducted using instruments that are part of the Biological Optical Microscopy Platform (BOMP) at University of Melbourne and electron microscopy was conducted using instruments that are part of the Melbourne Advanced Microscopy Facility. S.P. acknowledges the financial aid of an Australian Research Council (ARC) Discovery grant ( DP19001941 ), Villum Investigator (project ID: 25915), and Novo Nordisk Laureate ( NNF19OC0056076 ) grants. H.E.M. acknowledges an EMBO-LTF ( 1246-2013 ), Natrual Sciences and Engineering Council (NSERC) PDF ( 454454-2014 ), and an ARC Discovery Early Career Researcher award (DE170100054). J.M.A. acknowledges support from NSF grant IOS1444561 , D.M.-A. acknowledges financial support from Deutsche Forschungsgemeinschaft and T.E.G., S.M.A., and D.C. acknowledge support from the U.S. National Science Foundation ( MCB-1121612 , with additional support from MCB-1715826 ) and from the National Institute of General Medical Sciences of the NIH under award number R01GM126079. The content is solely the responsibility of the authors and does not necessarily represent the official views of the NIH.

Publisher Copyright:
© 2021 Elsevier Inc.

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