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

Research output: Contribution to journalJournal articleResearchpeer-review

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A G protein-coupled receptor-like module regulates cellulose synthase secretion from the endomembrane system in Arabidopsis. / McFarlane, Heather E.; Mutwil-Anderwald, Daniela; Verbančič, Jana; Picard, Kelsey L.; Gookin, Timothy E.; Froehlich, Anja; Chakravorty, David; Trindade, Luisa M.; Alonso, Jose M.; Assmann, Sarah M.; Persson, Staffan.

In: Developmental Cell, Vol. 56, No. 10, 2021, p. 1484-1497.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

McFarlane, HE, Mutwil-Anderwald, D, Verbančič, J, Picard, KL, Gookin, TE, Froehlich, A, Chakravorty, D, Trindade, LM, Alonso, JM, Assmann, SM & Persson, S 2021, 'A G protein-coupled receptor-like module regulates cellulose synthase secretion from the endomembrane system in Arabidopsis', Developmental Cell, vol. 56, no. 10, pp. 1484-1497. https://doi.org/10.1016/j.devcel.2021.03.031

APA

McFarlane, H. E., Mutwil-Anderwald, D., Verbančič, J., Picard, K. L., Gookin, T. E., Froehlich, A., Chakravorty, D., Trindade, L. M., Alonso, J. M., Assmann, S. M., & Persson, S. (2021). A G protein-coupled receptor-like module regulates cellulose synthase secretion from the endomembrane system in Arabidopsis. Developmental Cell, 56(10), 1484-1497. https://doi.org/10.1016/j.devcel.2021.03.031

Vancouver

McFarlane HE, Mutwil-Anderwald D, Verbančič J, Picard KL, Gookin TE, Froehlich A et al. A G protein-coupled receptor-like module regulates cellulose synthase secretion from the endomembrane system in Arabidopsis. Developmental Cell. 2021;56(10):1484-1497. https://doi.org/10.1016/j.devcel.2021.03.031

Author

McFarlane, Heather E. ; Mutwil-Anderwald, Daniela ; Verbančič, Jana ; Picard, Kelsey L. ; Gookin, Timothy E. ; Froehlich, Anja ; Chakravorty, David ; Trindade, Luisa M. ; Alonso, Jose M. ; Assmann, Sarah M. ; Persson, Staffan. / A G protein-coupled receptor-like module regulates cellulose synthase secretion from the endomembrane system in Arabidopsis. In: Developmental Cell. 2021 ; Vol. 56, No. 10. pp. 1484-1497.

Bibtex

@article{8649a45359cd4fd8b92211b6cb1e1c8d,
title = "A G protein-coupled receptor-like module regulates cellulose synthase secretion from the endomembrane system in Arabidopsis",
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.",
keywords = "cell wall signaling, cellulose, cellulose synthesis, G protein-coupled receptor, GPCR, plant cell biology, plant cell walls, secretion",
author = "McFarlane, {Heather E.} and Daniela Mutwil-Anderwald and Jana Verban{\v c}i{\v c} and Picard, {Kelsey L.} and Gookin, {Timothy E.} and Anja Froehlich and David Chakravorty and Trindade, {Luisa M.} and Alonso, {Jose M.} and Assmann, {Sarah M.} and Staffan Persson",
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: {\textcopyright} 2021 Elsevier Inc.",
year = "2021",
doi = "10.1016/j.devcel.2021.03.031",
language = "English",
volume = "56",
pages = "1484--1497",
journal = "Developmental Cell",
issn = "1534-5807",
publisher = "Cell Press",
number = "10",

}

RIS

TY - JOUR

T1 - A G protein-coupled receptor-like module regulates cellulose synthase secretion from the endomembrane system in Arabidopsis

AU - McFarlane, Heather E.

AU - Mutwil-Anderwald, Daniela

AU - Verbančič, Jana

AU - Picard, Kelsey L.

AU - Gookin, Timothy E.

AU - Froehlich, Anja

AU - Chakravorty, David

AU - Trindade, Luisa M.

AU - Alonso, Jose M.

AU - Assmann, Sarah M.

AU - Persson, Staffan

N1 - 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.

PY - 2021

Y1 - 2021

N2 - 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.

AB - 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.

KW - cell wall signaling

KW - cellulose

KW - cellulose synthesis

KW - G protein-coupled receptor

KW - GPCR

KW - plant cell biology

KW - plant cell walls

KW - secretion

U2 - 10.1016/j.devcel.2021.03.031

DO - 10.1016/j.devcel.2021.03.031

M3 - Journal article

C2 - 33878345

AN - SCOPUS:85105576123

VL - 56

SP - 1484

EP - 1497

JO - Developmental Cell

JF - Developmental Cell

SN - 1534-5807

IS - 10

ER -

ID: 271612007