title: S-Acylation of the cellulose synthase complex is essential for its plasma membrane localization.
abstract: Plant cellulose microfibrils are synthesized by a process that propels the cellulose synthase complex (CSC) through the plane of the plasma membrane. How interactions between membranes and the CSC are regulated is currently unknown. Here, we demonstrate that all catalytic subunits of the CSC, known as cellulose synthase A (CESA) proteins, are S-acylated. Analysis of Arabidopsis CESA7 reveals four cysteines in variable region 2 (VR2) and two cysteines at the carboxy terminus (CT) as S-acylation sites. Mutating both the VR2 and CT cysteines permits CSC assembly and trafficking to the Golgi but prevents localization to the plasma membrane. Estimates suggest that a single CSC contains more than 100 S-acyl groups, which greatly increase the hydrophobic nature of the CSC and likely influence its immediate membrane environment.
authors.affiliation: Faculty of Life Sciences, The University of Manchester, Michael Smith Building, The Michael Smith Building; Oxford Road, Manchester M13 9PT, UK.
authors.forename: Manoj
authors.initials: M
authors.lastname: Kumar
authors.affiliation: Microscopy Core Facility, Sainsbury Laboratory, University of Cambridge, Bateman Street, Cambridge CB2 1LR, UK.
authors.forename: Raymond
authors.initials: R
authors.lastname: Wightman
authors.affiliation: Faculty of Life Sciences, The University of Manchester, Michael Smith Building, The Michael Smith Building; Oxford Road, Manchester M13 9PT, UK.
authors.forename: Ivan
authors.initials: I
authors.lastname: Atanassov
authors.affiliation: Faculty of Life Sciences, The University of Manchester, Michael Smith Building, The Michael Smith Building; Oxford Road, Manchester M13 9PT, UK.
authors.forename: Anjali
authors.initials: A
authors.lastname: Gupta
authors.affiliation: Division of Plant Sciences, School of Life Sciences, University of Dundee, Dow Street, Dundee, DD1 5EH, Scotland, UK. Cell and Molecular Sciences, The James Hutton Institute, Invergowrie, DD2 5DA, Scotland, UK.
authors.forename: Charlotte H
authors.initials: CH
authors.lastname: Hurst
authors.affiliation: Division of Plant Sciences, School of Life Sciences, University of Dundee, Dow Street, Dundee, DD1 5EH, Scotland, UK. Cell and Molecular Sciences, The James Hutton Institute, Invergowrie, DD2 5DA, Scotland, UK. simon.turner@manchester.ac.uk p.a.hemsley@dundee.ac.uk.
authors.forename: Piers A
authors.initials: PA
authors.lastname: Hemsley
authors.affiliation: Faculty of Life Sciences, The University of Manchester, Michael Smith Building, The Michael Smith Building; Oxford Road, Manchester M13 9PT, UK. simon.turner@manchester.ac.uk p.a.hemsley@dundee.ac.uk.
authors.forename: Simon
authors.initials: S
authors.lastname: Turner
mesh_terms: D000215:Acylation; D017360:Arabidopsis / Q000201:enzymology* / Q000235:genetics; D029681:Arabidopsis Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D020134:Catalytic Domain; D002462:Cell Membrane / Q000201:enzymology*; D003545:Cysteine / Q000737:chemistry / Q000235:genetics; D005964:Glucosyltransferases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006056:Golgi Apparatus / Q000201:enzymology; D057927:Hydrophobic and Hydrophilic Interactions; D020894:Microfibrils / Q000378:metabolism; D009154:Mutation
chemical_list: D029681:Arabidopsis Proteins; C120025:IRX3 protein, Arabidopsis; C420969:CESA8 protein, Arabidopsis; D005964:Glucosyltransferases; C457769:PRC1 protein, Arabidopsis; D003545:Cysteine