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Updated: Mar 18, 2026

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture
Published on: April 10, 2020
S-Acylation of the cellulose synthase complex is essential for its plasma membrane localization
Manoj Kumar1, Raymond Wightman2, Ivan Atanassov1
1Faculty of Life Sciences, The University of Manchester, Michael Smith Building, The Michael Smith Building; Oxford Road, Manchester M13 9PT, UK.
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.
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