Journal
SCIENCE
Volume 353, Issue 6295, Pages 166-169Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aaf4009
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Funding
- Biotechnology and Biological Sciences Research Council [BB/H012923/1, BB/M004031/1, BB/M024911/1]
- Gatsby Charitable Foundation
- BBSRC [BB/M024911/1, BB/M004031/1, BB/H012923/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/M004031/1, BB/M024911/1, BB/H012923/1, BB/C511064/1] Funding Source: researchfish
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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 CTcysteines 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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