期刊
DEVELOPMENTAL CELL
卷 56, 期 10, 页码 1484-+出版社
CELL PRESS
DOI: 10.1016/j.devcel.2021.03.031
关键词
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资金
- Australian Research Council (ARC) [DP19001941]
- Novo Nordisk Laureate [NNF19OC0056076]
- EMBO-LTF [1246-2013]
- Natrual Sciences and Engineering Council (NSERC) PDF [454454-2014]
- ARC Discovery Early Career Researcher award [DE170100054]
- NSF [IOS1444561]
- Deutsche orschungsgemeinschaft
- U.S. National Science Foundation [MCB-1121612, MCB-1715826]
- National Institute of GeneralMedical Sciences of the NIH [R01GM126079]
- Australian Research Council [DE170100054] Funding Source: Australian Research Council
The study investigated the importance of a family of proteins containing seven transmembrane domains in cellulose synthesis during cell wall integrity stress, revealing their interaction with G protein signaling pathway and their role in regulating CESA trafficking, impacting the response to cell wall integrity stress.
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 Gb gamma 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 Gb gamma 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.
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