The TWD40-2 protein and the AP2 complex cooperate in the clathrin-mediated endocytosis of cellulose synthase to regulate cellulose biosynthesis

Cellulose biosynthesis is performed exclusively by plasma membranelocalized cellulose synthases (CESAs). Therefore, the trafficking of CESAs to and from the plasma membrane is an important mechanism for regulating cellulose biosynthesis. CESAs were recently identified as cargo proteins of the classi...

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Published in:Proceedings of the National Academy of Sciences - PNAS 2015-10, Vol.112 (41), p.12870-12875
Main Authors: Bashline, Logan, Li, Shundai, Zhu, Xiaoyu, Gu, Ying
Format: Article
Language:English
Subjects:
Arabidopsis - cytology
Arabidopsis - genetics
Arabidopsis - metabolism
Arabidopsis Proteins - genetics
Arabidopsis Proteins - metabolism
BASIC BIOLOGICAL SCIENCES
Biological Sciences
Biosynthesis
Cellulose
Cellulose - biosynthesis
Cellulose - genetics
cellulose synthase
clathrin
Clathrin - genetics
Clathrin - metabolism
Endocytosis
Endocytosis - physiology
Eukaryotes
Glucosyltransferases - genetics
Glucosyltransferases - metabolism
Membranes
Mutation
plasma membrane
Protein Transport - physiology
Seedlings - cytology
Seedlings - metabolism
trafficking
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Summary:Cellulose biosynthesis is performed exclusively by plasma membranelocalized cellulose synthases (CESAs). Therefore, the trafficking of CESAs to and from the plasma membrane is an important mechanism for regulating cellulose biosynthesis. CESAs were recently identified as cargo proteins of the classic adaptor protein 2 (AP2) complex of the clathrin-mediated endocytosis (CME) pathway. The AP2 complex of the CME pathway is conserved in yeast, animals, and plants, and has been well-characterized in many systems. In contrast, the recently discovered TPLATE complex (TPC), which is proposed to function as a CME adaptor complex, is only conserved in plants and a few other eukaryotes. In this study, we discovered that the TWD40-2 protein, a putative member of the TPC, is also important for the endocytosis of CESAs. Genetic analysis between TWD40-2 and AP2M of the AP2 complex revealed that the roles of TWD40-2 in CME are both distinct from and cooperative with the AP2 complex. Loss of efficient CME intwd40-2-3resulted in the unregulated overaccumulation of CESAs at the plasma membrane. In seedlings oftwd40-2-3and other CME-deficient mutants, a direct correlation was revealed between endocytic deficiency and cellulose content deficiency, highlighting the importance of controlled CESA endocytosis in regulating cellulose biosynthesis.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1509292112