Journal
PLANT PHYSIOLOGY
Volume 163, Issue 1, Pages 150-160Publisher
AMER SOC PLANT BIOLOGISTS
DOI: 10.1104/pp.113.221234
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Funding
- Center for LignoCellulose Structure and Formation, an Energy Frontier Research Center
- U.S. Department of Energy, Office of Science, Office of Basic Sciences [DE-SC0001090]
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Clathrin-mediated endocytosis (CME) is the best-characterized type of endocytosis in eukaryotic cells. Plants appear to possess all of the molecular components necessary to carry out CME; however, functional characterization of the components is still in its infancy. A yeast two-hybrid screen identified mu 2 as a putative interaction partner of CELLULOSE SYNTHASE6 (CESA6). Arabidopsis (Arabidopsis thaliana) mu 2 is homologous to the medium subunit 2 of the mammalian ADAPTOR PROTEIN COMPLEX2 (AP2). In mammals, the AP2 complex acts as the central hub of CME by docking to the plasma membrane while concomitantly recruiting cargo proteins, clathrin triskelia, and accessory proteins to the sites of endocytosis. We confirmed that mu 2 interacts with multiple CESA proteins through the mu-homology domain of mu 2, which is involved in specific interactions with endocytic cargo proteins in mammals. Consistent with its role in mediating the endocytosis of cargos at the plasma membrane, mu 2-YELLOW FLUORESCENT PROTEIN localized to transient foci at the plasma membrane, and loss of mu 2 resulted in defects in bulk endocytosis. Furthermore, loss of mu 2 led to increased accumulation of YELLOW FLUORESCENT PROTEIN-CESA6 particles at the plasma membrane. Our results suggest that CESA represents a new class of CME cargo proteins and that plant cells might regulate cellulose synthesis by controlling the abundance of active CESA complexes at the plasma membrane through CME.
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