The BioGRID | PUBLICATION VIEW

	Biochem. Biophys. Res. Commun. Nov (2002); 298(5):720-30
The beta2-adaptin clathrin adaptor interacts with the mitotic checkpoint kinase BubR1.
Cayrol C, Cougoule C, Wright M
Institut de Pharmacologie et de Biologie Structurale du CNRS-UMR 5089, 205 route de Narbonne, 31077 Toulouse, France. Corinne.Cayrol@ipbs.fr
Abstract: The adaptor AP2 is a heterotetrameric complex that associates with clathrin and regulatory proteins to mediate rapid endocytosis from the plasma membrane. Here, we report the identification of the mitotic checkpoint kinase BubR1 as a novel binding partner of beta2-adaptin, one of the AP2 large subunits. Using two-hybrid experiments and in vitro binding assays, we show that beta2-adaptin binds to BubR1 through its amino-terminal beta2-'trunk' domain, while the beta2-binding region of BubR1 maps to the carboxy-terminal kinase domain. Subcellular immunolocalization studies suggest that the interaction between BubR1 and beta2-adaptin could take place in the cytosol at any time during the cell cycle. In addition, we found that BubR1 and the BubR1-related kinase, Bub1, also bind to beta-adaptins of other AP complexes. Together, these results support a model in which the mitotic checkpoint kinases BubR1 and BuB1, by binding to beta-adaptins, may play novel roles in the regulation of vesicular intracellular traffic.
[PUBMED: 12419313]