期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 287, 期 34, 页码 28537-28551出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M112.354852
关键词
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资金
- National Institutes of Health [AR052133]
- Japan Society for the Promotion of Science
- Canadian Institutes for Health Research
- National Science and Engineering Research Council of Canada
- American Heart Association [11GRNT7820000]
- Department of Pathology at Emory University
- National Center for Research Resources of the National Institutes of Health
Caenorhabditis elegans muscle cells attach to basement membrane through adhesion plaques. PAT-3 (beta-integrin), UNC-112 (kindlin), and PAT-4 (integrin-linked kinase) are associated with these structures. Genetic analysis indicated that PAT-4 is required for UNC-112 to be properly localized. We investigated the molecular basis of this requirement. We show that the cytoplasmic tail of PAT-3 binds to full-length UNC-112 and that the N-and C-terminal halves of UNC-112 bind to each other. We demonstrate competition between the UNC-112 C-terminal half and PAT-4 for binding to the UNC-112 N-terminal half. The D382V mutation results in lack of binding to PAT-4 and lack of localization to adhesion structures. T346A or E349K mutations, which abolish interaction of the N-and C-terminal halves, permit D382V UNC-112 to localize to adhesion structures. The following model is proposed. UNC-112 exists in closed inactive and open active conformations, and upon binding of PAT-4 to the UNC-112 N-terminal half, UNC-112 is converted into the open state, able to bind to PAT-3.
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