期刊
SCIENCE
卷 317, 期 5842, 页码 1217-1220出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1144646
关键词
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资金
- Medical Research Council [G9722488, G9900061, G19/31] Funding Source: Medline
- Wellcome Trust [081894] Funding Source: Medline
- Medical Research Council [G9722488, G19/31, G9900061] Funding Source: researchfish
- MRC [G9722488, G9900061] Funding Source: UKRI
Cell-cell contacts are fundamental to multicellular organisms and are subject to exquisite levels of control. Human RPTP mu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes. Here we describe a 3.1 angstrom crystal structure of the RPTPm ectodomain that forms a homophilic trans ( antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions. Cell surface expression of deletion constructs induces intercellular spacings that correlate with the ectodomain length. These data suggest that the RPTPm ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location.
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