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• W1995661906 endingPage "1072" @default.
• W1995661906 startingPage "1059" @default.
• W1995661906 abstract "The receptor protein tyrosine phosphatase PTPmu belongs to a family of adhesion molecules that contain cell-cell adhesion motifs in their extracellular segments and catalytic domains within their intracellular segments. The ability of PTPmu both to mediate adhesion and exhibit enzymatic activity makes PTPmu an excellent candidate to transduce signals in response to cell-cell adhesion. In an effort to identify downstream signaling partners of PTPmu, we performed a modified yeast two-hybrid screen using the first tyrosine phosphatase domain of PTPmu as bait. We isolated an interacting clone encoding BRCA2 and CDKN1A interacting protein (BCCIP) from a HeLa cell library. BCCIP is a p21 and BRCA2 interacting protein that has been shown to play roles in both cell cycle arrest and DNA repair. In this manuscript, we confirm the interaction between BCCIP and PTPmu identified in yeast using in vitro biochemical studies and characterize BCCIP as a PTPmu binding protein. We demonstrate that BCCIP is phosphorylated by the Src tyrosine kinase and dephosphorylated by the PTPmu tyrosine phosphatase in vitro. Furthermore, we show that BCCIP is required for both the permissive and repulsive functions of PTPmu in neurite outgrowth assays, suggesting BCCIP and PTPmu are in a common signal transduction pathway." @default.
• W1995661906 created "2016-06-24" @default.
• W1995661906 creator A5010362232 @default.
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• W1995661906 date "2008-11-01" @default.
• W1995661906 modified "2023-10-10" @default.
• W1995661906 title "BCCIP associates with the receptor protein tyrosine phosphatase PTPµ" @default.
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• W1995661906 doi "https://doi.org/10.1002/jcb.21907" @default.
• W1995661906 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2758318" @default.
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