Physical and Functional Interactions between Receptor-like Protein-tyrosine Phosphatase α and p59 fyn *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 273, Issue: 15, Page: 8691-8698
1998
- 81Citations
- 20Captures
- 1Mentions
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Metrics Details
- Citations81
- Citation Indexes81
- 81
- CrossRef71
- Captures20
- Readers20
- 20
- Mentions1
- References1
- Wikipedia1
Article Description
We have examined the in vivo activity of receptor-like protein-tyrosine phosphatase α (PTPα) toward p59 fyn, a widely expressed Src family kinase. In a coexpression system, PTPα effected a dose-dependent tyrosine dephosphorylation and activation of p59 fyn, where maximal dephosphorylation correlated with a 5-fold increase in kinase activity. PTPα expression resulted in increased accessibility of the p59 fyn SH2 domain, consistent with a PTPα-mediated dephosphorylation of the regulatory C-terminal tyrosine residue of p59 fyn. No p59 fyn dephosphorylation was observed with an enzymatically inactive mutant form of PTPα or with another receptor-like PTP, CD45. Many enzyme-linked receptors are complexed with their substrates, and we examined whether PTPα and p59 fyn underwent association. Reciprocal immunoprecipitations and assays detected p59 fyn and an appropriate kinase activity in PTPα immunoprecipitates and PTPα and PTP activity in p59 fyn immunoprecipitates. No association between CD45 and p59 fyn was detected in similar experiments. The PTPα-mediated activation of p59 fyn is not prerequisite for association since wild-type and inactive mutant PTPα bound equally well to p59 fyn. Endogenous PTPα and p59 fyn were also found in association in mouse brain. Together, these results demonstrate a physical and functional interaction of PTPα and p59 fyn that may be of importance in PTPα-initiated signaling events.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925818495543; http://dx.doi.org/10.1074/jbc.273.15.8691; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=2642710919&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/9535845; https://linkinghub.elsevier.com/retrieve/pii/S0021925818495543; https://dx.doi.org/10.1074/jbc.273.15.8691
Elsevier BV
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