ArticleMolecular and cellular biology1993
Differential effects of expression of the CD45 tyrosine protein phosphatase on the tyrosine phosphorylation of the lck, fyn, and c-src tyrosine protein kinases.
Article in Molecular and cellular biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers, 1 of them a synthesis that pooled it.
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Who cites it
38 citing papers in PubMed, 1 synthesis or guideline pooled it, 179 citations in OpenAlex.
- Regulation of TCR signalling by tyrosine phosphatases: from immune homeostasis to autoimmunity.Immunology · 2012Pooled it
- Sensitive FRET Biosensor Reveals Fyn Kinase Regulation by Submembrane Localization.ACS sensors · 2019Article
- Cluster of differentiation 45 activation is crucial in interleukin-10-dependent tumor-associated dendritic cell differentiation.Oncology letters · 2014Article
- Lck, Membrane Microdomains, and TCR Triggering Machinery: Defining the New Rules of Engagement.Frontiers in immunology · 2012Article
- Loss of tyrosine phosphatase-dependent inhibition promotes activation of tyrosine kinase c-Src in detached pancreatic cells.Molecular carcinogenesis · 2010Article
- Intracellular reactive oxygen species activate Src tyrosine kinase during cell adhesion and anchorage-dependent cell growth.Molecular and cellular biology · 2005Article
- T cell receptor engagement leads to phosphorylation of clathrin heavy chain during receptor internalization.The Journal of experimental medicine · 2004Article
- HIV-1 infection is facilitated in T cells by decreasing p56lck protein tyrosine kinase activity.Clinical and experimental immunology · 2003Article
- Positive and negative regulation of T-cell activation through kinases and phosphatases.The Biochemical journal · 2003Review
- Development of T-leukaemias in CD45 tyrosine phosphatase-deficient mutant lck mice.The EMBO journal · 2000Article
- A phosphotyrosine displacement mechanism for activation of Src by PTPalpha.The EMBO journal · 2000Article
- Expression of the p56(Lck) Y505F mutation in CD45-deficient mice rescues thymocyte development.Molecular and cellular biology · 1999Article
- Article
- Cooperative inhibition of T-cell antigen receptor signaling by a complex between a kinase and a phosphatase.The Journal of experimental medicine · 1999Article
- CD45 and RPTPalpha display different protein tyrosine phosphatase activities in T lymphocytes.The Biochemical journal · 1997Article
- Impaired bone marrow microenvironment and immune function in T cell protein tyrosine phosphatase-deficient mice.The Journal of experimental medicine · 1997Article
- Regulation of cell signaling by the protein tyrosine phosphatases, CD45 and SHP-1.Immunologic research · 1997Review
- The Syk protein tyrosine kinase can function independently of CD45 or Lck in T cell antigen receptor signaling.The EMBO journal · 1996Article
- Dephosphorylation of receptor tyrosine kinases as target of regulation by radiation, oxidants or alkylating agents.The EMBO journal · 1996Article
- CD45-null transgenic mice reveal a positive regulatory role for CD45 in early thymocyte development, in the selection of CD4+CD8+ thymocytes, and B cell maturation.The Journal of experimental medicine · 1996Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Expression of the CD45 tyrosine protein phosphatase is required for the response of functional lymphocytes to stimulation through the antigen receptor. One or more of its substrates may therefore be essential for signal transduction during lymphocyte activation. We have studied the phosphorylation of the closely related lck, fyn, and c-src tyrosine protein kinases in leukemic murine T-cell lines that have lost the expression of CD45. The phosphorylation of the lck kinase at an inhibitory site of tyrosine phosphorylation, Tyr-505, was increased by two-, six-, and eightfold in three different cell lines. Phosphorylation of the fyn kinase at the homologous site, Tyr-531, was unaltered in one of these cell lines, but increased by 2.5-fold in the two others. The phosphorylation of p60c-src at the homologous tyrosine was essentially unchanged in the one CD45-negative cell line in which it was examined. The expression of CD45 therefore regulates the phosphorylation and potentially the activity of the lck and fyn tyrosine protein kinases, but the effect on the lck kinase is much greater than on the fyn kinase. This finding and the observation that CD45 had no effect on the phosphorylation of p60c-src suggest that CD45 exhibits polypeptide substrate specificity in vivo. Additionally, these findings are consistent with the hypothesis that the unresponsiveness of CD45-negative lymphoid cells to antigenic stimulation is due largely to hyperphosphorylation of the lck kinase.
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Registered trials
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