Linked Life Data

11487585

Source:http://linkedlifedata.com/resource/pubmed/id/11487585

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pubmed-article:11487585pubmed:abstractTextB cell linker protein (BLNK) is a SLP-76-related adaptor protein essential for signal transduction from the BCR. To identify components of BLNK-associated signaling pathways, we performed a phosphorylation-dependent yeast two-hybrid analysis using BLNK probes. Here we report that the serine/threonine kinase hematopoietic progenitor kinase 1 (HPK1), which is activated upon antigen-receptor stimulation and which has been implicated in the regulation of MAP kinase pathways, interacts physically and functionally with BLNK in B cells and with SLP-76 in T cells. This interaction requires Tyr(379) of HPK1 and the Src homology 2 (SH2) domain of BLNK/SLP-76. Via homology modeling, we defined a consensus binding site within ligands for SLP family SH2 domains. We further demonstrate that the SH2 domain of SLP-76 participates in the regulation of AP-1 and NFAT activation in response to T cell receptor (TCR) stimulation and that HPK1 inhibits AP-1 activation in a manner partially dependent on its interaction with SLP-76. Our data are consistent with a model in which full activation of HPK1 requires its own phosphorylation on tyrosine and subsequent interaction with adaptors of the SLP family, providing a mechanistic basis for the integration of this kinase into antigen receptor signaling cascades.lld:pubmed
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pubmed-article:11487585pubmed:articleTitleHematopoietic progenitor kinase 1 associates physically and functionally with the adaptor proteins B cell linker protein and SLP-76 in lymphocytes.lld:pubmed
pubmed-article:11487585pubmed:affiliationDepartment of Immunology and Rheumatology and Department of Molecular Systems, Merck Research Laboratories, Rahway, New Jersey 07065, USA. Karsten_Sauer@Merck.comlld:pubmed
pubmed-article:11487585pubmed:publicationTypeJournal Articlelld:pubmed
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