| pubmed-article:8114715 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8114715 | lifeskim:mentions | umls-concept:C0039194 | lld:lifeskim |
| pubmed-article:8114715 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:8114715 | lifeskim:mentions | umls-concept:C0085536 | lld:lifeskim |
| pubmed-article:8114715 | lifeskim:mentions | umls-concept:C1705637 | lld:lifeskim |
| pubmed-article:8114715 | lifeskim:mentions | umls-concept:C0591833 | lld:lifeskim |
| pubmed-article:8114715 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:8114715 | pubmed:dateCreated | 1994-3-25 | lld:pubmed |
| pubmed-article:8114715 | pubmed:abstractText | The phosphorylation and dephosphorylation of proteins on tyrosyl residues are key regulatory mechanisms in T-cell signal transduction and are controlled by the opposing activities of protein tyrosine kinases and phosphotyrosyl phosphatases (PTPs). In T cells, several nontransmembrane protein tyrosine kinases are associated with receptors; for example, Lck is bound to the coreceptors CD4 and CD8 and becomes activated upon their stimulation. In comparison, little is known about the role of nontransmembrane PTPs in early T-cell signaling. SH-PTP1 (PTP1C, HCP, SHP) is a nontransmembrane PTP expressed primarily in hematopoietic cells, including T cells. We have found that SH-PTP1 is basally phosphorylated on serine in resting T cells. Upon stimulation of CD4 or CD8 either in a T-cell hybridoma cell line or in primary thymocytes, SH-PTP1 becomes tyrosyl phosphorylated. Moreover, SH-PTP1 is constitutively phosphorylated on tyrosine in the Lck-overexpressing lymphoma cell line LSTRA. SH-PTP1 is also a good substrate for recombinant Lck in vitro. Comparisons of the tryptic phosphopeptide maps of wild-type SH-PTP1 and deletion and point mutations establish that the two sites (Y-536 and Y-564) which are directly phosphorylated by Lck in vitro are also phosphorylated in vivo in LSTRA cells. One of these sites (Y-564) is phosphorylated in T cells in response to Lck activation. We conclude that SH-PTP1 undergoes Lck-dependent tyrosyl phosphorylation in T cells and likely plays a role in early T-cell signaling. | lld:pubmed |
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| pubmed-article:8114715 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8114715 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8114715 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8114715 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:8114715 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:8114715 | pubmed:author | pubmed-author:WalshC TCT | lld:pubmed |
| pubmed-article:8114715 | pubmed:author | pubmed-author:BurakoffS JSJ | lld:pubmed |
| pubmed-article:8114715 | pubmed:author | pubmed-author:LorenzUU | lld:pubmed |
| pubmed-article:8114715 | pubmed:author | pubmed-author:NeelB GBG | lld:pubmed |
| pubmed-article:8114715 | pubmed:author | pubmed-author:RavichandranK... | lld:pubmed |
| pubmed-article:8114715 | pubmed:author | pubmed-author:PeiDD | lld:pubmed |
| pubmed-article:8114715 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8114715 | pubmed:volume | 14 | lld:pubmed |
| pubmed-article:8114715 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8114715 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8114715 | pubmed:pagination | 1824-34 | lld:pubmed |
| pubmed-article:8114715 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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