Cloning and characterization of Lnk, a signal transduction protein that links T-cell receptor activation signal to phospholipase C gamma 1, Grb2, and phosphatidylinositol 3-kinase.

A cDNA encoding a signal transduction protein with a Src homology 2 (SH2) domain and a tyrosine phosphorylation site was cloned from a rat lymph node cDNA library. This protein, which we designate Lnk, has a calculated molecular weight of 33,988. When T lymphocytes were activated by antibody-mediated crosslinking of the T-cell receptor and CD4, Lnk became tyrosine phosphorylated. In activated T lymphocytes, phospholipase C gamma 1, phosphatidylinositol 3-kinase, and Grb-2 coimmunoprecipitated with Lnk. Our results suggest that Lnk becomes tyrosine phosphorylated and links the immediate tyrosine phosphorylation signals of the TCR to the distal phosphatidylinositol 3-kinase, phospholipase C gamma 1 and Ras signaling pathways through its multifunctional tyrosine phosphorylation site.

Annexe II: Analyse de la situation politique en Mediterranee et dans les pays du golfe el les risques sur les approvisionnements petroliers et gaziers 1) Algerie & Pays D'Afrique du Nord 2) Pays de L'Est Mediterraneen et du Golfe. OME, Draft du 18 April 1995 = Annex II: Analysis of the political situation in the Mediterranean and the Gulf countries and risks on petroleum and gas supplies 1) Pays D'Algerie & North Africa 2) Country of Eastern Mediterraneen and the Gulf. OME, Draft of 18 April 1995

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