منابع مشابه
Cellular interactions of CRKL, and SH2-SH3 adaptor protein.
Chronic myelogenous leukemia is characterized by a specific chromosomal translocation, t(9;22), in which the ABL protooncogene and the BCR gene become juxtaposed. The chimeric BCR/ABL gene produces a P210 fusion protein with deregulated tyrosine kinase activity. We have recently isolated a complementary DNA, CRKL, which could code for an adaptor protein consisting of one SH2 and two SH3 domains...
متن کاملMolecular and biophysical analysis of the non-catalytic PH, TH, SH3 and SH2 domains of Bruton tyrosine kinase (Btk) protein
Academic dissertation To be presented for public criticism, with the permission of Abbreviations Abstract 1 Introduction 10 1.1 Primary immunodeficiencies (PIDs) 10 1.1.1 X-linked agammaglobulinemia (XLA) 12
متن کاملSH3 domains: complexity in moderation.
The SH3 domain is perhaps the best-characterized member of the growing family of protein-interaction modules. By binding with moderate affinity and selectivity to proline-rich ligands, these domains play critical roles in a wide variety of biological processes ranging from regulation of enzymes by intramolecular interactions, increasing the local concentration or altering the subcellular locali...
متن کاملBoth the SH2 and SH3 domains of human CRK protein are required for neuronal differentiation of PC12 cells.
Human CRK protein is a homolog of the chicken v-crk oncogene product and consists mostly of src homology region 2 (SH2) and SH3, which are shared by many proteins, in particular those involved in signal transduction. SH2 has been shown to bind specifically to phosphotyrosine-containing peptides. We report here that both SH2 and SH3 are required for signaling from CRK protein. Microinjection of ...
متن کاملRequirement of the SH3 and SH2 domains for the inhibitory function of tyrosine protein kinase p50csk in T lymphocytes.
Previous studies from our laboratory have shown that the cytosolic tyrosine protein kinase p50csk is involved in the negative regulation of T-cell activation (L.M. L. Chow, M. Fournel, D. Davidson, and A. Veillette, Nature [London] 365:156-160, 1993). This function most probably reflects the ability of Csk to phosphorylate the inhibitory carboxy-terminal tyrosine of p56lck and p59fynT, two Src-...
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ژورنال
عنوان ژورنال: Current Biology
سال: 1992
ISSN: 0960-9822
DOI: 10.1016/0960-9822(92)90873-9