Major substrate for growth factor-activated protein-tyrosine kinases is a low-abundance protein.
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Heat Shock Factor 1 Is a Substrate for p38 Mitogen-Activated Protein Kinases
Heat shock factor 1 (HSF1) monitors the structural integrity of the proteome. Phosphorylation at S326 is a hallmark for HSF1 activation, but the identity of the kinase(s) phosphorylating this site has remained elusive. We show here that the dietary agent phenethyl isothiocyanate (PEITC) inhibits heat shock protein 90 (Hsp90), the main negative regulator of HSF1; activates p38 mitogen-activated ...
متن کاملGrowth factors and mitogen-activated protein kinases.
Mammalian cells respond to external stimuli by activation of a variety of signal transduction pathways, which culminate in stereotypical responses, such as proliferation, growth arrest, hypertrophy, differentiation, or apoptosis. In vertebrates the actions of many stimuli resulting in proliferative or hypertrophic growth converge on a set of cellular kinase cascades, which are collectively call...
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Bacteria and Eukarya share essentially the same family of protein-serine/threonine kinases, also known as the Hanks-type kinases. However, when it comes to protein-tyrosine phosphorylation, bacteria seem to have gone their own way. Bacterial protein-tyrosine kinases (BY-kinases) are bacterial enzymes that are unique in exploiting the ATP/GTPbinding Walker motif to catalyze phosphorylation of pr...
متن کاملTyrosine-phosphorylated caveolin is a physiological substrate of the low M(r) protein-tyrosine phosphatase.
Low M(r) phosphotyrosine-protein phosphatase is involved in the regulation of several tyrosine kinase growth factor receptors. The best characterized action of this enzyme is on the signaling pathways activated by platelet-derived growth factor, where it plays multiple roles. In this study we identify tyrosine-phosphorylated caveolin as a new potential substrate for low M(r) phosphotyrosine-pro...
متن کاملNon-receptor protein tyrosine kinases.
The protein tyrosine kinases (PTKs) are enzymes catalyzing the transfer of the gamma-phosphate group of ATP to the hydroxyl groups of specific tyrosine residues in peptides. Although phosphotransfer reactions catalyzed by various PTKs are similar with regard to their basic mechanisms, their biological functions demonstrate a considerable degree of specificity. PTKs are divided into two groups a...
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ژورنال
عنوان ژورنال: Molecular and Cellular Biology
سال: 1985
ISSN: 0270-7306,1098-5549
DOI: 10.1128/mcb.5.11.3304