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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1992-12-30
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pubmed:abstractText |
It is important for the understanding of protein kinase action to differentiate between regulation at the enzyme and at the substrate levels. For example, the inhibitors dinitrophenol-tyrosine and tyrphostins act at the enzyme level to inhibit phosphorylation of all substrates by c-Src and v-Src kinases. In contrast, polylysine acts at the substrate level to stimulate Src-mediated phosphorylation of beta-casein but to inhibit phosphorylation of alpha-casein. Here we demonstrate novel enzyme-specific and substrate-specific modulations of Src kinase activity of potential physiological significance. At the enzyme level, we observed that c-Src kinase preferentially phosphorylates alpha-casein, while the v-Src kinase prefers beta-casein. At the substrate level we observed substrate-specific modulation by physiological factors including sphingosine, sphingosine derivatives and the ganglioside GM3. Galactosyl-sphingosine (psychosine) was more effective in stimulating phosphorylation of beta-casein and poly(E1A1Y1) than sphingosine. Glucosyl- and lactosyl-sphingosine were ineffective. Rat was extensively phosphorylated by c-Src in the presence of polylysine, and to a lesser extent in the sphingosine and galactosyl-sphingosine. These unexpected differences point out another potential mechanism for regulation of c-Src and v-Src kinase activities and may help to explain some of the pleotyptic manifestations of protein tyrosine kinase actions.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CSK tyrosine-protein kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Caseins,
http://linkedlifedata.com/resource/pubmed/chemical/Oncogene Protein pp60(v-src),
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins pp60(c-src),
http://linkedlifedata.com/resource/pubmed/chemical/Sphingosine
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
1137
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
349-55
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:1280164-Animals,
pubmed-meshheading:1280164-Caseins,
pubmed-meshheading:1280164-Cattle,
pubmed-meshheading:1280164-Dogs,
pubmed-meshheading:1280164-Genes, ras,
pubmed-meshheading:1280164-Genes, src,
pubmed-meshheading:1280164-Humans,
pubmed-meshheading:1280164-Oncogene Protein pp60(v-src),
pubmed-meshheading:1280164-Phosphorylation,
pubmed-meshheading:1280164-Protein-Tyrosine Kinases,
pubmed-meshheading:1280164-Proto-Oncogene Proteins pp60(c-src),
pubmed-meshheading:1280164-Sphingosine,
pubmed-meshheading:1280164-Substrate Specificity
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pubmed:year |
1992
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pubmed:articleTitle |
Substrate-specific modulation of Src-mediated phosphorylation of Ras and caseins by sphingosines and other substrate modulators.
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pubmed:affiliation |
Section of Biochemistry, Cornell University, Itahaca, NY 14853.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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