Linked Life Data

1838487

Source:http://linkedlifedata.com/resource/pubmed/id/1838487

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pubmed-article:1838487pubmed:abstractTextThe MARCKS (myristylated alanine-rich C-kinase substrate) protein is an abundant calmodulin-binding protein that is a major and specific endogenous substrate of protein kinase C (PKC). Stimulation of cells with phorbol esters or other activators of PKC has been shown previously to result in rapid phosphorylation of MARCKS proteins and redistribution of these myristylated C-kinase substrates from membrane to cytosol. Here we show that NIH3T3 murine fibroblasts transformed by p21-HA-C-RAS or pp60-V-SRC oncoproteins have markedly reduced levels of p68-MARCKS and that most of the remaining MARCKS protein is found in the cytosol. 3T3 cells containing a nontransforming oncoprotein p26-BCL2, in contrast, exhibited normal levels and distribution of p68-MARCKS. When taken together with recent evidence that MARCKS proteins are involved in regulating organization of the membrane cytoskeleton, our findings suggest that oncoprotein-mediated alterations in MARCKS protein levels and subcellular distribution may contribute to the development or maintenance of the transformed phenotype.lld:pubmed
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pubmed-article:1838487pubmed:dateRevised2009-11-19lld:pubmed
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pubmed-article:1838487pubmed:articleTitleTransformed 3T3 cells have reduced levels and altered subcellular distribution of the major PKC substrate protein MARCKS.lld:pubmed
pubmed-article:1838487pubmed:affiliationUniversity of Pennsylvania School of Medicine, Department of Pathology and Laboratory Medicine, Philadelphia 19104.lld:pubmed
pubmed-article:1838487pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1838487pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:1838487pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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