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rdf:type |
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lifeskim:mentions |
umls-concept:C0033634,
umls-concept:C0033684,
umls-concept:C0085087,
umls-concept:C0205164,
umls-concept:C0205349,
umls-concept:C0392756,
umls-concept:C0441889,
umls-concept:C1416956,
umls-concept:C1510411,
umls-concept:C1704711,
umls-concept:C1710236
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pubmed:issue |
6
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pubmed:dateCreated |
1992-3-20
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pubmed:abstractText |
The 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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
0898-6568
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
569-76
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:1838487-3T3 Cells,
pubmed-meshheading:1838487-Animals,
pubmed-meshheading:1838487-Cell Line, Transformed,
pubmed-meshheading:1838487-Cell Transformation, Neoplastic,
pubmed-meshheading:1838487-Immunoblotting,
pubmed-meshheading:1838487-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:1838487-Membrane Proteins,
pubmed-meshheading:1838487-Mice,
pubmed-meshheading:1838487-Oncogene Protein p21(ras),
pubmed-meshheading:1838487-Oncogene Protein pp60(v-src),
pubmed-meshheading:1838487-Oncogene Proteins,
pubmed-meshheading:1838487-Phosphorylation,
pubmed-meshheading:1838487-Protein Kinase C,
pubmed-meshheading:1838487-Proteins,
pubmed-meshheading:1838487-Rats,
pubmed-meshheading:1838487-Transfection
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pubmed:year |
1991
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pubmed:articleTitle |
Transformed 3T3 cells have reduced levels and altered subcellular distribution of the major PKC substrate protein MARCKS.
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pubmed:affiliation |
University of Pennsylvania School of Medicine, Department of Pathology and Laboratory Medicine, Philadelphia 19104.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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