Document Detail


Cell cycle-mediated structural and functional alteration of P85gag-mos protein kinase activity.
MedLine Citation:
PMID:  2138725     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We investigated cell cycle-dependent regulation of protein kinase activity encoded by the viral mos gene by using a normal rat kidney cell line (NRK-6m2) chronically infected with a temperature-sensitive mutant (ts110) of Moloney murine sarcoma virus, which produces the P85gag-mos transforming protein. In elutriation experiments, in which cells in various phases of the cell cycle are separated based upon size, a twofold increase in the specific activity of the P85gag-mos protein kinase was observed as cells progressed from G0/G1 through S and G2/M. A three- to fourfold increase in gas-mos protein kinase specific activity relative to unsynchronized cells was observed in mitotic NRK-6m2 cells synchronized by treatment with thymidine followed by colcemid or with nocodazole alone. Interestingly, the gag-mos protein was structurally altered in mitotic cells generating a protein species moving slower than P85gag-mos in SDS-polyacrylamide gels. Our findings indicate that viral mos protein kinase activity is regulated during the cell cycle via phosphorylation. We propose that the mos transforming protein functions in a pleiotropic manner, affecting both cytoplasmic and nuclear targets.
Authors:
J X Liu; B Singh; D Wlodek; R B Arlinghaus
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Oncogene     Volume:  5     ISSN:  0950-9232     ISO Abbreviation:  Oncogene     Publication Date:  1990 Feb 
Date Detail:
Created Date:  1990-05-04     Completed Date:  1990-05-04     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  8711562     Medline TA:  Oncogene     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  171-8     Citation Subset:  IM    
Affiliation:
Department of Molecular Pathology, University of Texas M.D. Anderson Cancer Center, Houston 77030.
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / analysis
Animals
Cell Cycle
Cell Separation
Immunoblotting
Mitosis
Oncogene Proteins v-mos
Peptide Mapping
Phosphorylation
Protein-Tyrosine Kinases / analysis*
Rats
Retroviridae Proteins, Oncogenic / analysis*,  immunology,  physiology
Grant Support
ID/Acronym/Agency:
CA16672/CA/NCI NIH HHS; CA45125/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Oncogene Proteins v-mos; 0/Retroviridae Proteins, Oncogenic; EC 2.7.10.1/Protein-Tyrosine Kinases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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