Document Detail


Evidence of an interaction between Mos and Hsp70: a role of the Mos residue serine 3 in mediating Hsp70 association.
MedLine Citation:
PMID:  10376524     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
c-Mos is a germ cell-specific MAP kinase kinase kinase (MAPKKK) that plays an essential role during meiotic divisions of oocytes. c-Mos is a key component of an activity, cytostatic factor, required for metaphase II arrest of unfertilized eggs in vertebrates. To understand the regulation of c-Mos, we are investigating c-Mos-interacting proteins. We provide evidence that mouse c-Mos binds to Hsp70, a molecular chaperone. Hsp70 was found to associate with Mos ectopically expressed in COS-1 cells. Mos-Hsp70 complexes could be immunoprecipitated with both Mos and Hsp70 antibodies. Despite a low-abundance of Mos, the Hsp70 antibody immunoprecipitated Mos as the major protein. Of importance, the Mos protein present in anti-Hsp70 immunoprecipitates functioned as an active MAPKKK indicating that it is not grossly misfolded. It is known that c-Mos protein kinase activity in cell extracts of transfected COS-1 or NIH3T3 cells is labile. We found that the inclusion of adenosine triphosphate (ATP) in cell extracts protected against the loss of Mos kinase activity. In the absence of ATP from cell extracts, protein kinase activity of Mos was lost within 6 h on ice even though the Mos protein was not degraded and remained bound to Hsp70. Based on our identification of c-Mos-Hsp70 interaction, one of the roles of ATP may be to assist the regulation of c-Mos via ATP involvement in the protein-folding function of Hsp70 and possibly other molecular chaperones. We also detected by coimmunoprecipitation a physical association between endogenous c-Mos and Hsp70 in Xenopus eggs. To provide further evidence for the functional significance of Hsp70 interaction to Mos function, we show that the residue serine 3 in Mos, which is important for the regulation of protein kinase activity of Mos is also important for Hsp70 association.
Authors:
H Liu; V B Vuyyuru; C D Pham; Y Yang; B Singh
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Oncogene     Volume:  18     ISSN:  0950-9232     ISO Abbreviation:  Oncogene     Publication Date:  1999 Jun 
Date Detail:
Created Date:  1999-06-30     Completed Date:  1999-06-30     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  8711562     Medline TA:  Oncogene     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  3461-70     Citation Subset:  IM    
Affiliation:
Department of Molecular Pathology, The University of Texas MD Anderson Cancer Center, Houston 77030, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
COS Cells
HSP70 Heat-Shock Proteins / physiology*
Mice
Proto-Oncogene Proteins c-mos / physiology*
Grant Support
ID/Acronym/Agency:
CA16672/CA/NCI NIH HHS; R01 CA45125/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/HSP70 Heat-Shock Proteins; EC 2.7.11.1/Proto-Oncogene Proteins c-mos

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