Document Detail


Hsp27 enhances recovery of splicing as well as rephosphorylation of SRp38 after heat shock.
MedLine Citation:
PMID:  16339078     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A heat stress causes a rapid inhibition of splicing. Exogenous expression of Hsp27 did not prevent that inhibition but enhanced the recovery of splicing afterward. Another small heat shock protein, alphaB-crystallin, had no effect. Hsp27, but not alphaB-crystallin, also hastened rephosphorylation of SRp38-dephosphorylated a potent inhibitor of splicing-after a heat shock, although it did not prevent dephosphorylation by a heat shock. The effect of Hsp27 on rephosphorylation of SRp38 required phosphorylatable Hsp27. A Hsp90 client protein was required for the effect of Hsp27 on recovery of spicing and on rephosphorylation of SRp38. Raising the Hsp70 level by either a pre-heat shock or by exogenous expression had no effect on either dephosphorylation of SRp38 during heat shock or rephosphorylation after heat shock. The phosphatase inhibitor calyculin A prevented dephosphorylation of SRp38 during a heat shock and caused complete rephosphorylation of SRp38 after a heat shock, indicating that cells recovering from a heat shock are not deficient in kinase activity. Together our data show that the activity of Hsp27 in restoring splicing is not due to a general thermoprotective effect of Hsp27, but that Hsp27 is an active participant in the (de)phosphorylation cascade controlling the activity of the splicing regulator SRp38.
Authors:
Laura Marin-Vinader; Chanseok Shin; Carla Onnekink; James L Manley; Nicolette H Lubsen
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2005-12-07
Journal Detail:
Title:  Molecular biology of the cell     Volume:  17     ISSN:  1059-1524     ISO Abbreviation:  Mol. Biol. Cell     Publication Date:  2006 Feb 
Date Detail:
Created Date:  2006-01-25     Completed Date:  2006-04-07     Revised Date:  2013-06-07    
Medline Journal Info:
Nlm Unique ID:  9201390     Medline TA:  Mol Biol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  886-94     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Radboud University Nijmegen, 6500 HB Nijmegen, The Netherlands.
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MeSH Terms
Descriptor/Qualifier:
Cell Cycle Proteins / metabolism*
HSP27 Heat-Shock Proteins
HSP70 Heat-Shock Proteins / physiology
HSP90 Heat-Shock Proteins / antagonists & inhibitors,  physiology
HeLa Cells
Heat-Shock Proteins / metabolism,  physiology*
Humans
Neoplasm Proteins / metabolism*,  physiology*
Oxazoles / pharmacology
Phosphorylation / drug effects
Protein Processing, Post-Translational
RNA Splicing / physiology*
RNA-Binding Proteins / metabolism*
Repressor Proteins / metabolism*
alpha-Crystallin B Chain / physiology
Grant Support
ID/Acronym/Agency:
R37 GM48259/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Cell Cycle Proteins; 0/HSP27 Heat-Shock Proteins; 0/HSP70 Heat-Shock Proteins; 0/HSP90 Heat-Shock Proteins; 0/HSPB1 protein, human; 0/Heat-Shock Proteins; 0/Neoplasm Proteins; 0/Oxazoles; 0/RNA-Binding Proteins; 0/Repressor Proteins; 0/SRSF10 protein, human; 0/alpha-Crystallin B Chain; 101932-71-2/calyculin A
Comments/Corrections

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