Document Detail


Regulation of p68 RNA helicase by calmodulin and protein kinase C.
MedLine Citation:
PMID:  7525583     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Human p68 RNA helicase is a nuclear RNA-dependent ATPase that belongs to a family of putative helicases known as the DEAD box proteins. These proteins have been implicated in aspects of RNA function including translation initiation, splicing, and ribosome assembly in a variety of organisms ranging from Escherichia coli to humans. While members of this family are believed to function in the manipulation of RNA secondary structure, little is known about the regulation of these enzymes. By immunological methods and sequence comparison, we have found that p68 possesses a region of sequence similarity to the conserved protein kinase C phosphorylation site and calmodulin binding domain (also known as the IQ domain) of the neural-specific proteins neuromodulin (GAP-43) and neurogranin (RC3). We report that p68 is phosphorylated by protein kinase C in vitro and binds calmodulin in a Ca(2+)-dependent manner. Both phosphorylation and calmodulin binding inhibited p68 ATPase activity, suggesting that the RNA unwinding activity of p68 may be regulated by dual Ca2+ signal transduction pathways through its IQ domain.
Authors:
M K Buelt; B J Glidden; D R Storm
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  269     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1994 Nov 
Date Detail:
Created Date:  1994-12-28     Completed Date:  1994-12-28     Revised Date:  2012-06-27    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  29367-70     Citation Subset:  IM    
Affiliation:
Department of Pharmacology, University of Washington, Seattle 98195.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphatases / antagonists & inhibitors
Animals
Antibodies / immunology
CHO Cells
Calmodulin / physiology*
Calmodulin-Binding Proteins / immunology
Cricetinae
Cross Reactions
DEAD-box RNA Helicases
Humans
Nerve Tissue Proteins / immunology
Neurogranin
Nuclear Proteins / antagonists & inhibitors,  metabolism*
PC12 Cells
Phosphorylation
Protein Binding
Protein Kinase C / physiology*
Protein Kinases*
RNA / metabolism
RNA Helicases
RNA Nucleotidyltransferases / antagonists & inhibitors,  metabolism*
Rats
Grant Support
ID/Acronym/Agency:
NS 31496/NS/NINDS NIH HHS; NS09174/NS/NINDS NIH HHS
Chemical
Reg. No./Substance:
0/Antibodies; 0/Calmodulin; 0/Calmodulin-Binding Proteins; 0/NRGN protein, human; 0/Nerve Tissue Proteins; 0/Nrgn protein, rat; 0/Nuclear Proteins; 132654-77-4/Neurogranin; 63231-63-0/RNA; EC 2.7.-/Protein Kinases; EC 2.7.11.13/Protein Kinase C; EC 2.7.7.-/RNA Helicases; EC 2.7.7.-/RNA Nucleotidyltransferases; EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.1.-/DEAD-box RNA Helicases; EC 3.6.1.-/Ddx5 protein, human; EC 3.6.4.13/Ddx5 protein, rat

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


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