Document Detail

Phosphorylation of brush border myosin by brush border calmodulin-dependent myosin heavy and light chain kinases.
MedLine Citation:
PMID:  2959565     Owner:  NLM     Status:  MEDLINE    
Calmodulin-dependent myosin light chain kinase isolated from chicken intestinal brush border phosphorylates brush border myosin at an apparently single serine identical to that phosphorylated by smooth muscle myosin light chain kinase. Phosphorylation to 1.8 mol phosphate/mol myosin activated the myosin actin-activated ATPase about 10-fold, to about 50 nmol/min per mg. Myosin phosphorylated on its light chains could then be further phosphorylated to a total of 3.2 mol phosphate per mol by brush border calmodulin-dependent heavy chain kinase. Heavy chain phosphorylation did not alter the actin-activated ATPase of either myosin prephosphorylated on its light chains or of unphosphorylated myosin.
J P Rieker; J H Collins
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  FEBS letters     Volume:  223     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1987 Nov 
Date Detail:
Created Date:  1987-12-09     Completed Date:  1987-12-09     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  262-6     Citation Subset:  IM    
Department of Microbiology, Biochemistry and Molecular Biology, School of Medicine, University of Pittsburgh, PA 15261.
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MeSH Terms
Actins / physiology
Adenosine Triphosphatases / metabolism
Calmodulin / physiology*
Intestinal Mucosa / metabolism
Microvilli / metabolism
Muscle, Smooth
Myosin-Light-Chain Kinase / metabolism*
Myosins / metabolism*
Structure-Activity Relationship
Grant Support
Reg. No./Substance:
0/Actins; 0/Calmodulin; EC Kinase; EC 3.6.1.-/Adenosine Triphosphatases; EC

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

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