Document Detail


Kinase-Kinase Interaction and Modulation of Tau Phosphorylation.
MedLine Citation:
PMID:  23273861     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
The microtubule (MT)-associated protein tau attaches to neuronal MT networks and regulates their integrity. The phosphorylation state of tau alters its binding activity. MT integrity is maintained by the phosphorylation state of tau, which is under the control of the kinase-phosphatase balance. This control requires the proper regulation of topographical and temporal characteristics of tau kinases and phosphatases. The tau phosphorylation protein complex (TPPC) anchors tau kinases and phosphatases via scaffold proteins, tau effectors, and tau itself. Targeting these proteins in TPPC fulfills the topographical requirements for maintaining MT functions. The switching of tau kinase activity determines the order of the kinase action. The combined action of kinases is temporally modulated; reversal of the time order of events results in a differential state of tau phosphorylation. Elucidation of protein-protein interaction in the regulation of tau phosphorylation will shed light on the physiology and pathology of tau phosphorylation.
Authors:
Mitsuko Hashiguchi; Toshio Hashiguchi
Publication Detail:
Type:  JOURNAL ARTICLE    
Journal Detail:
Title:  International review of cell and molecular biology     Volume:  300C     ISSN:  1937-6448     ISO Abbreviation:  Int Rev Cell Mol Biol     Publication Date:  2013  
Date Detail:
Created Date:  2012-12-31     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101475846     Medline TA:  Int Rev Cell Mol Biol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  121-160     Citation Subset:  -    
Copyright Information:
Copyright © 2013 Elsevier Inc. All rights reserved.
Affiliation:
Department of Physiology, Tokyo Medical University, Shinjuku, Tokyo, Japan.
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