Document Detail

Regulation of the phosphorylation state and microtubule-binding activity of Tau by protein phosphatase 2A.
MedLine Citation:
PMID:  8982166     Owner:  NLM     Status:  MEDLINE    
Recently, we reported that a pool of protein phosphatase 2A (PP2A) is associated with microtubules. Here, we demonstrate that specific isoforms of PP2A bind and dephosphorylate the neuronal microtubule-associated protein tau. Coexpression of tau and SV40 small t, a specific inhibitor of PP2A, in CV-1, NIH 3T3, or NT2 cells induced the phosphorylation of tau at multiple sites, including Ser-199, Ser-202, Thr-205, Ser-396, and Ser-404. Immunofluorescent and biochemical analyses revealed that hyperphosphorylation correlated with dissociation of tau from microtubules and a loss of tau-induced microtubule stabilization. Taken together, these results support the hypothesis that PP2A controls the phosphorylation state of tau in vivo.
E Sontag; V Nunbhakdi-Craig; G Lee; G S Bloom; M C Mumby
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Neuron     Volume:  17     ISSN:  0896-6273     ISO Abbreviation:  Neuron     Publication Date:  1996 Dec 
Date Detail:
Created Date:  1997-01-27     Completed Date:  1997-01-27     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  8809320     Medline TA:  Neuron     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1201-7     Citation Subset:  IM    
Department of Pharmacology, University of Texas, Southwestern Medical Center, Dallas 75235, USA.
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MeSH Terms
3T3 Cells
Cell Line
Drug Stability
Isoenzymes / metabolism
Microtubules / metabolism*
Phosphoprotein Phosphatases / metabolism*
Protein Phosphatase 2
tau Proteins / chemistry,  immunology,  metabolism*
Grant Support
Reg. No./Substance:
0/Epitopes; 0/Isoenzymes; 0/tau Proteins; EC Phosphatases; EC Phosphatase 2

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