RGD Reference Report - Microtubule bundling by tau proteins in vivo: analysis of functional domains. - Rat Genome Database

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Microtubule bundling by tau proteins in vivo: analysis of functional domains.

Authors: Kanai, Y  Chen, J  Hirokawa, N 
Citation: Kanai Y, etal., EMBO J. 1992 Nov;11(11):3953-61.
RGD ID: 10047156
Pubmed: PMID:1396588   (View Abstract at PubMed)
PMCID: PMC556906   (View Article at PubMed Central)

Tau varies both in the N-terminal region (three types) and in the C-terminal repeated microtubule binding domain (two types), generating six isoforms through alternative splicing. To understand the differences between the isoforms and to determine which domains are important for microtubule bundling, we performed transfection studies on fibroblasts using tau isoforms and deletion mutants to quantify their ability to bundle microtubules. By comparing the isoforms, we found that a longer N-terminal region induced microtubule bundling more efficiently, but changes in the microtubule binding domain did not. Mutants lacking the proline rich region or the repeated domain did not bind to microtubules. Although all the other mutants could bind to and bundle microtubules, deletion in the N-terminal neutral region or the first half of the C-terminal tail caused a significant decrease in microtubule bundling, indicating the importance of these regions in microtubule bundling.




Cellular Component

  
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Original Reference(s)
MaptRatmicrotubule part_ofIDA PMID:1396588CACAO 


Genes (Rattus norvegicus)
Mapt  (microtubule-associated protein tau)