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Differential phosphorylation of microtubule proteins by ATP and GTP

✍ Scribed by Javier Diaz-Nido; Luis Serrano; Jesus Avila


Book ID
104673524
Publisher
Springer
Year
1988
Tongue
English
Weight
507 KB
Volume
79
Category
Article
ISSN
0300-8177

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✦ Synopsis


Purified brain microtubule protein is phosphorylated by endogenous protein kinase activities in the presence of [gamma-32P] ATP or [gamma-32P] GTP. Here we show that certain microtubule-associated proteins are phosphorylated differently by GTP or ATP as direct phosphoryl donors, suggesting the presence of distinct kinase activities, with different specificities, associated with microtubule protein.


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## Abstract Phosphorylation of tau protein has been suggested as a major mechanism regulating its functions. In assembled brain microtubules, tau is phosphorylated, but additional phosphorylation can be induced in vitro. Supply of excess ATP alone was sufficient to reduce migration of tau on SDS ge