Mechanism of endogenous phosphorylation of microtubule proteins during GTP-induced microtubule assembly and implications for stability of the assembled structures

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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Differential phosphorylation of microtubule proteins by ATP and GTP

Diaz-Nido

Serrano

Ávila

1988

Mol Cell Biochem

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Mechanism of endogenous phosphorylation of microtubule proteins during GTP-induced microtubule assembly and implications for stability of the assembled structures

Cited by 1 publication

References 21 publications

Differential phosphorylation of microtubule proteins by ATP and GTP

Differential phosphorylation of microtubule proteins by ATP and GTP

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