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The role of microtubules and inositol triphosphate induced Ca2+ release in the tyrosine phosphorylation of mitogen-activated protein kinase in extracts of Xenopus laevis oocytes

Published online by Cambridge University Press:  26 September 2008

N.S. Duesbery  and
Y. Masui
N.S. Duesbery*
Affiliation:
Department of Zoology, University of Toronto, Toronto, Canada
Y. Masui
Affiliation:
Department of Zoology, University of Toronto, Toronto, Canada
*
N.S. Duesbery, Department of Zoology, University of Toronto, Toronto, Canada M5S 1A1. Telephone: (416) 978-3493. Fax; (416) 978-8532 e-mail: duesbery@zoo.toronto.edu.
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Summary

Microsomal fractions of Xenopus oocytes release preloaded 45Ca2+ when treated with inositol triphosphate (InsP3). The effective concentration of InsP3 required for half-maximal release (EC50) is 59 nM and maximal release occurs at ∼ 2 μM InsP3. Uptake and release of 45Ca2+ are not altered by the catalytic subunit of protein kinase A, dibutyrl cyclic adenosine monophosphate, protein kinase A peptide inhibitor or nocodazole. In contrast, taxol decreases the sensitivity of the microsomal fraction to InsP3, shifting the EC50 for InsP3-induced Ca2+ release from 59 to 259 nM. In lysates of oocytes, InsP3-induced Ca2+ release causes the tyrosine phorphorylation of a 42000 (Mr 42k) protein identified as 42k mitogen-activated protein (MAP) kinase. InsP3-induced tyrosine phosphorylation of MAP kinase is prevented by BAPTA and taxol, but not by nocodazole. Thus, microtubule polymerisation modifies InsP3-induced Ca2+ release, thereby inhibiting phosphorylation of MAP kinase.

Keywords

Ca2+MAP kinaseMaturationMicrotubulesXenopus

Information

Type
Article
Information
Zygote , Volume 4 , Issue 1 , February 1996 , pp. 21 - 30
Copyright
Copyright © Cambridge University Press 1996

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