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J. Biochem, 1986, Vol. 99, No. 2 521-525
© 1986 Japanese Biochemical Society

other

On the Mechanism of Calmodulin-Induced Inhibition of Microtubule Assembly In Vitro1

Hiromichi KUMAGAI2, Eisuke NISHIDA3, Susumu KOTANI and Hikoichi SAKAI

Department of Biophysics and Biochemistry, Faculty of Science, The University of Tokyo Hongo, Bunkyo-ku, Tokyo 113

3 To whom correspondence should be addressed

Binding of calmodulin to microtubule-associated proteins (MAPs) was analyzed by the equilibrium gel filtration method. The apparent dissociation constant (Kd) of calmodulin binding was found to be 2 µM for tau, and 5 µM for MAP2. These Kd values were similar to the Kd previously determined for calmodulin binding to tubulin. The inhibitory effect of increasing concentrations of calmodulin on the kinetics of microtubule assembly from tau and tubulin was not mimicked by decreasing the concentration of tau alone or tubulin alone. These results suggest that calmodulin inhibits microtubule assembly by its binding to both MAPs and tubulin.

1 This work was supported in part by Grants-in-Aid from the Ministry of Education, Science and Culture of Japan (Nos. 57440004, 57380016, and 59390006).

2 Present address: Department of Metabolism, National Center for Nervous, Mental, and Muscular Disorders, Kodaira, Tokyo 187.


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