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J Biol Chem, Vol. 274, Issue 35, 24445-24448, August 27, 1999

COMMUNICATION
Calmodulin Binds to p21^Cip1 and Is Involved in the Regulation of Its Nuclear Localization

Marta Taulés, Aina Rodríguez-Vilarrupla, Eulàlia Rius, Josep M. Estanyol, Oriol Casanovas, David B. Sacks^¶, Enrique Pérez-Payá, Oriol Bachs, and Neus Agell

From the  Departament de Biologia Cel.lular i Anatomia Patològica, Institut d'Investigacions Biomèdiques August Pi i Sunyer (IDIBAPS), Facultat de Medicina, Universitat de Barcelona, 08036 Barcelona, Spain, the ^¶ Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115, and the  Departamento de Bioquímica y Biología Molecular, Universidad de Valencia, E-46100 Burjassot, Valencia, Spain

p21^Cip1, first described as an inhibitor of cyclin-dependent kinases, has recently been shown to have a function in the formation of cyclin D-Cdk4 complexes and in their nuclear translocation. The dual behavior of p21^Cip1 may be due to its association with other proteins. Different evidence presented here indicate an in vitro and in vivo interaction of p21^Cip1 with calmodulin: 1) purified p21^Cip1 is able to bind to calmodulin-Sepharose in a Ca²⁺-dependent manner, and this binding is inhibited by the calmodulin-binding domain of calmodulin-dependent kinase II; 2) both molecules coimmunoprecipitate when extracted from cellular lysates; and 3) colocalization of calmodulin and p21^Cip1 can be detected in vivo by electron microscopy immunogold analysis. The carboxyl-terminal domain of p21^Cip1 is responsible for the calmodulin interaction, since p21^145-164 peptide is also able to bind calmodulin and to compete with full-length p21^Cip1 for the calmodulin binding. Because treatment of cells with anti-calmodulin drugs decreases the nuclear accumulation of p21^Cip1, we hypothesize that calmodulin interaction with p21^Cip1 is important for p21^Cip1, and in consequence for cyclin D-Cdk4, translocation into the cell nucleus.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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