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Volume 271, Number 43, Issue of October 25, 1996 pp. 26698-26705
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Analysis of the Role of Calmodulin Binding and Sequestration in Neuromodulin (GAP-43) Function

(Received for publication, May 24, 1996, and in revised form, August 14, 1996)

Chantal Gamby ^§ , Martha C. Waage , Richard G. Allen ^¶ and Lawrence Baizer

From the  R. S. Dow Neurological Sciences Institute, Good Samaritan Hospital and Medical Center, Portland, Oregon 97209 and the ^§ Department of Cell Biology and Anatomy and the ^¶ Center for Research on Occupational and Environmental Toxicology, Oregon Health Sciences University, Portland, Oregon 97201

We demonstrated previously that forced expression of the neuronal phosphoprotein neuromodulin (also known as GAP-43, F1, B-50, and p57) in mouse anterior pituitary AtT-20 cells enhances depolarization-mediated secretion and alters cellular morphology. Here we analyze the role of calmodulin binding by neuromodulin in these responses. In cells expressing wild-type neuromodulin, a complex with calmodulin that is sensitive to intracellular calcium and phosphorylation is localized to the plasma membrane. Transfection of several mutant forms of neuromodulin shows that the effects of this protein on secretion are dependent on both calmodulin binding and association with the plasma membrane. In contrast, the morphological changes depend only on membrane association. Thus, the multitude of effects of neuromodulin noted in previous studies may result from divergent properties of this protein.

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