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J. Biol. Chem., Vol. 276, Issue 26, 23253-23261, June 29, 2001

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The Giant Protein AHNAK Is a Specific Target for the Calcium- and Zinc-binding S100B Protein
POTENTIAL IMPLICATIONS FOR Ca²⁺ HOMEOSTASIS REGULATION BY S100B^*

Benoit J. Gentil, Christian Delphin, Gaëlh Ouengue Mbele, Jean Christophe Deloulme, Myriam Ferro^§, Jérôme Garin^§, and Jacques Baudier^¶

From the  Département de Biologie Moléculaire et Structurale du Commissariat à l'Energie Atomic, INSERM EPI-0104 and ^§ Laboratoire de Chimie des Proteines DBMS-CP, CEN-G, 38054 Grenoble, France

Transformation of rat embryo fibroblast clone 6 cells by ras and temperature-sensitive p53val¹³⁵ is reverted by ectopic expression of the calcium- and zinc-binding protein S100B. In an attempt to define the molecular basis of the S100B action, we have identified the giant phosphoprotein AHNAK as the major and most specific Ca²⁺-dependent S100B target protein in rat embryo fibroblast cells. We next characterized AHNAK as a major Ca²⁺-dependent S100B target protein in the rat glial C6 and human U-87MG astrocytoma cell lines. AHNAK binds to S100B-Sepharose beads and is also recovered in anti-S100B immunoprecipitates in a strict Ca²⁺- and Zn²⁺-dependent manner. Using truncated AHNAK fragments, we demonstrated that the domains of AHNAK responsible for interaction with S100B correspond to repeated motifs that characterize the AHNAK molecule. These motifs show no binding to calmodulin or to S100A6 and S100A11. We also provide evidence that the binding of 2 Zn²⁺ equivalents/mol S100B enhances Ca²⁺-dependent S100B-AHNAK interaction and that the effect of Zn²⁺ relies on Zn²⁺-dependent regulation of S100B affinity for Ca²⁺. Taking into consideration that AHNAK is a protein implicated in calcium flux regulation, we propose that the S100B-AHNAK interaction may participate in the S100B-mediated regulation of cellular Ca²⁺ homeostasis.

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