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Volume 272, Number 20, Issue of May 16, 1997 pp. 12885-12888
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

COMMUNICATION:
Clustering and Enhanced Activity of an Inwardly Rectifying Potassium Channel, Kir4.1, by an Anchoring Protein, PSD-95/SAP90

(Received for publication, November 11, 1996, and in revised form, February 14, 1997)

Yoshiyuki Horio Dagger , Hiroshi Hibino Dagger , Atsushi Inanobe § , Mitsuhiko Yamada Dagger , Masaru Ishii Dagger , Yoshihiko Tada Dagger , Eisaku Satoh Dagger , Yutaka Hata par , Yoshimi Takai par ** and Yoshihisa Kurachi Dagger §

From the Dagger  Department of Pharmacology II, ** Department of Molecular Biology and Biochemistry, Faculty of Medicine, Osaka University, Suita, Osaka 565, Japan, the § Department of Cell Signaling, Yamagata University School of Medicine, Yamagata 993-23, Japan, the  Department of Pharmacology, Akita University School of Medicine, Akita 010, Japan, and the par  Takai Biotimer Project, ERATO, Japan Science and Technology Corporation, Kobe 651-22, Japan

An inwardly rectifying potassium channel predominantly expressed in glial cells, Kir4.1/KAB-2, has a sequence of Ser-Asn-Val in its carboxyl-terminal end, suggesting a possible interaction with an anchoring protein of the PSD-95 family. We examined the effects of PSD-95 on the distribution and function of Kir4.1 in a mammalian cell line. When Kir4.1 was expressed alone, the channel immunoreactivity was distributed homogeneously. In contrast, when co-expressed with PSD-95, prominent clustering of Kir4.1 in the cell membrane occurred. Kir4.1 was co-immunoprecipitated with PSD-95 in the co-expressed cells. Glutathione S-transferase-fusion protein of COOH terminus of Kir4.1 bound to PSD-95. These interactions disappeared when the Ser-Asn-Val motif was deleted. The magnitude of whole-cell Kir4.1 current was increased by 2-fold in cells co-expressing Kir4.1 and PSD-95 compared with cells expressing Kir4.1 alone. SAP97, another member of the PSD-95 family, showed similar effects on Kir4.1. Furthermore, we found that Kir4.1 as well as SAP97 distributed not diffusely but clustered in retinal glial cells. Therefore, PSD-95 family proteins may be a physiological regulator of the distribution and function of Kir4.1 in glial cells.


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Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.