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Volume 272, Number 22, Issue of May 30, 1997 pp. 14021-14024
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

COMMUNICATION:
Inactivation of a Voltagedependent K⁺ Channel by  Subunit
MODULATION BY A PHOSPHORYLATION-DEPENDENT INTERACTION BETWEEN THE DISTAL C TERMINUS OF  SUBUNIT AND CYTOSKELETON

(Received for publication, March 7, 1997, and in revised form, April 1, 1997)

Jie Jing , Tuvia Peretz , Dafna Singer-Lahat , Dodo Chikvashvili , William B. Thornhill and Ilana Lotan

From the Department of Physiology and Pharmacology, Sackler School of Medicine, Tel-Aviv University, 69978 Ramat Aviv, Israel and the  Department of Physiology and Biophysics, Mount Sinai School of Medicine, The Mount Sinai Hospital, New York, New York 10029-6574

Kv1.1/Kv1.1 () K⁺ channel expressed in Xenopus oocytes was shown to have a fast inactivating current component. The fraction of this component (extent of inactivation) is increased by microfilament disruption induced by cytochalasins or by phosphorylation of the  subunit at Ser-446, which impairs the interaction of the channel with microfilaments. The relevant sites of interaction on the channel molecules have not been identified. Using a phosphorylation-deficient mutant of , S446A, to ensure maximal basal interaction of the channel with the cytoskeleton, we show that one relevant site is the end of the C terminus of . Truncation of the last six amino acids resulted in channels with an extent of inactivation up to 2.5-fold larger and its further enhancement by cytochalasins being reduced 2-fold. The wild-type channels exhibited strong inactivation, which could not be markedly increased either by cytochalasins or by the C-terminal mutations, indicating that the interaction of the wild-type channels with microfilaments was minimal to begin with, presumably because of extensive basal phosphorylation. Since the C-terminal end of Kv1.1 was shown to participate in channel clustering via an interaction with members of the PSD-95 family of proteins, we propose that a similar interaction with an endogenous protein takes place, contributing to channel connection to the oocyte cytoskeleton. This is the first report to assign a modulatory role to such an interaction: together with the state of phosphorylation of the channel, it regulates the extent of inactivation conferred by the  subunit.

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