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. 1995 Nov 2;378(6552):85-8.
doi: 10.1038/378085a0.

Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases

E Kim  1 , M Niethammer, A Rothschild, Y N Jan, M Sheng
Affiliations

Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases

E Kim et al. Nature. .

Abstract

ANCHORING of ion channels at specific subcellular sites is critical for neuronal signalling, but the mechanisms underlying channel localization and clustering are largely unknown (reviewed in ref. 1). Voltage-gated K+ channels are concentrated in various neuronal domains, including presynaptic terminals, nodes of Ranvier and dendrites, where they regulate local membrane excitability. Here we present functional and biochemical evidence that cell-surface clustering of Shaker-subfamily K+ channels is mediated by the PSD-95 family of membrane-associated putative guanylate kinases, as a result of direct binding of the carboxy-terminal cytoplasmic tails to the K+ channel subunits to two PDZ (also known as GLGF or DHR) domains in the PSD-95 protein. The ability of PDZ domains to function as independent modules for protein-protein interaction, and their presence in other junction-associated molecules (such as ZO-1 (ref. 3) and syntrophin), suggest that PDZ-domain-containing polypeptides may be widely involved in the organization of proteins at sites of membrane specialization.

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