{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,10]],"date-time":"2026-04-10T02:45:21Z","timestamp":1775789121378,"version":"3.50.1"},"reference-count":24,"publisher":"Oxford University Press (OUP)","issue":"13","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2006,7,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Membrane-embedded voltage-activated potassium channels (Kv) bind intracellular scaffold proteins, such as the Post Synaptic Density 95 (PSD-95) protein, using a conserved PDZ-binding motif located at the channels' C-terminal tip. This interaction underlies Kv-channel clustering, and is important for the proper assembly and functioning of the synapse. Here we demonstrate that the C-terminal segments of Kv channels adjacent to the PDZ-binding motif are intrinsically disordered. Phylogenetic analysis of the Kv channel family reveals a cluster of channel sequences belonging to three out of the four main channel families, for which an association is demonstrated between the presence of the consensus terminal PDZ-binding motif and the intrinsically disordered nature of the immediately adjacent C-terminal segment. Our observations, combined with a structural analogy to the N-terminal intra-molecular ball-and-chain mechanism for Kv channel inactivation, suggest that the C-terminal disordered segments of these channel families encode an inter-molecular fishing rod-like mechanism for K+ channel binding to scaffold proteins.<\/jats:p>\n               <jats:p>Contact: \u00a0ofery@bgu.ac.il<\/jats:p>\n               <jats:p>Supplementary information: Supplementary data are available at Bioinformatics online.<\/jats:p>","DOI":"10.1093\/bioinformatics\/btl137","type":"journal-article","created":{"date-parts":[[2006,4,7]],"date-time":"2006-04-07T00:24:36Z","timestamp":1144369476000},"page":"1546-1550","source":"Crossref","is-referenced-by-count":39,"title":["Intrinsically disordered C-terminal segments of voltage-activated potassium channels: a possible fishing rod-like mechanism for channel binding to scaffold proteins"],"prefix":"10.1093","volume":"22","author":[{"given":"Elhanan","family":"Magidovich","sequence":"first","affiliation":[{"name":"Department of Life Sciences and the Zlotowski Center for Neurosciences, Ben Gurion University of the Negev 1 \u00a0 1 \u00a0 \u00a0 Beer Sheva, Israel"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sarel J.","family":"Fleishman","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Tel Aviv University 2 \u00a0 2 \u00a0 \u00a0 Ramat Aviv, Israel"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ofer","family":"Yifrach","sequence":"additional","affiliation":[{"name":"Department of Life Sciences and the Zlotowski Center for Neurosciences, Ben Gurion University of the Negev 1 \u00a0 1 \u00a0 \u00a0 Beer Sheva, Israel"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2006,6,4]]},"reference":[{"key":"2023012408323256800_b1","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1152\/physrev.2000.80.2.555","article-title":"The voltage sensor in voltage-dependent ion channels","volume":"80","author":"Bezanilla","year":"2000","journal-title":"Physiol. 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