{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,20]],"date-time":"2026-08-20T13:30:38Z","timestamp":1787232638197,"version":"build-2736575974"},"reference-count":26,"publisher":"American Chemical Society (ACS)","issue":"7","license":[{"start":{"date-parts":[[2007,1,1]],"date-time":"2007-01-01T00:00:00Z","timestamp":1167609600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2007,1,1]],"date-time":"2007-01-01T00:00:00Z","timestamp":1167609600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2007,1,1]],"date-time":"2007-01-01T00:00:00Z","timestamp":1167609600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2007,1,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>KCNE transmembrane peptides are a family of modulatory \u03b2-subunits that assemble with voltage-gated K+ channels, producing the diversity of potassium currents needed for proper function in a variety of tissues. Although all five KCNE transcripts have been found in cardiac and other tissues, it is unclear whether two different KCNE peptides can assemble with the same K+ channel to form a functional complex. Here, we describe the derivatization of a scorpion toxin that irreversibly inhibits KCNQ1 K+ channel complexes that contain a specific KCNE peptide. Using this KCNE sensor, we show that heteromeric complexes form, and the functional output from these complexes reveals a hierarchy in KCNE modulation of KCNQ1 channels: KCNE3 &amp;gt; KCNE1 \u226b KCNE4. Furthermore, our results demonstrate that KCNQ1\/KCNE1\/KCNE4 complexes also generate a slowly activating current that has been previously attributed to homomeric KCNQ1\/KCNE1 complexes, providing a potential functional role for KCNE4 peptides in the heart.<\/jats:p>","DOI":"10.1021\/cb700089s","type":"journal-article","created":{"date-parts":[[2007,6,30]],"date-time":"2007-06-30T07:58:22Z","timestamp":1183190302000},"page":"00-00","source":"Crossref","is-referenced-by-count":30,"title":["A Derivatized Scorpion Toxin Reveals the Functional Output of Heteromeric KCNQ1\u2013KCNE K+ Channel Complexes"],"prefix":"10.1021","volume":"2","author":[{"given":"Trevor J.","family":"Morin","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Pharmacology, Programs in Neuroscience and Chemical Biology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, Massachusetts 01605-2324"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William R.","family":"Kobertz","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Pharmacology, Programs in Neuroscience and Chemical Biology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, Massachusetts 01605-2324"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2007,1,1]]},"reference":[{"key":"2026082008283773900_micit1","doi-asserted-by":"publisher","first-page":"787","DOI":"10.1016\/j.neuropharm.2004.06.018","article-title":"The MinK-related peptides","volume":"47","author":"McCrossan","year":"2004","journal-title":"Neuropharmacology","ISSN":"https:\/\/id.crossref.org\/issn\/0028-3908","issn-type":"print"},{"key":"2026082008283773900_micit2","doi-asserted-by":"publisher","first-page":"15","DOI":"10.1016\/S0896-6273(03)00570-1","article-title":"Charybdotoxin binding in the IKs pore demonstrates two MinK subunits in each channel complex","volume":"40","author":"Chen","year":"2003","journal-title":"Neuron","ISSN":"https:\/\/id.crossref.org\/issn\/0896-6273","issn-type":"print"},{"key":"2026082008283773900_micit3","doi-asserted-by":"publisher","first-page":"34069","DOI":"10.1074\/jbc.273.51.34069","article-title":"MinK-KvLQT1 fusion proteins, evidence for multiple stoichiometries of the assembled IsK channel","volume":"273","author":"Wang","year":"1998","journal-title":"J. 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