{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,9]],"date-time":"2026-01-09T15:43:56Z","timestamp":1767973436350,"version":"3.49.0"},"reference-count":15,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2022,1,3]],"date-time":"2022-01-03T00:00:00Z","timestamp":1641168000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2022,1,3]],"date-time":"2022-01-03T00:00:00Z","timestamp":1641168000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Mol Brain"],"published-print":{"date-parts":[[2022,12]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Voltage-gated calcium channels are essential regulators of brain function where they support depolarization-induced calcium entry into neurons. They consist of a pore-forming subunit (Ca<jats:sub>v<\/jats:sub>\u03b1<jats:sub>1<\/jats:sub>) that requires co-assembly with ancillary subunits to ensure proper functioning of the channel. Among these ancillary subunits, the Ca<jats:sub>v<\/jats:sub>\u03b2 plays an essential role in regulating surface expression and gating of the channels. This regulation requires the direct binding of Ca<jats:sub>v<\/jats:sub>\u03b2 onto Ca<jats:sub>v<\/jats:sub>\u03b1<jats:sub>1<\/jats:sub> and is mediated by the alpha interacting domain (AID) within the Ca<jats:sub>v<\/jats:sub>\u03b1<jats:sub>1<\/jats:sub> subunit and the \u03b1 binding pocket (ABP) within the Ca<jats:sub>v<\/jats:sub>\u03b2 subunit. However, additional interactions between Ca<jats:sub>v<\/jats:sub>\u03b1<jats:sub>1<\/jats:sub> and Ca<jats:sub>v<\/jats:sub>\u03b2 have been proposed. In this study, we analyzed the importance of Ca<jats:sub>v<\/jats:sub>\u03b2<jats:sub>3<\/jats:sub> surface charged residues in the regulation of Ca<jats:sub>v<\/jats:sub>2.1 channels. Using alanine-scanning mutagenesis combined with electrophysiological recordings we identified several amino acids within the Ca<jats:sub>v<\/jats:sub>\u03b2<jats:sub>3<\/jats:sub> subunit that contribute to the gating of the channel. These findings add to the notion that additional contacts besides the main AID\/ABP interaction may occur to fine-tune the expression and properties of the channel.<\/jats:p>","DOI":"10.1186\/s13041-021-00887-3","type":"journal-article","created":{"date-parts":[[2022,1,3]],"date-time":"2022-01-03T10:04:48Z","timestamp":1641204288000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Cav\u03b2 surface charged residues contribute to the regulation of neuronal calcium channels"],"prefix":"10.1186","volume":"15","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8522-1088","authenticated-orcid":false,"given":"Alexandra","family":"Tran-Van-Minh","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2782-9615","authenticated-orcid":false,"given":"Michel","family":"De Waard","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0040-1109","authenticated-orcid":false,"given":"Norbert","family":"Weiss","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2022,1,3]]},"reference":[{"issue":"4","key":"887_CR1","doi-asserted-by":"publisher","first-page":"821","DOI":"10.1124\/pr.114.009654","volume":"67","author":"GW Zamponi","year":"2015","unstructured":"Zamponi GW, Striessnig J, Koschak A, Dolphin AC. The physiology, pathology, and pharmacology of voltage-gated calcium channels and their future therapeutic potential. Pharmacol Rev. 2015;67(4):821\u201370.","journal-title":"Pharmacol Rev"},{"issue":"7","key":"887_CR2","doi-asserted-by":"publisher","first-page":"1530","DOI":"10.1016\/j.bbamem.2012.08.028","volume":"1828","author":"Z Buraei","year":"2013","unstructured":"Buraei Z, Yang J. Structure and function of the \u03b2 subunit of voltage-gated Ca2+ channels. Biochim Biophys Acta. 2013;1828(7):1530\u201340.","journal-title":"Biochim Biophys Acta"},{"issue":"6466","key":"887_CR3","doi-asserted-by":"publisher","first-page":"67","DOI":"10.1038\/368067a0","volume":"368","author":"M Pragnell","year":"1994","unstructured":"Pragnell M, De Waard M, Mori Y, Tanabe T, Snutch TP, Campbell KP. Calcium channel beta-subunit binds to a conserved motif in the I-II cytoplasmic linker of the alpha 1-subunit. 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