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We investigated GABABR-mediated modulation by Vc1.1, a cyclized form of Vc1.1 (c-Vc1.1), and the GABABR agonist baclofen of human Cav2.1 or Cav2.3 channels heterologously expressed in human embryonic kidney cells. 50 \u00b5M baclofen inhibited Cav2.1 and Cav2.3 channel Ba2+ currents by \u223c40%, whereas c-Vc1.1 did not affect Cav2.1 but potently inhibited Cav2.3, with a half-maximal inhibitory concentration of \u223c300 pM. Depolarizing paired pulses revealed that \u223c75% of the baclofen inhibition of Cav2.1 was voltage dependent and could be relieved by strong depolarization. In contrast, baclofen or Vc1.1 inhibition of Cav2.3 channels was solely mediated through voltage-independent pathways that could be disrupted by pertussis toxin, guanosine 5\u2032-[\u03b2-thio]diphosphate trilithium salt, or the GABABR antagonist CGP55845. Overexpression of the kinase c-Src significantly increased inhibition of Cav2.3 by c-Vc1.1. Conversely, coexpression of a catalytically inactive double mutant form of c-Src or pretreatment with a phosphorylated pp60c-Src peptide abolished the effect of c-Vc1.1. Site-directed mutational analyses of Cav2.3 demonstrated that tyrosines 1761 and 1765 within exon 37 are critical for inhibition of Cav2.3 by c-Vc1.1 and are involved in baclofen inhibition of these channels. Remarkably, point mutations introducing specific c-Src phosphorylation sites into human Cav2.1 channels conferred c-Vc1.1 sensitivity. Our findings show that Vc1.1 inhibition of Cav2.3, which defines Cav2.3 channels as potential targets for analgesic \u03b1-conotoxins, is caused by specific c-Src phosphorylation sites in the C terminus.<\/jats:p>","DOI":"10.1085\/jgp.201311104","type":"journal-article","created":{"date-parts":[[2014,3,31]],"date-time":"2014-03-31T15:50:03Z","timestamp":1396281003000},"page":"465-479","update-policy":"https:\/\/doi.org\/10.1085\/jgp.crossmarkpolicy","source":"Crossref","is-referenced-by-count":44,"title":["Differential Cav2.1 and Cav2.3 channel inhibition by baclofen and \u03b1-conotoxin Vc1.1 via GABAB receptor activation"],"prefix":"10.1085","volume":"143","author":[{"given":"G\u00e9za","family":"Berecki","sequence":"first","affiliation":[{"name":"Health Innovations Research Institute, RMIT University, Melbourne, Victoria 3083, Australia 1"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeffrey R.","family":"McArthur","sequence":"additional","affiliation":[{"name":"Health Innovations Research Institute, RMIT University, Melbourne, Victoria 3083, Australia 1"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hartmut","family":"Cuny","sequence":"additional","affiliation":[{"name":"Health Innovations Research Institute, RMIT University, Melbourne, Victoria 3083, Australia 1"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard J.","family":"Clark","sequence":"additional","affiliation":[{"name":"School of Biomedical Sciences, The University of Queensland, Brisbane, Queensland 4072, Australia 2"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David J.","family":"Adams","sequence":"additional","affiliation":[{"name":"Health Innovations Research Institute, RMIT University, Melbourne, Victoria 3083, Australia 1"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"291","published-online":{"date-parts":[[2014,3,31]]},"reference":[{"key":"2023072623164088700_bib1","doi-asserted-by":"publisher","first-page":"1619","DOI":"10.1016\/j.bbamem.2013.01.019","article-title":"Mechanisms of conotoxin inhibition of N-type (Cav2.2) calcium channels","volume":"1828","author":"Adams","year":"2013","journal-title":"Biochim. 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