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However, the apparent affinity for Ca2+ of its physiologically relevant form (myristoylated recoverin) is almost two orders of magnitude too low to support this mechanism in vivo. In this work, we compared the individual and synergistic roles of the myristic moiety, the GRK1 target and the disc membrane in modulating the calcium sensitivity of Rec. We show that the sole presence of the target or the disc membrane alone are not sufficient to achieve a physiological response to changes in intracellular [Ca2+]. Instead, the simultaneous presence of GRK1 and membrane allows the T to R transition to occur in a physiological range of [Ca2+] with high cooperativity via a conformational selection mechanism that drives the structural transitions of Rec in the presence of multiple ligands. Our conclusions may apply to other sensory transduction systems involving protein complexes and biological membranes.<\/jats:p>","DOI":"10.1098\/rsob.200346","type":"journal-article","created":{"date-parts":[[2021,1,6]],"date-time":"2021-01-06T03:11:31Z","timestamp":1609902691000},"update-policy":"https:\/\/doi.org\/10.1098\/crossmark-policy","source":"Crossref","is-referenced-by-count":7,"title":["Bringing the Ca2+ sensitivity of myristoylated recoverin into the physiological range"],"prefix":"10.1098","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7821-3717","authenticated-orcid":true,"given":"Valerio","family":"Marino","sequence":"first","affiliation":[{"name":"37134 Verona, Italy 1","department":["Department of Neurosciences, Biomedicine and Movement Sciences, Section of Biological Chemistry, University of Verona,"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matteo","family":"Riva","sequence":"additional","affiliation":[{"name":"37134 Verona, Italy 1","department":["Department of Neurosciences, Biomedicine and Movement Sciences, Section of Biological Chemistry, University of Verona,"]},{"name":"26111 Oldenburg, Germany 2","department":["Department of Neuroscience, Division of Biochemistry, University of Oldenburg,"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Davide","family":"Zamboni","sequence":"additional","affiliation":[{"name":"37134 Verona, Italy 1","department":["Department of Neurosciences, Biomedicine and Movement Sciences, Section of Biological Chemistry, University of Verona,"]},{"name":"26111 Oldenburg, Germany 2","department":["Department of Neuroscience, Division of Biochemistry, University of Oldenburg,"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1501-0044","authenticated-orcid":true,"given":"Karl-Wilhelm","family":"Koch","sequence":"additional","affiliation":[{"name":"26111 Oldenburg, Germany 2","department":["Department of Neuroscience, Division of Biochemistry, University of Oldenburg,"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3724-3044","authenticated-orcid":true,"given":"Daniele","family":"Dell'Orco","sequence":"additional","affiliation":[{"name":"37134 Verona, Italy 1","department":["Department of Neurosciences, Biomedicine and Movement Sciences, Section of Biological Chemistry, University of Verona,"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"175","published-online":{"date-parts":[[2021,1,6]]},"reference":[{"key":"2026010717190542500_RSOB200346C1","doi-asserted-by":"crossref","first-page":"1205","DOI":"10.1016\/j.bbagen.2011.10.003","article-title":"Molecular structure and target recognition of neuronal calcium sensor proteins","volume":"1820","author":"Ames","year":"2012","journal-title":"Biochim. 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