Journal
JOURNAL OF GENERAL PHYSIOLOGY
Volume 150, Issue 5, Pages 683-696Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1085/jgp.201812064
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Funding
- Montana State University
- National Institute of General Medical Science of the National Institutes of Health [R01GM111685, P20GM103474]
- Fondation pour la Recherche Medicale Equipe FRM [DEQ20170336753]
- ATIP-AVE NIR grants
- Fondation NRJ-Institut de France
- Agence Nationale de la Recherche [ANR-11LABX-0015-01]
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Multimerization is a key characteristic of most voltage-sensing proteins. The main exception was thought to be the Ciona intestinalis voltage-sensing phosphatase (Ci-VSP). In this study, we show that multimerization is also critical for Ci-VSP function. Using coimmunoprecipitation and single-molecule pull-down, we find that Ci-VSP stoichiometry is flexible. It exists as both monomers and dimers, with dimers favored at higher concentrations. We show strong dimerization via the voltage-sensing domain (VSD) and weak dimerization via the phosphatase domain. Using voltage-clamp fluorometry, we also find that VSDs cooperate to lower the voltage dependence of activation, thus favoring the activation of Ci-VSP. Finally, using activity assays, we find that dimerization alters Ci-VSP substrate specificity such that only dimeric Ci-VSP is able to dephosphorylate the 3-phosphate from P1(3,4,5)P-3 or P1(3,4)P-2. Our results indicate that dimerization plays a significant rote in Ci-VSP function.
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