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dc.contributor.authorKruse, Martin
dc.contributor.authorKohout, Susy C.
dc.contributor.authorHille, Bertil
dc.date.accessioned2019-03-05T15:32:56Z
dc.date.available2019-03-05T15:32:56Z
dc.date.issued2019-02
dc.identifier.citationKruse, Martin, Susy C. Kohout, and Bertil Hille. "Reinterpretation of the substrate specificity of the voltage-sensing phosphatase during dimerization." Journal of General Physiology 151, no. 2 (February 2019): 258-263. DOI:10.1085/jgp.201812260.en_US
dc.identifier.issn1540-7748
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/15310
dc.description.abstractVoltage-sensing phosphatases (VSPs) cleave both 3- and 5-phosphates from inositol phospholipids in response to membrane depolarization. When low concentrations of Ciona intestinalis VSP are expressed in Xenopus laevis oocytes, the 5-phosphatase reaction can be observed during large membrane depolarizations. When higher concentrations are expressed, the 5-phosphatase activity is observed with smaller depolarizations, and the 3-phosphatase activity is revealed with strong depolarization. Here we ask whether this apparent induction of 3-phosphatase activity is attributable to the dimerization that has been reported when VSP is expressed at higher concentrations. Using a simple kinetic model, we show that these enzymatic phenomena can be understood as an emergent property of a voltage-dependent enzyme with invariant substrate selectivity operating in the context of endogenous lipid-metabolizing enzymes present in oocytes. Thus, a switch of substrate specificity with dimerization need not be invoked to explain the appearance of 3-phosphatase activity at high VSP concentrations.en_US
dc.description.sponsorshipNational Institutes of Health; National Institute of General Medical Sciences grant R01GM111685; NIH National Institute of Neurological Disorders and Stroke grant R37-NS08174-50; NIH National Institute of General Medical Sciences grant P41GM103313en_US
dc.language.isoenen_US
dc.rightsCC BY-NC-SA: This license lets you remix, tweak, and build upon this work non-commercially, as long as you give credit to the original creator and license your new creations under the identical terms.en_US
dc.rights.urihttps://creativecommons.org/licenses/by-nc-sa/4.0/legalcodeen_US
dc.titleReinterpretation of the substrate specificity of the voltage-sensing phosphatase during dimerizationen_US
dc.typeArticleen_US
mus.citation.extentfirstpage258en_US
mus.citation.extentlastpage263en_US
mus.citation.issue2en_US
mus.citation.journaltitleJournal of General Physiologyen_US
mus.citation.volume151en_US
mus.identifier.categoryHealth & Medical Sciencesen_US
mus.identifier.doi10.1085/jgp.201812260en_US
mus.relation.collegeCollege of Agricultureen_US
mus.relation.departmentMicrobiology & Cell Biology.en_US
mus.relation.universityMontana State University - Bozemanen_US
mus.data.thumbpage4en_US
mus.contributor.orcidKohout, Susy C.|0000-0002-8159-8934en_US


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