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dc.contributor.authorRatzan, Wil
dc.contributor.authorRayaprolu, Vamseedhar
dc.contributor.authorKillian, Scott E.
dc.contributor.authorBradley, Roger
dc.contributor.authorKohout, Susy C.
dc.date.accessioned2019-06-07T19:24:25Z
dc.date.available2019-06-07T19:24:25Z
dc.date.issued2019-04
dc.identifier.citationRatzan, Wil, Vamseedhar Rayaprolu, Scott E. Killian, Roger Bradley, and Susy C. Kohout. "The voltage sensing phosphatase (VSP) localizes to the apical membrane of kidney tubule epithelial cells." PLoS One 14, no. 4 (April 2019). DOI:10.1371/journal.pone.0209056.en_US
dc.identifier.issn1932-6203
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/15493
dc.description.abstractVoltage-sensing phosphatases (VSPs) are transmembrane proteins that couple changes in membrane potential to hydrolysis of inositol signaling lipids. VSPs catalyze the dephosphorylation of phosphatidylinositol phosphates (PIPs) that regulate diverse aspects of cell membrane physiology including cell division, growth and migration. VSPs are highly conserved among chordates, and their RNA transcripts have been detected in the adult and embryonic stages of frogs, fish, chickens, mice and humans. However, the subcellular localization and biological function of VSP remains unknown. Using reverse transcriptase-PCR (RT-PCR), we show that both Xenopus laevis VSPs (Xl-VSP1 and Xl-VSP2) mRNAs are expressed in early embryos, suggesting that both Xl-VSPs are involved in early tadpole development. To understand which embryonic tissues express Xl-VSP mRNA, we used in situ hybridization (ISH) and found Xl-VSP mRNA in both the brain and kidney of NF stage 32-36 embryos. By Western blot analysis with a VSP antibody, we show increasing levels of Xl-VSP protein in the developing embryo, and by immunohistochemistry (IHC), we demonstrate that Xl-VSP protein is specifically localized to the apical membrane of both embryonic and adult kidney tubules. We further characterized the catalytic activity of both Xl-VSP homologs and found that while Xl-VSP1 catalyzes 3- and 5-phosphate removal, Xl-VSP2 is a less efficient 3-phosphatase with different substrate specificity. Our results suggest that Xl-VSP1 and Xl-VSP2 serve different functional roles and that VSPs are an integral component of voltage-dependent PIP signaling pathways during vertebrate kidney tubule development and function.en_US
dc.description.sponsorshipVice President for Research, Creativity and Technology Transfer at Montana State University; Fund for Science; NIH National Institute of General Medical Science grants R01GM111685, P20GM103474en_US
dc.rightsCC BY: This license lets you distribute, remix, tweak, and build upon this work, even commercially, as long as you credit the original creator for this work. This is the most accommodating of licenses offered. Recommended for maximum dissemination and use of licensed materials.en_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/legalcodeen_US
dc.titleThe voltage sensing phosphatase (VSP) localizes to the apical membrane of kidney tubule epithelial cellsen_US
dc.typeArticleen_US
mus.citation.issue4en_US
mus.citation.journaltitlePLoS Oneen_US
mus.citation.volume14en_US
mus.identifier.categoryHealth & Medical Sciencesen_US
mus.identifier.categoryLife Sciences & Earth Sciencesen_US
mus.identifier.doi10.1371/journal.pone.0209056en_US
mus.relation.collegeCollege of Letters & Scienceen_US
mus.relation.departmentCell Biology & Neuroscience.en_US
mus.relation.universityMontana State University - Bozemanen_US
mus.data.thumbpage7


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CC BY: This license lets you distribute, remix, tweak, and build upon this work, even commercially, as long as you credit the original creator for this work. This is the most accommodating of licenses offered. Recommended for maximum dissemination and use of licensed materials.
Except where otherwise noted, this item's license is described as CC BY: This license lets you distribute, remix, tweak, and build upon this work, even commercially, as long as you credit the original creator for this work. This is the most accommodating of licenses offered. Recommended for maximum dissemination and use of licensed materials.