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Synaptopodin Is a Coincidence Detector of Tyrosine versus Serine/Threonine Phosphorylation for the Modulation of Rho Protein Crosstalk in Podocytes

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dc.contributor.author최훈영-
dc.date.accessioned2017-11-02T08:39:15Z-
dc.date.available2017-11-02T08:39:15Z-
dc.date.issued2017-
dc.identifier.issn1046-6673-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/154722-
dc.description.abstractTyrosine and serine/threonine signal-transduction pathways influence many aspects of cell behavior, including the spatial and temporal regulation of the actin cytoskeleton. However, little is known about how input from diverse tyrosine and serine/threonine kinases is integrated to control Rho protein crosstalk and actin remodeling, which are critically important in podocyte health and disease. Here we unveil the proteolytically-regulated, actin organizing protein synaptopodin as a coincidence detector of tyrosine versus serine/threonine phosphorylation. We show that serine/threonine and tyrosine kinases duel for synaptopodin stability versus degradation. EGFR/Src-mediated tyrosine phosphorylation of synaptopodin in podocytes promotes binding to the serine/threonine phosphatase calcineurin. This leads to the loss of 14-3-3 binding, resulting in synaptopodin degradation, Vav2 activation, enhanced Rac1 signaling, and ultimate loss of stress fibers. Our studies reveal how synaptopodin, a single proteolytically-controlled protein, integrates antagonistic tyrosine versus serine/threonine phosphorylation events for the dynamic control of the actin cytoskeleton in podocytes.-
dc.description.statementOfResponsibilityrestriction-
dc.languageEnglish-
dc.publisherAmerican Society of Nephrology-
dc.relation.isPartOfJOURNAL OF THE AMERICAN SOCIETY OF NEPHROLOGY-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/2.0/kr/-
dc.subject.MESHAnimals-
dc.subject.MESHCalcineurin/metabolism-
dc.subject.MESHCells, Cultured-
dc.subject.MESHMice-
dc.subject.MESHMicrofilament Proteins/physiology*-
dc.subject.MESHPhosphorylation-
dc.subject.MESHPodocytes/physiology*-
dc.subject.MESHReceptor Cross-Talk-
dc.subject.MESHSerine/metabolism*-
dc.subject.MESHSignal Transduction-
dc.subject.MESHThreonine/metabolism*-
dc.subject.MESHTyrosine/metabolism*-
dc.subject.MESHrhoA GTP-Binding Protein/physiology*-
dc.titleSynaptopodin Is a Coincidence Detector of Tyrosine versus Serine/Threonine Phosphorylation for the Modulation of Rho Protein Crosstalk in Podocytes-
dc.typeArticle-
dc.publisher.locationUnited States-
dc.contributor.collegeCollege of Medicine-
dc.contributor.departmentDept. of Internal Medicine-
dc.contributor.googleauthorLisa Buvall-
dc.contributor.googleauthorHanna Wallentin-
dc.contributor.googleauthorJonas Sieber-
dc.contributor.googleauthorSvetlana Andreeva-
dc.contributor.googleauthorHoon Young Choi-
dc.contributor.googleauthorPeter Mundel-
dc.contributor.googleauthorAnna Greka-
dc.identifier.doi10.1681/ASN.2016040414-
dc.contributor.localIdA04226-
dc.relation.journalcodeJ01779-
dc.identifier.eissn1533-3450-
dc.identifier.pmid27628902-
dc.identifier.urlhttp://jasn.asnjournals.org/content/28/3/837.long-
dc.subject.keywordEGFR-
dc.subject.keywordFSGS-
dc.subject.keywordRac1-
dc.subject.keywordTRPC5-
dc.subject.keywordcytoskeleton-
dc.subject.keywordglomerular disease-
dc.contributor.alternativeNameChoi, Hoon Young-
dc.contributor.affiliatedAuthorChoi, Hoon Young-
dc.citation.titleJournal of the American Society of Nephrology-
dc.citation.volume28-
dc.citation.number3-
dc.citation.startPage837-
dc.citation.endPage851-
dc.identifier.bibliographicCitationJOURNAL OF THE AMERICAN SOCIETY OF NEPHROLOGY, Vol.28(3) : 837-851, 2017-
dc.date.modified2017-11-01-
dc.identifier.rimsid44203-
dc.type.rimsART-
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Internal Medicine (내과학교실) > 1. Journal Papers

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