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Homer2 Protein Regulates Plasma Membrane Ca2+ ATPase -mediated Ca2+ Signaling in Mouse Parotid Gland Acinar Cells

DC FieldValueLanguage
dc.contributor.author박순홍-
dc.contributor.author신동민-
dc.contributor.author양유미-
dc.contributor.author이지애-
dc.contributor.author장인익-
dc.date.accessioned2015-01-06T17:17:36Z-
dc.date.available2015-01-06T17:17:36Z-
dc.date.issued2014-
dc.identifier.issn0021-9258-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/99704-
dc.description.abstractHomer proteins are scaffold molecules with a domain structure consisting of an N-terminal Ena/VASP homology 1 protein-binding domain and a C-terminal leucine zipper/coiled-coil domain. The Ena/VASP homology 1 domain recognizes proline-rich motifs and binds multiple Ca(2+)-signaling proteins, including G protein-coupled receptors, inositol 1,4,5-triphosphate receptors, ryanodine receptors, and transient receptor potential channels. However, their role in Ca(2+) signaling in nonexcitable cells is not well understood. In this study, we investigated the role of Homer2 on Ca(2+) signaling in parotid gland acinar cells using Homer2-deficient (Homer2(-/-)) mice. Homer2 is localized at the apical pole in acinar cells. Deletion of Homer2 did not affect inositol 1,4,5-triphosphate receptor localization or channel activity and did not affect the expression and activity of sarco/endoplasmic reticulum Ca(2+)-ATPase pumps. In contrast, Homer2 deletion markedly increased expression of plasma membrane Ca(2+)-ATPase (PMCA) pumps, in particular PMCA4, at the apical pole. Accordingly, Homer2 deficiency increased Ca(2+) extrusion by acinar cells. These findings were supported by co-immunoprecipitation of Homer2 and PMCA in wild-type parotid cells and transfected human embryonic kidney 293 (HEK293) cells. We identified a Homer-binding PPXXF-like motif in the N terminus of PMCA that is required for interaction with Homer2. Mutation of the PPXXF-like motif did not affect the interaction of PMCA with Homer1 but inhibited its interaction with Homer2 and increased Ca(2+) clearance by PMCA. These findings reveal an important regulation of PMCA by Homer2 that has a central role on PMCA-mediated Ca(2+) signaling in parotid acinar cells.-
dc.description.statementOfResponsibilityopen-
dc.format.extent24971~24979-
dc.relation.isPartOfJournal of Biological Chemistry-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/2.0/kr/-
dc.subject.MESHAcinar Cells/metabolism*-
dc.subject.MESHAmino Acid Sequence-
dc.subject.MESHAnimals-
dc.subject.MESHBinding Sites/genetics-
dc.subject.MESHBlotting, Western-
dc.subject.MESHCalcium/metabolism*-
dc.subject.MESHCalcium Signaling-
dc.subject.MESHCarrier Proteins/genetics-
dc.subject.MESHCarrier Proteins/metabolism*-
dc.subject.MESHHEK293 Cells-
dc.subject.MESHHomer Scaffolding Proteins-
dc.subject.MESHHumans-
dc.subject.MESHInositol 1,4,5-Trisphosphate Receptors/metabolism-
dc.subject.MESHMice, Knockout-
dc.subject.MESHMicroscopy, Confocal-
dc.subject.MESHMolecular Sequence Data-
dc.subject.MESHParotid Gland/cytology-
dc.subject.MESHParotid Gland/metabolism*-
dc.subject.MESHPlasma Membrane Calcium-Transporting ATPases/genetics-
dc.subject.MESHPlasma Membrane Calcium-Transporting ATPases/metabolism*-
dc.subject.MESHProtein Binding-
dc.subject.MESHSarcoplasmic Reticulum Calcium-Transporting ATPases/metabolism-
dc.subject.MESHSequence Homology, Amino Acid-
dc.titleHomer2 Protein Regulates Plasma Membrane Ca2+ ATPase -mediated Ca2+ Signaling in Mouse Parotid Gland Acinar Cells-
dc.typeArticle-
dc.contributor.collegeCollege of Dentistry (치과대학)-
dc.contributor.departmentDept. of Oral Biology (구강생물학)-
dc.contributor.googleauthorYu-Mi Yang-
dc.contributor.googleauthorJiae Lee-
dc.contributor.googleauthorHae Jo-
dc.contributor.googleauthorSoonhong Park-
dc.contributor.googleauthorInik Chang-
dc.contributor.googleauthorShmuel Muallem-
dc.contributor.googleauthorDong Min Shin-
dc.identifier.doi10.1074/jbc.M114.577221-
dc.admin.authorfalse-
dc.admin.mappingfalse-
dc.contributor.localIdA01547-
dc.contributor.localIdA02091-
dc.contributor.localIdA03192-
dc.contributor.localIdA03461-
dc.contributor.localIdA05148-
dc.relation.journalcodeJ01258-
dc.identifier.pmid25049230-
dc.identifier.urlhttp://www.jbc.org/content/289/36/24971.long-
dc.subject.keywordCalcium ATPase-
dc.subject.keywordCalcium Transport-
dc.subject.keywordCell Signaling-
dc.subject.keywordHomer Proteins-
dc.subject.keywordParotid Gland-
dc.subject.keywordPlasma Membrane Ca2+-ATPase-
dc.subject.keywordProline-rich Motif-
dc.subject.keywordProtein-Protein Interaction-
dc.subject.keywordScaffold Protein-
dc.contributor.alternativeNamePark, Soon Hong-
dc.contributor.alternativeNameShin, Dong Min-
dc.contributor.alternativeNameYang, Yu-Mi-
dc.contributor.alternativeNameLee, Ji Ae-
dc.contributor.alternativeNameChang, In Ik-
dc.contributor.affiliatedAuthorPark, Soon Hong-
dc.contributor.affiliatedAuthorShin, Dong Min-
dc.contributor.affiliatedAuthorLee, Ji Ae-
dc.contributor.affiliatedAuthorChang, In Ik-
dc.contributor.affiliatedAuthorYang, Yu Mi-
dc.rights.accessRightsfree-
dc.citation.volume289-
dc.citation.number36-
dc.citation.startPage24971-
dc.citation.endPage24979-
dc.identifier.bibliographicCitationJournal of Biological Chemistry, Vol.289(36) : 24971-24979, 2014-
Appears in Collections:
2. College of Dentistry (치과대학) > Dept. of Oral Biology (구강생물학교실) > 1. Journal Papers
5. Research Institutes (연구소) > Research Center for Human Natural Defense System (생체방어연구센터) > 1. Journal Papers

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