Identification of novel retromer complexes in the mouse testis = 마우스 정소에서 정소특이적인 리트로마 복합체 동정

Cited 14 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorEkyune Kim-
dc.contributor.authorJae Woong Lee-
dc.contributor.authorDong Chul Baek-
dc.contributor.authorSang Rae Lee-
dc.contributor.authorMyeong Su Kim-
dc.contributor.authorSang-Hyun Kim-
dc.contributor.authorK Imakawa-
dc.contributor.authorKyu Tae Chang-
dc.date.accessioned2017-04-19T09:11:31Z-
dc.date.available2017-04-19T09:11:31Z-
dc.date.issued2008-
dc.identifier.issn0006-291X-
dc.identifier.uri10.1016/j.bbrc.2008.07.067ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/8562-
dc.description.abstractA family of vacuolar protein sorting (Vps) proteins, which are components of mammalian retromer complex, has been studied in the mouse. Vps26a is known as a retromer component that plays an important role in embryonic development: however, its cell-type expression and precise role remain to be elucidated. In this study, we identified a new isoform of Vps26a, called Vps26aT, which was expressed specifically in the mouse testis. Diverse expression patterns of Vps26 variants in mouse tissues were determined by Western blot and RT-PCR analyses, and the direct interaction of Vps26aT with Vps35 was also demonstrated by immunoprecipitation and pull-down assay using antibodies raised against each Vps component. Our results revealed that the retromer complex could be formed from different Vps26 isoforms in a tissue-specific manner, resulting in more than two types of the retromer complex, including the Vps26a-Vps29-Vps35, Vps26aT-Vps29-Vps35, and Vps26b-Vps29-Vps35 complexes in mouse tissues.-
dc.publisherElsevier-
dc.titleIdentification of novel retromer complexes in the mouse testis = 마우스 정소에서 정소특이적인 리트로마 복합체 동정-
dc.title.alternativeIdentification of novel retromer complexes in the mouse testis-
dc.typeArticle-
dc.citation.titleBiochemical and Biophysical Research Communications-
dc.citation.number1-
dc.citation.endPage21-
dc.citation.startPage16-
dc.citation.volume375-
dc.contributor.affiliatedAuthorEkyune Kim-
dc.contributor.affiliatedAuthorJae Woong Lee-
dc.contributor.affiliatedAuthorDong Chul Baek-
dc.contributor.affiliatedAuthorSang Rae Lee-
dc.contributor.affiliatedAuthorMyeong Su Kim-
dc.contributor.affiliatedAuthorSang-Hyun Kim-
dc.contributor.affiliatedAuthorKyu Tae Chang-
dc.contributor.alternativeName김익균-
dc.contributor.alternativeName이재웅-
dc.contributor.alternativeName백동철-
dc.contributor.alternativeName이상래-
dc.contributor.alternativeName김명수-
dc.contributor.alternativeName김상현-
dc.contributor.alternativeNameImakawa-
dc.contributor.alternativeName장규태-
dc.identifier.bibliographicCitationBiochemical and Biophysical Research Communications, vol. 375, no. 1, pp. 16-21-
dc.identifier.doi10.1016/j.bbrc.2008.07.067-
dc.subject.keywordEmbryonic development-
dc.subject.keywordEndosome-
dc.subject.keywordRetromer complex-
dc.subject.keywordSpermatogenesis-
dc.subject.keywordVacuolar protein sorting-
dc.subject.localEmbryonic development-
dc.subject.localembryonic development-
dc.subject.localEndosome-
dc.subject.localEndosomes-
dc.subject.localRetromer complex-
dc.subject.localretromer complex-
dc.subject.localSpermatogenesis-
dc.subject.localspermatogenesis-
dc.subject.localVacuolar protein sorting-
dc.description.journalClassY-
Appears in Collections:
Ochang Branch Institute > Division of National Bio-Infrastructure > National Primate Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.