| Literature DB >> 18656452 |
Ekyune Kim1, Jae-Woong Lee, Dong-Chul Baek, Sang-Rae Lee, Myeong-Su Kim, Sang-Hyun Kim, Kazuhiko Imakawa, Kyu-Tae Chang.
Abstract
A 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.Entities:
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Year: 2008 PMID: 18656452 DOI: 10.1016/j.bbrc.2008.07.067
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575