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  • Title: Testicular proteins associated with the germ cell-marker, TEX101: involvement of cellubrevin in TEX101-trafficking to the cell surface during spermatogenesis.
    Author: Tsukamoto H, Yoshitake H, Mori M, Yanagida M, Takamori K, Ogawa H, Takizawa T, Araki Y.
    Journal: Biochem Biophys Res Commun; 2006 Jun 23; 345(1):229-38. PubMed ID: 16678124.
    Abstract:
    Recently, we identified a cell-surface marker protein, TEX101, that is unique to male and female germ cells. On/off switching of TEX101 expression in germ cells is closely linked to the kinetics of gametogenesis. In the present study, we isolated testicular proteins by immunoprecipitation with anti-TEX101 antibody and identified the proteins using liquid chromatography/tandem mass spectrometry. Of three proteins identified (annexin 2, ly6k, and cellubrevin), a biochemical association between TEX101 and cellubrevin was confirmed by immunoprecipitation-Western blotting experiments. Immunohistochemistry using a cellubrevin-specific antibody indicated that the molecule is abundant on spermatocytes and early-stage spermatids, whereas negligible amounts are found in Sertoli cells, spermatogonia, spermatozoa, and late-stage spermatids. Most of the intracellular cellubrevin appeared to be juxtaposed with intracellular TEX101, and membrane-associated cellubrevin was docked near TEX101-positive plasma membranes on the cytoplasmic side. This close association was never observed on the outer surface of the plasma membrane. From these results we concluded that cellubrevin-dependent membrane trafficking is involved in TEX101-transport to the surface of male germ cells.
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