Alberti Simon, Esser Claudia, Höhfeld Jörg
Institut für Zellbiologie und Bonner Forum Biomedizin, Rheinische Friedrich-Wilhelms-Universität Bonn, Ulrich-Haberland-Str. 61a, D-53121 Bonn, Germany.
Cell Stress Chaperones. 2003 Fall;8(3):225-31. doi: 10.1379/1466-1268(2003)008<0225:bnefoh>2.0.co;2.
BAG-1 (Bcl-2-associated athanogene) is a multifaceted protein implicated in the modulation of a large variety of cellular processes. Elucidating the molecular mechanisms that underlie the cellular functions of BAG-1 becomes an increasingly important task, particularly in light of the growing evidence connecting aberrant BAG-1 expression to certain human cancers. A common element of the remarkable functional diversity of BAG-1 appears to be the interaction with molecular chaperones of the Hsp70 family. In fact, BAG-1 functions as a nucleotide exchange factor of mammalian cytosolic Hsc70, thereby triggering substrate unloading from the chaperone. In addition, recent findings reveal an association of BAG-1 with the proteasome, which suggests a role in coordinating chaperone and degradation pathways.
BAG-1(Bcl-2相关永生基因)是一种多面蛋白,与多种细胞过程的调节有关。阐明BAG-1细胞功能背后的分子机制已成为一项日益重要的任务,特别是鉴于越来越多的证据将异常的BAG-1表达与某些人类癌症联系起来。BAG-1显著的功能多样性的一个共同要素似乎是与Hsp70家族分子伴侣的相互作用。事实上,BAG-1作为哺乳动物胞质Hsc70的核苷酸交换因子发挥作用,从而触发伴侣蛋白上底物的卸载。此外,最近的研究结果揭示了BAG-1与蛋白酶体的关联,这表明其在协调伴侣蛋白和降解途径中发挥作用。