| Literature DB >> 14984055 |
Simon Alberti1, Claudia Esser, Jörg Höhfeld.
Abstract
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.Entities:
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Year: 2003 PMID: 14984055 PMCID: PMC514875 DOI: 10.1379/1466-1268(2003)008<0225:bnefoh>2.0.co;2
Source DB: PubMed Journal: Cell Stress Chaperones ISSN: 1355-8145 Impact factor: 3.667