BAG-1—a nucleotide exchange factor of Hsc70 with multiple cellular functions

AUTOR(ES)

Alberti, Simon

FONTE

Cell Stress Society International

RESUMO

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.

Documentos Relacionados

• Nucleotide sequence of a processed human hsc70 pseudogene.
• Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53
• In vivo and in vitro association of hsc70 with polyomavirus capsid proteins.
• Hsc70 Regulates Accumulation of Cyclin D1 and Cyclin D1-Dependent Protein Kinase
• Interaction of Rotaviruses with Hsc70 during Cell Entry Is Mediated by VP5