Molecular chaperone targeting and regulation by BAG family proteins
Top Cited Papers
- 1 October 2001
- journal article
- review article
- Published by Springer Nature in Nature Cell Biology
- Vol. 3 (10), E237-E241
- https://doi.org/10.1038/ncb1001-e237
Abstract
Regulated changes in protein conformation can have profound effects on protein function, although routine laboratory methods often fail to detect them. The recently discovered BAG-family proteins may operate as bridging molecules that recruit molecular chaperones to target proteins, presumably modulating protein functions through alterations in their conformations, and ultimately affecting diverse cellular behaviours including cell division, migration, differentiation and death. Emerging knowledge about BAG-family proteins indicates that there may be a mechanism for influencing signal transduction through non-covalent post-translational modifications.Keywords
This publication has 54 references indexed in Scilit:
- Folding of Newly Translated Proteins In Vivo: The Role of Molecular ChaperonesAnnual Review of Biochemistry, 2001
- Stress management – heat shock protein-70 and the regulation of apoptosisTrends in Cell Biology, 2001
- Molecular Chaperone Interactions with Steroid Receptors: an UpdateMolecular Endocrinology, 2000
- The Ubiquitin-related BAG-1 Provides a Link between the Molecular Chaperones Hsc70/Hsp70 and the ProteasomeJournal of Biological Chemistry, 2000
- A Nuclear Action of the Eukaryotic Cochaperone Rap46 in Downregulation of Glucocorticoid Receptor ActivityThe Journal of cell biology, 1999
- Function of WW Domains as Phosphoserine- or Phosphothreonine-Binding ModulesScience, 1999
- An Evolutionarily Conserved Family of Hsp70/Hsc70 Molecular Chaperone RegulatorsJournal of Biological Chemistry, 1999
- Mammalian protein RAP46: an interaction partner and modulator of 70kDa heat shock proteinsThe EMBO Journal, 1997
- BAG-1 modulates the chaperone activity of Hsp70/Hsc70The EMBO Journal, 1997
- Cloning and functional analysis of BAG-1: A novel Bcl-2-binding protein with anti-cell death activityCell, 1995