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J Biol Chem, Vol. 274, Issue 2, 781-786, January 8, 1999
From The Burnham Institute, La Jolla, California 92037
Heat Shock Protein 70 kDa (Hsp70) family
molecular chaperones play critical roles in protein folding and
trafficking in all eukaryotic cells. The mechanisms by which Hsp70
family chaperones are regulated, however, are only partly understood.
BAG-1 binds the ATPase domains of Hsp70 and Hsc70, modulating their
chaperone activity and functioning as a competitive antagonist of the
co-chaperone Hip. We describe the identification of a family of
BAG-1-related proteins from humans (BAG-2, BAG-3, BAG-4, BAG-5), the
invertebrate Caenorhabditis elegans (BAG-1, BAG-2), and the
fission yeast Schizosaccharomyces pombe (BAG-1A, BAG-1B).
These proteins all contain a conserved ~45-amino acid region near
their C termini (the BAG domain) that binds Hsc70/Hsp70, but they
differ widely in their N-terminal domains. The human BAG-1, BAG-2, and
BAG-3 proteins bind with high affinity (KD 
1-10 nM) to the ATPase domain of Hsc70 and inhibit its
chaperone activity in a Hip-repressible manner. The findings suggest
opportunities for specification and diversification of Hsp70/Hsc70
chaperone functions through interactions with various BAG-family proteins.
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K. C. Kanelakis, Y. Morishima, K. D. Dittmar, M. D. Galigniana, S. Takayama, J. C. Reed, and W. B. Pratt Differential Effects of the hsp70-binding Protein BAG-1 on Glucocorticoid Receptor Folding by the hsp90-based Chaperone Machinery J. Biol. Chem., November 26, 1999; 274(48): 34134 - 34140. [Abstract] [Full Text] [PDF]
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G. Petersen, C. Hahn, and U. Gehring Dissection of the ATP-binding Domain of the Chaperone hsc70 for Interaction with the Cofactor Hap46 J. Biol. Chem., March 23, 2001; 276(13): 10178 - 10184. [Abstract] [Full Text] [PDF]
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E. A. A. Nollen, A. E. Kabakov, J. F. Brunsting, B. Kanon, J. Hohfeld, and H. H. Kampinga Modulation of in Vivo HSP70 Chaperone Activity by Hip and Bag-1 J. Biol. Chem., February 9, 2001; 276(7): 4677 - 4682. [Abstract] [Full Text] [PDF]
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J. Lin, L. Hutchinson, S. M. Gaston, G. Raab, and M. R. Freeman BAG-1 Is a Novel Cytoplasmic Binding Partner of the Membrane Form of Heparin-binding EGF-like Growth Factor. A UNIQUE ROLE FOR proHB-EGF IN CELL SURVIVAL REGULATION J. Biol. Chem., August 3, 2001; 276(32): 30127 - 30132. [Abstract] [Full Text] [PDF]
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D. A. Knee, B. A. Froesch, U. Nuber, S. Takayama, and J. C. Reed Structure-Function Analysis of Bag1 Proteins. EFFECTS ON ANDROGEN RECEPTOR TRANSCRIPTIONAL ACTIVITY J. Biol. Chem., April 13, 2001; 276(16): 12718 - 12724. [Abstract] [Full Text] [PDF]
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C. S. Gassler, T. Wiederkehr, D. Brehmer, B. Bukau, and M. P. Mayer Bag-1M Accelerates Nucleotide Release for Human Hsc70 and Hsp70 and Can Act Concentration-dependent as Positive and Negative Cofactor J. Biol. Chem., August 24, 2001; 276(35): 32538 - 32544. [Abstract] [Full Text] [PDF]
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