Chaperone Function of Hsp90-Associated Proteins

The Hsp90 heat shock protein of eukaryotic cells regulates the activity of proteins involved in signal transduction pathways and may direct intracellular protein folding in general. Hsp90 performs at least part of its function in a complex with a specific set of partner proteins that include members of the prolyl isomerase family. The properties of the major components of the Hsp90 complex were examined through the use of in vitro protein folding assays. Two of the components, FKBP52 and p23, functioned as mechanistically distinct molecular chaperones. These results suggest the existence of a super-chaperone complex in the cytosol of eukaryotic cells.

[1]  R. Morimoto,et al.  Molecular Chaperone Machines: Chaperone Activities of the Cyclophilin Cyp-40 and the Steroid Aporeceptor-Associated Protein p23 , 1996, Science.

[2]  R. Morimoto,et al.  The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj‐1 have distinct roles in recognition of a non‐native protein and protein refolding. , 1996, The EMBO journal.

[3]  J. Reinstein,et al.  Assessment of the ATP Binding Properties of Hsp90 (*) , 1996, The Journal of Biological Chemistry.

[4]  J. Buchner.  Supervising the fold: functional principles of molecular chaperones , 1996, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[5]  R. Rimerman,et al.  Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent , 1995, Molecular and cellular biology.

[6]  J. Buchner,et al.  Structural Organization of Procaryotic and Eucaryotic Hsp90. INFLUENCE OF DIVALENT CATIONS ON STRUCTURE AND FUNCTION (*) , 1995, The Journal of Biological Chemistry.

[7]  J. Buchner,et al.  Transient Interaction of Hsp90 with Early Unfolding Intermediates of Citrate Synthase , 1995, The Journal of Biological Chemistry.

[8]  L. Randall,et al.  High selectivity with low specificity: how SecB has solved the paradox of chaperone binding. , 1995, Trends in biochemical sciences.

[9]  S. Lindquist,et al.  Conservation of Hsp90 macromolecular complexes in Saccharomyces cerevisiae. , 1994, The Journal of biological chemistry.

[10]  G. Fischer,et al.  Peptidyl-prolyl cis/trans isomerases and their effectors , 1994 .

[11]  R. Freedman,et al.  Peptidyl prolyl cis-trans-isomerase activity associated with the lumen of the endoplasmic reticulum. , 1994, The Biochemical journal.

[12]  J. Buchner,et al.  Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones. , 1994, Trends in biochemical sciences.

[13]  M. Welsh,et al.  Chaperone functions of the heat shock proteins associated with steroid receptors. , 1994, Seminars in cell biology.

[14]  A Helenius,et al.  How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. , 1994, Molecular biology of the cell.

[15]  F. Schmid,et al.  Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions. , 1993, Annual review of biophysics and biomolecular structure.

[16]  M. Gaestel,et al.  Small heat shock proteins are molecular chaperones. , 1993, The Journal of biological chemistry.

[17]  A. Burny,et al.  An immunophilin that binds M(r) 90,000 heat shock protein: main structural features of a mammalian p59 protein. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[18]  J. Buchner,et al.  Hsp90 chaperones protein folding in vitro , 1992, Nature.

[19]  F. Hartl,et al.  Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding , 1992, Nature.

[20]  J. Sambrook,et al.  Protein folding in the cell , 1992, Nature.

[21]  S. Schreiber,et al.  The mechanism of action of cyclosporin A and FK506. , 1992, Immunology today.

[22]  E. Baulieu,et al.  Steroid hormone receptors. , 1975, Vitamins and hormones.