Pathways of chaperone-mediated protein folding in the cytosol.
Cells are faced with the task of folding thousands of different polypeptides into a wide range of conformations. For many proteins, the folding process requires the action of molecular chaperones. In the cytosol of prokaryotic and eukaryotic cells, molecular chaperones of different structural classes form a network of pathways that can handle substrate polypeptides from the point of initial synthesis on ribosomes to the final stages of folding.
Department of Biochemistry, McIntyre Medical Sciences Building, McGill University, 3655 Promenade Sir William Osler, Montreal, Quebec H3G 1Y6, Canada.
Jason C
JC
Young
Vishwas R
VR
Agashe
Katja
K
Siegers
F Ulrich
FU
Hartl
D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism; D018833:Chaperonins / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism*; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism; D008954:Models, Biological; D018832:Molecular Chaperones / Q000378:metabolism*; D011487:Protein Conformation; D017510:Protein Folding; D021381:Protein Transport; D012270:Ribosomes / Q000378:metabolism
D001426:Bacterial Proteins; D018840:HSP70 Heat-Shock Proteins; D018841:HSP90 Heat-Shock Proteins; D018832:Molecular Chaperones; D018833:Chaperonins