Pathways for protein disulphide bond formation.
The folding of many secretory proteins depends upon the formation of disulphide bonds. Recent advances in genetics and cell biology have outlined a core pathway for disulphide bond formation in the endoplasmic reticulum (ER) of eukaryotic cells. In this pathway, oxidizing equivalents flow from the recently identified ER membrane protein Ero1p to secretory proteins via protein disulphide isomerase (PDI). Contrary to prior expectations, oxidation of glutathione in the ER competes with oxidation of protein thiols. Contributions of PDI homologues to the catalysis of oxidative folding will be discussed, as will similarities between eukaryotic and prokaryotic disulphide-bond-forming systems.
Frand
A R
AR
Dept of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.
Cuozzo
J W
JW
Kaiser
C A
CA
D000818:Animals; D003545:Cysteine / Q000378:metabolism*; D004220:Disulfides / Q000737:chemistry / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000737:chemistry / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism; D006801:Humans; D008562:Membrane Glycoproteins; D010084:Oxidation-Reduction; D010088:Oxidoreductases; D019704:Protein Disulfide-Isomerases / Q000378:metabolism; D017510:Protein Folding
D004220:Disulfides; D006023:Glycoproteins; D008562:Membrane Glycoproteins; C405327:ERO1A protein, human; C491864:Ero1l protein, mouse; D010088:Oxidoreductases; D019704:Protein Disulfide-Isomerases; D003545:Cysteine