Reactome | Protein folding

Protein folding

Stable Identifier

R-HSA-391251

DOI

10.3180/REACT_17004.1

Type

Pathway

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

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Due to the crowded envirnoment within the cell, many proteins must interact with molecular chaperones to attain their native conformation (reviewed in Young et al., 2004). Chaperones recognize and associate with proteins in their non-native state and facilitate their folding by stabilizing the conformation of productive folding intermediates. Chaperones that take part broadly in de novo protein folding, such as the Hsp70s and the chaperonins, facilitate the folding process through cycles of substrate binding and release regulated by their ATPase activity (see Young et al., 2004; Spiess et al., 2004; Bigotti and Clarke, 2008).

Literature References

PubMed ID	Title	Journal	Year
18395510	Chaperonins: The hunt for the Group II mechanism Bigotti, MG, Clarke, AR	Arch Biochem Biophys	2008
15459659	Pathways of chaperone-mediated protein folding in the cytosol Young, JC, Agashe, VR, Siegers, K, Hartl, FU	Nat Rev Mol Cell Biol	2004
15519848	Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets Spiess, C, Meyer, AS, Reissmann, S, Frydman, J	Trends Cell Biol	2004