Reactome | ATP hydrolysis promotes folding of G-protein beta by TRiC/CCT

ATP hydrolysis promotes folding of G-protein beta by TRiC/CCT

Stable Identifier

R-HSA-6814120

Type

Reaction [dissociation]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

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ATP hydrolysis promotes folding of G-protein beta by TRiC/CCT

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In an ATP-dependent process, G-beta reaches a near-native state in the folding cavity of TRiC, except that TRiC cannot mediate the folding of the seven-bladed beta propeller of the G-protein beta to a stable conformation (Plimpton et al. 2015).

Literature References

PubMed ID	Title	Journal	Year
16717095	Mechanism of assembly of G protein betagamma subunits by protein kinase CK2-phosphorylated phosducin-like protein and the cytosolic chaperonin complex Thulin, CD, Lukov, GL, Ludtke, PJ, Hu, T, Carter, MD, Baker, CM, Hackett, RA, Willardson, BM	J. Biol. Chem.	2006
15889144	Phosducin-like protein acts as a molecular chaperone for G protein betagamma dimer assembly Lukov, GL, Hu, T, Hamm, HE, McLaughlin, JN, Willardson, BM	EMBO J.	2005
25675501	Structures of the Gβ-CCT and PhLP1-Gβ-CCT complexes reveal a mechanism for G-protein β-subunit folding and Gβγ dimer assembly Makaju, A, Lai, CW, Prince, JT, Carrascosa, JL, Plimpton, RL, Cuellar, J, Valpuesta, JM, Aoba, T, Franklin, S, Willardson, BM, Mathis, AD	Proc. Natl. Acad. Sci. U.S.A.	2015