Reactome | TRiC/CCT binds unfolded G-protein beta subunit

TRiC/CCT binds unfolded G-protein beta subunit

Stable Identifier

R-HSA-6814119

Type

Reaction [binding]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

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TRiC/CCT binds unfolded G-protein beta subunit

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The TRiC/CCT chaperonin complex binds nascent, unfolded, G-protein beta subunit (GNB1, GNB2, GNB3, GNB4 or GNB5) (Wells et al. 2006). 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
16702223	Role of the chaperonin CCT/TRiC complex in G protein betagamma-dimer assembly Dingus, J, Hildebrandt, JD, Wells, CA	J. Biol. Chem.	2006
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