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

Stable Identifier
R-HSA-6814120
Type
Reaction [dissociation]
Species
Homo sapiens
Compartment
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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
15889144 Phosducin-like protein acts as a molecular chaperone for G protein betagamma dimer assembly

Lukov, GL, Hu, T, McLaughlin, JN, Hamm, HE, Willardson, BM

EMBO J. 2005
16717095 Mechanism of assembly of G protein betagamma subunits by protein kinase CK2-phosphorylated phosducin-like protein and the cytosolic chaperonin complex

Lukov, GL, Baker, CM, Ludtke, PJ, Hu, T, Carter, MD, Hackett, RA, Thulin, CD, Willardson, BM

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

Plimpton, RL, Cuellar, J, Lai, CW, Aoba, T, Makaju, A, Franklin, S, Mathis, AD, Prince, JT, Carrascosa, JL, Valpuesta, JM, Willardson, BM

Proc. Natl. Acad. Sci. U.S.A. 2015
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