Structure and dynamics of a pentameric KCTD5/Cullin3/GBeta1Gamma2 E3 ubiquitin ligase complex
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ABSTRACT:
SUBMITTER: Douglas A Kuntz
PROVIDER: EMPIAR-11734 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structure and dynamics of a pentameric KCTD5/CUL3/Gβγ E3 ubiquitin ligase complex.
Nguyen Duc Minh DM Rath Deanna H DH Devost Dominic D Pétrin Darlaine D Rizk Robert R Ji Alan X AX Narayanan Naveen N Yong Darren D Zhai Andrew A Kuntz Douglas A DA Mian Maha U Q MUQ Pomroy Neil C NC Keszei Alexander F A AFA Benlekbir Samir S Mazhab-Jafari Mohammad T MT Rubinstein John L JL Hébert Terence E TE Privé Gilbert G GG
Proceedings of the National Academy of Sciences of the United States of America 20240416 17
Heterotrimeric G proteins can be regulated by posttranslational modifications, including ubiquitylation. KCTD5, a pentameric substrate receptor protein consisting of an N-terminal BTB domain and a C-terminal domain, engages CUL3 to form the central scaffold of a cullin-RING E3 ligase complex (CRL3<sup>KCTD5</sup>) that ubiquitylates Gβγ and reduces Gβγ protein levels in cells. The cryo-EM structure of a 5:5:5 KCTD5/CUL3<sup>NTD</sup>/Gβ<sub>1</sub>γ<sub>2</sub> assembly reveals a highly dynamic ...[more]
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