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Structural and Functional Insights into GID/CTLH E3 Ligase Complexes.

ABSTRACT: Multi-subunit E3 ligases facilitate ubiquitin transfer by coordinating various substrate receptor subunits with a single catalytic center. Small molecules inducing targeted protein degradation have exploited such complexes, proving successful as therapeutics against previously undruggable targets. The C-terminal to LisH (CTLH) complex, also called the glucose-induced degradation deficient (GID) complex, is a multi-subunit E3 ligase complex highly conserved from Saccharomyces cerevisiae to humans, with roles in fundamental pathways controlling homeostasis and development in several species. However, we are only beginning to understand its mechanistic basis. Here, we review the literature of the CTLH complex from all organisms and place previous findings on individual subunits into context with recent breakthroughs on its structure and function.

SUBMITTER: Maitland MER

PROVIDER: S-EPMC9180843 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature

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Structural and Functional Insights into GID/CTLH E3 Ligase Complexes.

Maitland Matthew E R MER Lajoie Gilles A GA Shaw Gary S GS Schild-Poulter Caroline C

International journal of molecular sciences 20220524 11

Multi-subunit E3 ligases facilitate ubiquitin transfer by coordinating various substrate receptor subunits with a single catalytic center. Small molecules inducing targeted protein degradation have exploited such complexes, proving successful as therapeutics against previously undruggable targets. The C-terminal to LisH (CTLH) complex, also called the glucose-induced degradation deficient (GID) complex, is a multi-subunit E3 ligase complex highly conserved from <i>Saccharomyces cerevisiae</i> to ...[more]

PMID: 35682545

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