Multi-subunit E3 ligases facilitate ubiquitin transfer by coordinating various substrate
receptor subunits with a single catalytic center. Small molecules inducing targeted protein …

In 2008, we published the first set of guidelines for standardizing research in autophagy.
Since then, this topic has received increasing attention, and many scientists have entered …

INTRODUCTION Cells synthesize glucose if deprived of it, and destroy gluconeogenic
enzymes upon return to glucose-replete conditions. Gluconeogenesis (de novo synthesis of …

Abstract The Saccharomyces cerevisiae Gid-complex is a highly evolutionary conserved
ubiquitin ligase with at least seven protein subunits. Here, we review our knowledge about …

Ubiquitylation is catalyzed by coordinated actions of E3 and E2 enzymes. Molecular
principles governing many important E3-E2 partnerships remain unknown, including those …

How are E3 ubiquitin ligases configured to match substrate quaternary structures? Here, by
studying the yeast GID complex (mutation of which causes deficiency in glucose-induced …

Selective protein degradation by the ubiquitin-proteasome system (UPS) is involved in all
cellular processes. However, the substrates and specificity of most UPS components are not …

The AMP-activated protein kinase (AMPK) regulates cellular energy homeostasis by sensing
the metabolic status of the cell. AMPK is regulated by phosphorylation and …

The multi-subunit C-terminal to LisH (CTLH) complex is the mammalian homologue of the
yeast Gid E3 ubiquitin ligase complex. In this study, we investigated the human CTLH …

N-degron E3 ubiquitin ligases recognize specific residues at the N-termini of substrates.
Although molecular details of N-degron recognition are known for several E3 ligases, the …