Specificity of eukaryotic protein degradation is determined by E3 ubiquitin ligases and their
selective binding to protein motifs, termed" degrons," in substrates for ubiquitin-mediated …

The N-degron pathway is a degradative system in which the N-terminal residues of proteins
modulate the half-lives of proteins and other cellular materials. The majority of amino acids …

Targeted protein degradation (TPD) strategies exploit bivalent small molecules to bridge
substrate proteins to an E3 ubiquitin ligase to induce substrate degradation. Few E3s have …

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 …

Most eukaryotic proteins are N-terminally acetylated, but the functional impact on a global
scale has remained obscure. Using genome-wide CRISPR knockout screens in human …

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 development of haematopoietic stem cells into mature erythrocytes–erythropoiesis–is a
controlled process characterized by cellular reorganization and drastic reshaping of the …

A diverse antibody repertoire is essential for humoral immunity. Antibody diversification
requires the introduction of deoxyuridine (dU) mutations within immunoglobulin genes to …

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

The C-terminal to LisH (CTLH) complex is a ubiquitin ligase complex that recognizes
substrates with Pro/N-degrons via its substrate receptor Glucose-Induced Degradation 4 …