Protein ubiquitination is a fundamental regulatory component in eukaryotic cell biology,
where a cascade of ubiquitin activating (E1), conjugating (E2), and ligating (E3) enzymes …

To understand the mechanism for assembly of Lys 48-linked polyubiquitin degradation
signals, we previously demonstrated that the E6AP/UBE3A ligase harbors two functionally …

The biochemical and structural characterization of ubiquitin-conjugating enzymes (E2s) over
the past 30 years has fostered important insights into ubiquitin transfer mechanisms …

Post-translational covalent modification by ubiquitin and ubiquitin-like proteins (UBLs) is a
major eukaryotic mechanism for regulating protein function. In general, each UBL has its …

The ubiquitination pathway is the main pathway for protein degradation in eukaryotic cells.
The attachment of ubiquitin to a substrate protein is catalyzed by three types of enzymes …

Although ubiquitination plays a critical role in virtually all cellular processes, mechanistic
details of ubiquitin (Ub) transfer are still being defined. To identify the molecular …

Ubiquitination targets proteins for degradation and is a potent regulator of cellular protein
function. Recent results implicate the RING finger domain in specific ubiquitination events; it …

Polyubiquitination by E2 and E3 enzymes is crucial to cell cycle control, epigenetic
regulation, and development. The hallmark of the E2 family is the ubiquitin (Ub)‐conjugating …

Rate studies have been employed as a reporter function to probe protein-protein
interactions within a biochemically defined reconstituted N-end rule ubiquitin ligation …

Cellular adaptation to proteotoxic stress at the endoplasmic reticulum (ER) depends on L
ys48‐linked polyubiquitination by ER‐associated ubiquitin ligases (E 3s) and subsequent …