The structure of the nuclear pore complex (an update)

DH Lin, A Hoelz - Annual review of biochemistry, 2019 - annualreviews.org
The nuclear pore complex (NPC) serves as the sole bidirectional gateway of
macromolecules in and out of the nucleus. Owing to its size and complexity (∼ 1,000 protein …

Ubiquitin ligases: structure, function, and regulation

N Zheng, N Shabek - Annual review of biochemistry, 2017 - annualreviews.org
Ubiquitin E3 ligases control every aspect of eukaryotic biology by promoting protein
ubiquitination and degradation. At the end of a three-enzyme cascade, ubiquitin ligases …

Architecture of the cytoplasmic face of the nuclear pore

CJ Bley, S Nie, GW Mobbs, S Petrovic, AT Gres, X Liu… - Science, 2022 - science.org
INTRODUCTION Cytoplasmic face of the human NPC. Near-atomic composite structure of
the NPC generated by docking high-resolution crystal structures into a cryo‑ET …

Compositional control of phase-separated cellular bodies

SF Banani, AM Rice, WB Peeples, Y Lin, S Jain… - Cell, 2016 - cell.com
Cellular bodies such as P bodies and PML nuclear bodies (PML NBs) appear to be phase-
separated liquids organized by multivalent interactions among proteins and RNA molecules …

Structural insights into the catalysis and regulation of E3 ubiquitin ligases

L Buetow, DT Huang - Nature reviews Molecular cell biology, 2016 - nature.com
Covalent attachment (conjugation) of one or more ubiquitin molecules to protein substrates
governs numerous eukaryotic cellular processes, including apoptosis, cell division and …

Ubiquitin-like protein conjugation: structures, chemistry, and mechanism

L Cappadocia, CD Lima - Chemical reviews, 2018 - ACS Publications
Ubiquitin-like proteins (Ubl's) are conjugated to target proteins or lipids to regulate their
activity, stability, subcellular localization, or macromolecular interactions. Similar to ubiquitin …

E2 enzymes: more than just middle men

MD Stewart, T Ritterhoff, RE Klevit, PS Brzovic - Cell research, 2016 - nature.com
Ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes
responsible for the attachment of ubiquitin (Ub) to cellular proteins. Humans have∼ 40 E2s …

A comprehensive compilation of SUMO proteomics

IA Hendriks, ACO Vertegaal - Nature reviews Molecular cell biology, 2016 - nature.com
Small ubiquitin-like modifiers (SUMOs) are essential for the regulation of several cellular
processes and are potential therapeutic targets owing to their involvement in diseases such …

[HTML][HTML] The post-translational modification, SUMOylation, and cancer

ZJ Han, YH Feng, BH Gu, YM Li… - … journal of oncology, 2018 - spandidos-publications.com
SUMOylation is a reversible post-translational modification which has emerged as a crucial
molecular regulatory mechanism, involved in the regulation of DNA damage repair, immune …

New insights into ubiquitin E3 ligase mechanism

CE Berndsen, C Wolberger - Nature structural & molecular biology, 2014 - nature.com
E3 ligases carry out the final step in the ubiquitination cascade, catalyzing transfer of
ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine. Three distinct …