SUMO: from bench to bedside

HM Chang, ETH Yeh - Physiological Reviews, 2020 - journals.physiology.org
Sentrin/small ubiquitin-like modifier (SUMO) is protein modification pathway that regulates
multiple biological processes, including cell division, DNA replication/repair, signal …

Protein modification by SUMO

ES Johnson - Annual review of biochemistry, 2004 - annualreviews.org
▪ Abstract Small ubiquitin-related modifier (SUMO) family proteins function by becoming
covalently attached to other proteins as post-translational modifications. SUMO modifies …

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 …

Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways

BA Schulman, J Wade Harper - Nature reviews Molecular cell biology, 2009 - nature.com
Attachment of ubiquitin or ubiquitin-like proteins (known as UBLs) to their targets through
multienzyme cascades is a central mechanism to modulate protein functions. This process is …

Sumoylation on its 25th anniversary: mechanisms, pathology, and emerging concepts

AB Celen, U Sahin - The FEBS journal, 2020 - Wiley Online Library
Sumoylation is an essential post‐translational modification intimately involved in a diverse
range of eukaryotic cellular mechanisms. Small ubiquitin‐like modifier (SUMO) protein …

Identification of a SUMO-binding motif that recognizes SUMO-modified proteins

J Song, LK Durrin, TA Wilkinson… - Proceedings of the …, 2004 - National Acad Sciences
Posttranslational modification by the ubiquitin homologue, small ubiquitin-like modifier 1
(SUMO-1), has been established as an important regulatory mechanism. However, in most …

SUMO conjugation–a mechanistic view

A Pichler, C Fatouros, H Lee, N Eisenhardt - Biomolecular concepts, 2017 - degruyter.com
The regulation of protein fate by modification with the small ubiquitin-related modifier
(SUMO) plays an essential and crucial role in most cellular pathways. Sumoylation is highly …

Cbx4 governs HIF-1α to potentiate angiogenesis of hepatocellular carcinoma by its SUMO E3 ligase activity

J Li, Y Xu, XD Long, W Wang, HK Jiao, Z Mei, QQ Yin… - Cancer cell, 2014 - cell.com
Cbx4 is a polycomb group protein that is also a SUMO E3 ligase, but its potential roles in
tumorigenesis remain to be explored. Here, we report that Cbx4, but not other members of …

Neuronal SUMOylation: mechanisms, physiology, and roles in neuronal dysfunction

JM Henley, TJ Craig, KA Wilkinson - Physiological reviews, 2014 - journals.physiology.org
Protein SUMOylation is a critically important posttranslational protein modification that
participates in nearly all aspects of cellular physiology. In the nearly 20 years since its …

Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1

LM Lois, CD Lima - The EMBO journal, 2005 - embopress.org
E1 enzymes facilitate conjugation of ubiquitin and ubiquitin‐like proteins through
adenylation, thioester transfer within E1, and thioester transfer from E1 to E2 conjugating …