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 …
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 …
covalently attached to other proteins as post-translational modifications. SUMO modifies …
Ubiquitin-like protein conjugation: structures, chemistry, and mechanism
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 …
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 …
multienzyme cascades is a central mechanism to modulate protein functions. This process is …
Sumoylation on its 25th anniversary: mechanisms, pathology, and emerging concepts
Sumoylation is an essential post‐translational modification intimately involved in a diverse
range of eukaryotic cellular mechanisms. Small ubiquitin‐like modifier (SUMO) protein …
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-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 …
(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 …
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 …
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
E1 enzymes facilitate conjugation of ubiquitin and ubiquitin‐like proteins through
adenylation, thioester transfer within E1, and thioester transfer from E1 to E2 conjugating …
adenylation, thioester transfer within E1, and thioester transfer from E1 to E2 conjugating …