SUMO-Targeted Ubiquitin Ligases and Their Functions in Maintaining Genome Stability.
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TLDR
Small ubiquitin-like modifier (SUMO)-targeted E3 UCLs (STUbLs) as discussed by the authors are specialized enzymes that recognize SUMOylated proteins and attach UCL to them, and participate in diverse molecular processes that span cell cycle regulated events.Abstract:
Small ubiquitin-like modifier (SUMO)-targeted E3 ubiquitin ligases (STUbLs) are specialized enzymes that recognize SUMOylated proteins and attach ubiquitin to them. They therefore connect the cellular SUMOylation and ubiquitination circuits. STUbLs participate in diverse molecular processes that span cell cycle regulated events, including DNA repair, replication, mitosis, and transcription. They operate during unperturbed conditions and in response to challenges, such as genotoxic stress. These E3 ubiquitin ligases modify their target substrates by catalyzing ubiquitin chains that form different linkages, resulting in proteolytic or non-proteolytic outcomes. Often, STUbLs function in compartmentalized environments, such as the nuclear envelope or kinetochore, and actively aid in nuclear relocalization of damaged DNA and stalled replication forks to promote DNA repair or fork restart. Furthermore, STUbLs reside in the same vicinity as SUMO proteases and deubiquitinases (DUBs), providing spatiotemporal control of their targets. In this review, we focus on the molecular mechanisms by which STUbLs help to maintain genome stability across different species.read more
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References
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TL;DR: Data is provided suggesting that two of the four mammalian ubiquitin precursors, UBA52 and UBA80, are processed mostly post-translationally whereas the other two, UBB and UBC, probably undergo a combination of co- and post-translational processing.
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SUMO-independent in vivo activity of a SUMO-targeted ubiquitin ligase toward a short-lived transcription factor
TL;DR: It is suggested that alpha2, and presumably other proteins, have surface features that mimic SUMO, and therefore can directly recruit STUbLs without prior SUMO conjugation.
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The STUbL RNF4 regulates protein group SUMOylation by targeting the SUMO conjugation machinery.
Ramesh Kumar,Ramesh Kumar,Román González-Prieto,Zhenyu Xiao,Matty Verlaan-de Vries,Alfred C.O. Vertegaal +5 more
TL;DR: A method for selective enrichment of ubiquitin substrates for E3 ligases from complex cellular proteomes is described and the SUMO conjugation machinery as direct RNF4 substrates are identified.
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The kinetochore-microtubule interface at a glance.
Julie K. Monda,Iain M. Cheeseman +1 more
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Journal ArticleDOI
Arkadia, a novel SUMO-targeted ubiquitin ligase involved in PML degradation.
TL;DR: This work shows that Arkadia contains three successive SUMO-interacting motifs (SIMs) that mediate noncovalent interaction with poly-SUMO2 and identifies the third SIM (VVDL) of Arkadia to be the most relevant one in this interaction.
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