Journal ArticleDOI
Nuclear and unclear functions of SUMO.
Jacob-S. Seeler,Anne Dejean +1 more
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TLDR
This work has shown that post-translational modification by the ubiquitin-like SUMO protein is emerging as a defining feature of eukaryotic cells.Abstract:
Post-translational modification by the ubiquitin-like SUMO protein is emerging as a defining feature of eukaryotic cells. Sumoylation has crucial roles in the regulatory challenges that face nucleate cells, including the control of nucleocytoplasmic signalling and transport and the faithful replication of a large and complex genome, as well as the regulation of gene expression.read more
Citations
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Regulation of chromatin by histone modifications
TL;DR: The known histone modifications are described, where they are found genomically and discussed and some of their functional consequences are discussed, concentrating mostly on transcription where the majority of characterisation has taken place.
Journal ArticleDOI
Protein Modification by SUMO
TL;DR: The current understanding of how SUMO conjugation is controlled, as well as the roles of SUMO in a number of biological processes are discussed.
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Concepts in sumoylation: a decade on
TL;DR: A decade has passed since SUMO was discovered to be a reversible post-translational protein modifier and many enzymes that participate in regulated SUMO-conjugation and -deconjugation pathways have been identified and characterized.
Journal ArticleDOI
Trinucleotide Repeat Disorders
Harry T. Orr,Huda Y. Zoghbi +1 more
TL;DR: It is exciting that within a span of 15 years, pathogenesis studies of this class of disorders are beginning to reveal pathways that are potential therapeutic targets.
Journal ArticleDOI
Ubiquitin: structures, functions, mechanisms.
TL;DR: The basic biochemistry of these protein conjugation reactions is reviewed, focusing on ubiquitin itself and emphasizing recent insights into mechanism and specificity.
References
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Journal ArticleDOI
RAD6 -dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
TL;DR: It is shown that UBC9, a small ubiquitin-related modifier (SUMO)-conjugating enzyme, is also affiliated with this pathway and that proliferating cell nuclear antigen (PCNA) is a substrate, and that damage-induced PCNA ubiquitination is elementary for DNA repair and occurs at the same conserved residue in yeast and humans.
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RING finger proteins: mediators of ubiquitin ligase activity.
TL;DR: The field of intracellular protein degradation now leaves the era where mediators of substrate-specific ubiquitination were scarce and enters a new and exciting phase where databases provide us with a large number of candidate E3s awaiting characterization.
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Protein regulation by monoubiquitin
TL;DR: Multi-ubiquitin chains at least four subunits long are required for efficient recognition and degradation of ubiquitylated proteins by the proteasome, but other functions of ubiquitin have been discovered that do not involve the protease.
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A Small Ubiquitin-Related Polypeptide Involved in Targeting RanGAP1 to Nuclear Pore Complex Protein RanBP2
TL;DR: It is found that the mammalian Ran GTPase-activating protein RanGAP1 is highly concentrated at the cytoplasmic periphery of the nuclear pore complex (NPC), where it associates with the 358-kDa Ran-GTP-binding protein RanBP2, indicating that GTP hydrolysis by Ran at Ran BP2 is required for nuclear protein import.
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A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex.
TL;DR: The identification and localization of a novel form of RanGAP1, a nuclear Ras-like GTPase that is required for the bidirectional transport of proteins and ribnucleoproteins across the nuclear pore complex (NPC), was reported.