SUMO-2 promotes mRNA translation by enhancing interaction between eIF4E and eIF4G. [PDF]
PLoS ONE, 2014 Small ubiquitin-like modifier (SUMO) proteins regulate many important eukaryotic cellular processes through reversible covalent conjugation to target proteins.
Li-zhao Chen +12 more
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SUMOylation is required for glycine-induced increases in AMPA receptor surface expression (ChemLTP) in hippocampal neurons. [PDF]
PLoS ONE, 2013 Multiple pathways participate in the AMPA receptor trafficking that underlies long-term potentiation (LTP) of synaptic transmission. Here we demonstrate that protein SUMOylation is required for insertion of the GluA1 AMPAR subunit following transient ...
Nadia Jaafari +7 more
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Intracellular delivery of peptides via association with ubiquitin or SUMO-1 coupled to protein transduction domains [PDF]
BMC Biotechnology, 2008 Background We previously developed small hybrid proteins consisting of SUMO-1 linked to an heptapeptide fused to the Tat protein transduction domain (PTD).
Jalinot Pierre, Vitte Anne-Laure
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Expression, Localization of SUMO-1, and Analyses of Potential SUMOylated Proteins in Bubalus bubalis Spermatozoa [PDF]
Frontiers in Physiology, 2017 Mature spermatozoa have highly condensed DNA that is essentially silent both transcriptionally and translationally. Therefore, post translational modifications are very important for regulating sperm motility, morphology, and for male fertility in ...
Rahim Dad Brohi +18 more
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SUMO-4: A novel functional candidate in the human placental protein SUMOylation machinery. [PDF]
PLoS ONE, 2017 BACKGROUND:Small ubiquitin-like modifiers (SUMOs) conjugate to proteins post-translationally, thereby affecting target localization, activity and stability.
Dora Baczyk +4 more
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A Photo-Crosslinking Approach to Identify Class II SUMO-1 Binders
Frontiers in Chemistry, 2022 The small ubiquitin-like modifier (SUMO) is involved in various cellular processes and mediates known non-covalent protein-protein interactions by three distinct binding surfaces, whose interactions are termed class I to class III.
Kira Brüninghoff +4 more
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A Central Cysteine Residue Is Essential for the Thermal Stability and Function of SUMO-1 Protein and SUMO-1 Peptide–Protein Conjugates [PDF]
Bioconjugate Chemistry, 2016 SUMOylation constitutes a major post-translational modification (PTM) used by the eukaryote cellular machinery to modulate protein interactions of the targeted proteins. The small ubiquitin-like modifier-1 (SUMO-1) features a central and conserved cysteine residue (Cys52) that is located in the hydrophobic core of the protein and in tight contact with ...
Drobecq, Hervé +8 more
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Tomosyn interacts with the SUMO E3 ligase PIASγ. [PDF]
PLoS ONE, 2014 Protein modification by Small Ubiquitin-like MOdifier (SUMO) entities is involved in a number of neuronal functions, including synaptogenesis and synaptic plasticity. Tomosyn-1 (syntaxin-binding protein 5; STXPB5) binds to t-SNARE (Soluble NSF Attachment
Cornelia J Geerts +4 more
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Generation of SUMO‐1 modified proteins in E. coli: towards understanding the biochemistry/structural biology of the SUMO‐1 pathway [PDF]
FEBS Letters, 2004 Here, we developed a binary vector system that introduces a synthetic SUMO‐1 conjugation pathway into Escherichia coli and demonstrated that large amounts of sumoylated Ran GTPase activating protein 1 C‐terminal region (RanGAP1‐C2), Ran binding protein 2 internal repeat domain, p53 and promyelocytic leukemia were efficiently produced.
Uchimura, Yasuhiro +2 more
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Proteomics Analysis of Nucleolar SUMO-1 Target Proteins upon Proteasome Inhibition [PDF]
Molecular & Cellular Proteomics, 2009 Many cellular processes are regulated by the coordination of several post-translational modifications that allow a very fine modulation of substrates. Recently it has been reported that there is a relationship between sumoylation and ubiquitination.
Matafora, Vittoria +4 more
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