Sumo and the cellular stress response

The ubiquitin family member Sumo has important functions in many cellular processes including DNA repair, transcription and cell division. Numerous studies have shown that Sumo is essential for maintaining cell homeostasis when the cell encounters endogenous or environmental stress, such as osmotic stress, hypoxia, heat shock, genotoxic stress, and nutrient stress. Regulation of transcription is a key component of the Sumo stress response, and multiple mechanisms have been described by which Sumo can regulate transcription. Although many individual substrates have been described that are sumoylated during the Sumo stress response, an emerging concept is modification of entire complexes or pathways by Sumo. This review focuses on the function and regulation of Sumo during the stress response.

• Publication year

  2015

• Venue

  Cell Division

• Publication date

  2015-06-20

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1186/s13008-015-0010-1PMID 26101541PMCID 4476178
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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  2014cited by this paper
• Dynamic SUMO modification regulates mitotic chromosome assembly and cell cycle progression in Caenorhabditis elegans

  2014cited by this paper
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  2014cited by this paper
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  2014cited by this paper
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  2014cited by this paper
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  2014cited by this paper
• Uncovering Global SUMOylation Signaling Networks in a Site-Specific Manner

  2014cited by this paper
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  2013cited by this paper
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  2013cited by this paper
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  2013cited by this paper
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  2013cited by this paper
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  2013cited by this paper
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  2013influential reference
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  2013cited by this paper
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  2013cited by this paper
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  2013cited by this paper
• Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation

  2013cited by this paper
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  2013cited by this paper
• SENP1 deficiency promotes ER stress-induced apoptosis by increasing XBP1 SUMOylation

  2012cited by this paper
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  2012cited by this paper
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  2012cited by this paper
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  2012cited by this paper
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  2012influential reference
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  2012influential reference
• Extensive DNA damage-induced sumoylation contributes to replication and repair and acts in addition to the mec1 checkpoint.

  2012cited by this paper
• The unfolded protein response: controlling cell fate decisions under ER stress and beyond

  2012cited by this paper
• Phosphorylation of Ubc9 by Cdk1 Enhances SUMOylation Activity

  2012cited by this paper
• Human Pathogens and the Host Cell SUMOylation System

  2011cited by this paper
• Comparative Proteomic Analysis Identifies a Role for SUMO in Protein Quality Control

  2011cited by this paper
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  2011cited by this paper
• Target of Rapamycin (TOR) in Nutrient Signaling and Growth Control

  2011cited by this paper
• SUMO and SUMOylation in plants

  2011cited by this paper
• PML nuclear bodies.

  2010cited by this paper
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  2010cited by this paper
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  2010influential reference
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  2010cited by this paper
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  2010cited by this paper
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  2010cited by this paper
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  2010cited by this paper
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  2010cited by this paper
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  2009cited by this paper
• System-Wide Changes to SUMO Modifications in Response to Heat Shock

  2009cited by this paper
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  2009influential reference
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  2009cited by this paper
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• A Multidimensional Chromatography Technology for In-depth Phosphoproteome Analysis*S

  2008cited by this paper
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  2008cited by this paper
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  2008cited by this paper
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  2008cited by this paper
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  2008cited by this paper
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  2008cited by this paper
• A SIM-ultaneous role for SUMO and ubiquitin.

  2008cited by this paper
• Faculty Opinions recommendation of Arsenic degrades PML or PML-RARalpha through a SUMO-triggered RNF4/ubiquitin-mediated pathway.

  2008cited by this paper
• Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity

  2007cited by this paper
• Modification in reverse: the SUMO proteases.

  2007cited by this paper
• Proinflammatory Stimuli Induce IKKα-Mediated Phosphorylation of PIAS1 to Restrict Inflammation and Immunity

  2007cited by this paper
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  2007influential reference
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  2007cited by this paper
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  2007cited by this paper
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  2007cited by this paper
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  2007influential reference
• Review International Journal of Biological Sciences

  2007cited by this paper
• Stress-induced Inactivation of the c-Myb Transcription Factor through Conjugation of SUMO-2/3 Proteins*

  2006cited by this paper
• PIASy mediates NEMO sumoylation and NF-κB activation in response to genotoxic stress

  2006cited by this paper
• An extended consensus motif enhances the specificity of substrate modification by SUMO

  2006cited by this paper
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  2006cited by this paper
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• Specification of SUMO1- and SUMO2-interacting Motifs*

  2006cited by this paper
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  2006cited by this paper
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• PCNA controls establishment of sister chromatid cohesion during S phase.

  2006cited by this paper
• Insights into E3 ligase activity revealed by a SUMO–RanGAP1–Ubc9–Nup358 complex

  2005cited by this paper
• Defining the SUMO-modified Proteome by Multiple Approaches in Saccharomyces cerevisiae*

  2005cited by this paper
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  2005cited by this paper
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  2005cited by this paper
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  2005cited by this paper
• SUMO promotes HDAC-mediated transcriptional repression.

  2004cited by this paper
• SUMO and ubiquitin in the nucleus: different functions, similar mechanisms?

  2004cited by this paper
• Global Analyses of Sumoylated Proteins in Saccharomyces cerevisiae

  2004cited by this paper
• Identification of a SUMO-binding motif that recognizes SUMO-modified proteins.

  2004cited by this paper
• Growth-regulated recruitment of the essential yeast ribosomal protein gene activator Ifh1

  2004cited by this paper
• The transcription factor Ifh1 is a key regulator of yeast ribosomal protein genes

  2004cited by this paper
• A mechanism for inhibiting the SUMO pathway.

  2004cited by this paper
• Sequential modification of NEMO/IKKgamma by SUMO-1 and ubiquitin mediates NF-kappaB activation by genotoxic stress.

  2003cited by this paper
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  2003cited by this paper
• DNA helicase Srs2 disrupts the Rad51 presynaptic filament

  2003cited by this paper
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  2002cited by this paper
• Identification of a Multifunctional Binding Site on Ubc9p Required for Smt3p Conjugation*

  2002cited by this paper
• SUMO-1 Modification of Histone Deacetylase 1 (HDAC1) Modulates Its Biological Activities*

  2002cited by this paper
• Effects of Promyelocytic Leukemia Protein on Virus-Host Balance

  2002cited by this paper
• Identification of a Substrate Recognition Site on Ubc9*

  2002cited by this paper
• RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO

  2002cited by this paper

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  2025cites this paper
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  2025influential citation
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  2024cites this paper
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  2024cites this paper
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  2024cites this paper
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  2024cites this paper
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  2023cites this paper
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  2023cites this paper
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  2023cites this paper
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  2023cites this paper
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  2023cites this paper
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  2023cites this paper
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  2023cites this paper
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  2023cites this paper
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  2023cites this paper
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  2023cites this paper
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  2023cites this paper
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  2022cites this paper
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  2022cites this paper
• Natural Products Against Renal Fibrosis via Modulation of SUMOylation

  2022cites this paper
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  2022cites this paper
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  2022cites this paper
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  2022cites this paper
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  2022cites this paper
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• Cancer-Associated Dysregulation of Sumo Regulators: Proteases and Ligases

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• SUMO conjugation regulates immune signalling

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