Special Issue "Protein SUMOylation"

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A special issue of Biomolecules (ISSN 2218-273X).

Deadline for manuscript submissions: closed (28 February 2012)

Special Issue Editor

Guest Editor
Prof. Dr. Seth Blackshaw (Website)

Associate Professor, Department of Neuroscience, Johns Hopkins University, School of Medicine, BRB 332 733 N. Broadway Avenue, Baltimore, MD 21287, USA
Fax: (410) 502-1872
Interests: transcriptional control of neural and glial development; protein SUMOylation; noncoding RNAs; functional proteomics; chronobiology

Special Issue Information

Dear Colleagues,

SUMOylation has emerged as a reversible and widely used means of modulating the activity and localization of many different classes of protein. Originally thought to primarily regulate nuclear processes such as transcription and DNA repair, recent work has revealed that SUMOylation plays a critical role in such diverse functions as regulating kinase and G-protein activity, cytoskeletal structure and ion channel function. It is now appreciated that site-specific SUMOylation guides cellular differentiation, regulates neuronal activity, and is misregulated in a range of human diseases. This issue intends to both review recent findings and to showcase original research in this fast moving field.

We thus invite submission of research and review manuscripts that cover any aspect of the biochemistry, cell biology, genetics or pharmacology of SUMO, SUMOylation enzymes and their cellular substrates and effector molecules. Areas of particular interest include, but are not limited to, advances in SUMOylation-dependent regulation of transcription factor activity and chromatin structure, dynamic regulation of SUMOylation by intracellular signaling, novel functional classes of proteins regulated by SUMOylation, and the role of SUMOylation in embryonic development, cancer and neurodegeneration. Other potential topics include the biology of the growing number of E3 SUMO ligases, SUMO binding proteins, and new genetic and pharmacological techniques for modulating protein SUMOylation in vivo.

We look forward to reading your contributions,

Prof. Dr. Seth Blackshaw
Guest Editor

Keywords

  • SUMO and SUMOylation
  • cytoskeleton
  • neurodegeneration
  • development and differentiation
  • ion channel and synapse
  • proteomics cell dynamics
  • Transcription and gene expression
  • protein transport stability and structure
  • ubiquitin, acetylation,  phosphorylation, and post-translational modification
  • protease
  • chromatin and epigenetics
  • signal transduction

Published Papers (8 papers)

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Research

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Open AccessArticle SUMOylation in Giardia lamblia: A Conserved Post-Translational Modification in One of the Earliest Divergent Eukaryotes
Biomolecules 2012, 2(3), 312-330; doi:10.3390/biom2030312
Received: 16 June 2012 / Revised: 5 July 2012 / Accepted: 13 July 2012 / Published: 25 July 2012
Cited by 1 | PDF Full-text (1223 KB) | HTML Full-text | XML Full-text
Abstract
Post-translational modifications are able to regulate protein function and cellular processes in a rapid and reversible way. SUMOylation, the post-translational modification of proteins by the addition of SUMO, is a highly conserved process that seems to be present in modern cells. However, [...] Read more.
Post-translational modifications are able to regulate protein function and cellular processes in a rapid and reversible way. SUMOylation, the post-translational modification of proteins by the addition of SUMO, is a highly conserved process that seems to be present in modern cells. However, the mechanism of protein SUMOylation in earlier divergent eukaryotes, such as Giardia lamblia, is only starting to become apparent. In this work, we report the presence of a single SUMO gene encoding to SUMO protein in Giardia. Monoclonal antibodies against recombinant Giardia SUMO protein revealed the cytoplasmic localization of native SUMO in wild-type trophozoites. Moreover, the over-expression of SUMO protein showed a mainly cytoplasmic localization, though also neighboring the plasma membrane, flagella, and around and even inside the nuclei. Western blot assays revealed a number of SUMOylated proteins in a range between 20 and 120 kDa. The genes corresponding to putative enzymes involved in the SUMOylation pathway were also explored. Our results as a whole suggest that SUMOylation is a process conserved in the eukaryotic lineage, and that its study is significant for understanding the biology of this interesting parasite and the role of post-translational modification in its evolution. Full article
(This article belongs to the Special Issue Protein SUMOylation)
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Open AccessArticle DeSUMOylation Controls Insulin Exocytosis in Response to Metabolic Signals
Biomolecules 2012, 2(2), 269-281; doi:10.3390/biom2020269
Received: 3 May 2012 / Revised: 14 May 2012 / Accepted: 16 May 2012 / Published: 24 May 2012
Cited by 4 | PDF Full-text (475 KB) | HTML Full-text | XML Full-text
Abstract
The secretion of insulin by pancreatic islet β-cells plays a pivotal role in glucose homeostasis and diabetes. Recent work suggests an important role for SUMOylation in the control of insulin secretion from β-cells. In this paper we discuss mechanisms whereby (de)SUMOylation may [...] Read more.
The secretion of insulin by pancreatic islet β-cells plays a pivotal role in glucose homeostasis and diabetes. Recent work suggests an important role for SUMOylation in the control of insulin secretion from β-cells. In this paper we discuss mechanisms whereby (de)SUMOylation may control insulin release by modulating β-cell function at one or more key points; and particularly through the acute and reversible regulation of the exocytotic machinery. Furthermore, we postulate that the SUMO-specific protease SENP1 is an important mediator of insulin exocytosis in response to NADPH, a metabolic secretory signal and major determinant of β-cell redox state. Dialysis of mouse β-cells with NADPH efficiently amplifies β-cell exocytosis even when extracellular glucose is low; an effect that is lost upon knockdown of SENP1. Conversely, over-expression of SENP1 itself augments β-cell exocytosis in a redox-dependent manner. Taken together, we suggest that (de)SUMOylation represents an important mechanism that acutely regulates insulin secretion and that SENP1 can act as an amplifier of insulin exocytosis. Full article
(This article belongs to the Special Issue Protein SUMOylation)
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Review

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Open AccessReview SUMOylation in Drosophila Development
Biomolecules 2012, 2(3), 331-349; doi:10.3390/biom2030331
Received: 13 June 2012 / Revised: 23 June 2012 / Accepted: 25 June 2012 / Published: 25 July 2012
Cited by 3 | PDF Full-text (575 KB) | HTML Full-text | XML Full-text
Abstract
Small ubiquitin-related modifier (SUMO), an ~90 amino acid ubiquitin-like protein, is highly conserved throughout the eukaryotic domain. Like ubiquitin, SUMO is covalently attached to lysine side chains in a large number of target proteins. In contrast to ubiquitin, SUMO does not have [...] Read more.
Small ubiquitin-related modifier (SUMO), an ~90 amino acid ubiquitin-like protein, is highly conserved throughout the eukaryotic domain. Like ubiquitin, SUMO is covalently attached to lysine side chains in a large number of target proteins. In contrast to ubiquitin, SUMO does not have a direct role in targeting proteins for proteasomal degradation. However, like ubiquitin, SUMO does modulate protein function in a variety of other ways. This includes effects on protein conformation, subcellular localization, and protein–protein interactions. Significant insight into the in vivo role of SUMOylation has been provided by studies in Drosophila that combine genetic manipulation, proteomic, and biochemical analysis. Such studies have revealed that the SUMO conjugation pathway regulates a wide variety of critical cellular and developmental processes, including chromatin/chromosome function, eggshell patterning, embryonic pattern formation, metamorphosis, larval and pupal development, neurogenesis, development of the innate immune system, and apoptosis. This review discusses our current understanding of the diverse roles for SUMO in Drosophila development. Full article
(This article belongs to the Special Issue Protein SUMOylation)
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Open AccessReview SUMO Wrestles with Recombination
Biomolecules 2012, 2(3), 350-375; doi:10.3390/biom2030350
Received: 10 June 2012 / Revised: 27 June 2012 / Accepted: 13 July 2012 / Published: 25 July 2012
Cited by 4 | PDF Full-text (1095 KB) | HTML Full-text | XML Full-text
Abstract
DNA double-strand breaks (DSBs) comprise one of the most toxic DNA lesions, as the failure to repair a single DSB has detrimental consequences on the cell. Homologous recombination (HR) constitutes an error-free repair pathway for the repair of DSBs. On the other [...] Read more.
DNA double-strand breaks (DSBs) comprise one of the most toxic DNA lesions, as the failure to repair a single DSB has detrimental consequences on the cell. Homologous recombination (HR) constitutes an error-free repair pathway for the repair of DSBs. On the other hand, when uncontrolled, HR can lead to genome rearrangements and needs to be tightly regulated. In recent years, several proteins involved in different steps of HR have been shown to undergo modification by small ubiquitin-like modifier (SUMO) peptide and it has been suggested that deficient sumoylation impairs the progression of HR. This review addresses specific effects of sumoylation on the properties of various HR proteins and describes its importance for the homeostasis of DNA repetitive sequences. The article further illustrates the role of sumoylation in meiotic recombination and the interplay between SUMO and other post-translational modifications. Full article
(This article belongs to the Special Issue Protein SUMOylation)
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Open AccessReview Regulation of Neuronal Protein Trafficking and Translocation by SUMOylation
Biomolecules 2012, 2(2), 256-268; doi:10.3390/biom2020256
Received: 14 April 2012 / Revised: 24 April 2012 / Accepted: 24 April 2012 / Published: 14 May 2012
Cited by 1 | PDF Full-text (646 KB) | HTML Full-text | XML Full-text
Abstract
Post-translational modifications of proteins are essential for cell function. Covalent modification by SUMO (small ubiquitin-like modifier) plays a role in multiple cell processes, including transcriptional regulation, DNA damage repair, protein localization and trafficking. Factors affecting protein localization and trafficking are particularly crucial [...] Read more.
Post-translational modifications of proteins are essential for cell function. Covalent modification by SUMO (small ubiquitin-like modifier) plays a role in multiple cell processes, including transcriptional regulation, DNA damage repair, protein localization and trafficking. Factors affecting protein localization and trafficking are particularly crucial in neurons because of their polarization, morphological complexity and functional specialization. SUMOylation has emerged as a major mediator of intranuclear and nucleo-cytoplasmic translocations of proteins involved in critical pathways such as circadian rhythm, apoptosis and protein degradation. In addition, SUMO-regulated re-localization of extranuclear proteins is required to sustain neuronal excitability and synaptic transmission. Thus, SUMOylation is a key arbiter of neuronal viability and function. Here, we provide an overview of recent advances in our understanding of regulation of neuronal protein localization and translocation by SUMO and highlight exciting areas of ongoing research. Full article
(This article belongs to the Special Issue Protein SUMOylation)
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Open AccessReview The Role of the Small Ubiquitin-Related Modifier (SUMO) Pathway in Prostate Cancer
Biomolecules 2012, 2(2), 240-255; doi:10.3390/biom2020240
Received: 15 March 2012 / Revised: 28 March 2012 / Accepted: 9 April 2012 / Published: 23 April 2012
PDF Full-text (291 KB) | HTML Full-text | XML Full-text
Abstract
SUMO (small ubiquitin-related modifier) conjugation is a reversible three-step process of protein post-translational modifications mediating protein-protein interactions, subcellular compartmentalization and regulation of transcriptional events. Among divergent transcription factors regulated by SUMOylation and deSUMOylation, the androgen receptor (AR) is of exceptional significance, given [...] Read more.
SUMO (small ubiquitin-related modifier) conjugation is a reversible three-step process of protein post-translational modifications mediating protein-protein interactions, subcellular compartmentalization and regulation of transcriptional events. Among divergent transcription factors regulated by SUMOylation and deSUMOylation, the androgen receptor (AR) is of exceptional significance, given its established role in prostate carcinogenesis. The enzymes of the SUMO pathway can have diverse effects on AR transcriptional activity, either via direct modification of the AR or through modification of AR co-regulators. Accumulating in vitro and in vivo evidence implicates the SUMO pathway in AR-dependent signaling. Prostate cancer cell proliferation and hypoxia-induced angiogenesis are also regulated by the SUMO pathway, through an AR-independent mechanism. Thus, an important role has been revealed for members of the SUMO pathway in prostate cancer (PCa) development and progression, offering new therapeutic targets. Full article
(This article belongs to the Special Issue Protein SUMOylation)
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Open AccessReview Sumoylation at the Host-Pathogen Interface
Biomolecules 2012, 2(2), 203-227; doi:10.3390/biom2020203
Received: 21 February 2012 / Revised: 21 March 2012 / Accepted: 27 March 2012 / Published: 5 April 2012
Cited by 11 | PDF Full-text (680 KB) | HTML Full-text | XML Full-text
Abstract
Many viral proteins have been shown to be sumoylated with corresponding regulatory effects on their protein function, indicating that this host cell modification process is widely exploited by viral pathogens to control viral activity. In addition to using sumoylation to regulate their [...] Read more.
Many viral proteins have been shown to be sumoylated with corresponding regulatory effects on their protein function, indicating that this host cell modification process is widely exploited by viral pathogens to control viral activity. In addition to using sumoylation to regulate their own proteins, several viral pathogens have been shown to modulate overall host sumoylation levels. Given the large number of cellular targets for SUMO addition and the breadth of critical cellular processes that are regulated via sumoylation, viral modulation of overall sumoylation presumably alters the cellular environment to ensure that it is favorable for viral reproduction and/or persistence. Like some viruses, certain bacterial plant pathogens also target the sumoylation system, usually decreasing sumoylation to disrupt host anti-pathogen responses. The recent demonstration that Listeria monocytogenes also disrupts host sumoylation, and that this is required for efficient infection, extends the plant pathogen observations to a human pathogen and suggests that pathogen modulation of host sumoylation may be more widespread than previously appreciated. This review will focus on recent aspects of how pathogens modulate the host sumoylation system and how this benefits the pathogen. Full article
(This article belongs to the Special Issue Protein SUMOylation)
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Open AccessReview Fucosylation Is a Promising Target for Cancer Diagnosis and Therapy
Biomolecules 2012, 2(1), 34-45; doi:10.3390/biom2010034
Received: 30 November 2011 / Revised: 5 January 2012 / Accepted: 20 January 2012 / Published: 30 January 2012
Cited by 23 | PDF Full-text (336 KB) | HTML Full-text | XML Full-text
Abstract
Oligosaccharides, sequences of carbohydrates conjugated to proteins and lipids, are arguably the most abundant and structurally diverse class of molecules. Fucosylation is one of the most important oligosaccharide modifications involved in cancer and inflammation. Recent advances in glycomics have identified several types [...] Read more.
Oligosaccharides, sequences of carbohydrates conjugated to proteins and lipids, are arguably the most abundant and structurally diverse class of molecules. Fucosylation is one of the most important oligosaccharide modifications involved in cancer and inflammation. Recent advances in glycomics have identified several types of glyco-biomarkers containing fucosylation that are linked to certain types of cancer. Fucosylated alpha-fetoprotein (AFP) is widely used in the diagnosis of hepatocellular carcinoma because it is more specific than alpha-fetoprotein. High levels of fucosylated haptoglobin have also been found in sera of patients with various carcinomas. We have recently established a simple lectin-antibody ELISA to measure fucosylated haptoglobin and to investigate its clinical use. Cellular fucosylation is dependent upon fucosyltransferase activity and the level of its donor substrate, guanosine diphosphate (GDP)-fucose. GDP-mannose-4,6-dehydratase (GMDS) is a key enzyme involved in the synthesis of GDP-fucose. Mutations of GMDS found in colon cancer cells induced a malignant phenotype, leading to rapid growth in athymic mice resistant to natural killer cells. This review describes the role of fucosylated haptoglobin as a cancer biomarker, and discusses the possible biological role of fucosylation in cancer development. Full article
(This article belongs to the Special Issue Protein SUMOylation)
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