SUMO Regulation of Cellular Processes

SUMO Regulation of Cellular Processes
Author: Van G. Wilson
Publisher: Springer
Total Pages: 413
Release: 2017-02-13
Genre: Medical
ISBN: 3319500449
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This is the second edition of a very well received book that details how the sumoylation system functions and how it modulates numerous cellular activities. SUMO is a post-translational modifier in the ubiquitin super-family that has gained recognition over the last twenty years as an essential and prevalent regulatory molecule. Individual chapters explore the biochemistry, molecular biology, and cell biology of the sumoylation system and its substrate proteins. The book is divided into three themed parts: Molecular Functions (I), Cell Growth Regulation (II), and Diseases (III). Parts I and II focus on the contribution of sumoylation to cellular activities in both the nuclear and cytoplasmic compartments. The nuclear activities covered include nucleic acid metabolism (both RNA and DNA), chromosome structure and replication, and nucleocytoplasmic transport. Cytoplasmic processes presented include regulation of membrane ion channels, general metabolism, and apoptotic signalling. Topics in Part III include the role of sumoylation in developmental abnormalities (craniofacial and cardiovascular), diabetes, neurodegenerative diseases, cancer, and infections with viruses and bacteria. Each of the corresponding chapter authors is an active researcher who has made significant contributions to understanding sumoylation. This second edition provides updates and revisions to most of the original chapters plus adds six new chapters to address important developing areas of sumoylation research. This volume is intended for a scientific audience from undergraduates to independent researchers. The content will serve as both a solid introduction for the novice reader and an in depth treatment for the advanced scholar.

SUMO

SUMO
Author: Manuel S. Rodriguez
Publisher: Humana
Total Pages: 0
Release: 2016-09-08
Genre: Science
ISBN: 9781493963560
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This volume explores various methodologies to study biochemical, molecular, and cellular biology aspects of some processes regulated by protein SUMOylation. SUMO: Methods and Protocols is organized into four parts, and starts with an historical overview on protein SUMOylation and a presentation of the methods included in the book. The first part also includes a review on chromatin regulation by dynamic SUMO modifications. The second part focuses on in vitro techniques, including biochemical methods to study mechanistic aspects of protein SUMOylation. The third part includes protocols to be used with cell cultures, which often are the first approaches used in most laboratories. The final part includes methodologies adapted for the analysis in vivo using distinct model organisms. Written in the highly successful Methods in Molecular Biology series format, chapters include a brief introduction to the subject, a list of necessary materials and reagents, a step-by-step reproducible laboratory protocol ending with a Notes section on troubleshooting tips, and tips and strategies to avoid known pitfalls. Unique and cutting-edge, SUMO: Methods and Protocols provides a comprehensive source of protocols for specialists and researchers not familiar with this vital system.

SUMO-1 Mapping in the Human Genome Andits Implications for Transcription Control

SUMO-1 Mapping in the Human Genome Andits Implications for Transcription Control
Author: Hui-Wen Liu
Publisher:
Total Pages:
Release: 2014
Genre:
ISBN:
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SUMOylation, a post-translational modification with SUMO proteins covalently conjugated to a variety of proteins, regulates a range of cellular processes, including cell proliferation and maintenance of genome stability. In this study, we investigated how SUMO-1 functions as a chromatin mark on the human genome during cell cycle progression by ChIP-seq approach. Surprisingly, despite the known repressive role of SUMOylation on histones, we found that SUMO-1 localizes to the promoters of constitutively active genes involved in protein translation and proliferation during interphase. For example, ribosomal protein genes; and SUMO-1 marks on these promoters were absent during mitosis. In addition, SUMO-1 association on the promoters recruits RNAPII, and depletion of SUMO-1 leads to down regulation of those ribosomal protein genes, suggesting a positive role of SUMO-1 in gene activation. To further elucidate how SUMOylation regulates transcription process related to protein synthesis, we identified that SUMO-1 marks the promoters via the Scaffold Associated Factor B (SAFB) protein. The results showed that SAFB is SUMOylated, and depletion of SAFB caused the decrease of SUMO-1 marks on the promoters of those housekeeping genes transcribed by RNAPII. In addition, depletion of SAFB decreased the splicing of the mRNAs and disrupted the organization of Cajal body, which is important for snRNP and snoRNP biogenesis. All these findings suggested that SUMOylation plays an important role in the regulatory process for transcription initiation and splicing of mRNA of ribosomal protein genes.

Characterization and Profiling of the SUMO Conjugation Pathway in Populus

Characterization and Profiling of the SUMO Conjugation Pathway in Populus
Author: Jon-Michael Reed
Publisher:
Total Pages:
Release: 2005
Genre:
ISBN:
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ABSTRACT: Covalent attachment of the Small Ubiquitin-like Modifier (SUMO) to proteins in eukaryotic cells has been demonstrated to be an important step in the regulation of a wide variety of cellular processes. Such processes include transcriptional regulation, mediating DNA/protein interaction, and increasing protein stability by interfering with the ubiquitin conjugation pathway in some cases. While much work has been done to characterize the SUMO pathway in yeast, insect, and mammalian systems, relatively little is known about the roles that SUMO conjugation plays in plants. In this study, I make use of the Populus model system to investigate the gene structures of the various family members of the SUMO pathway in plants, as well as demonstrate that the pathway is active in a number of tissue types. Additionally, we show that the SUMOylation is inducible through acute stress treatments such as desiccation, heat shock, and peroxide application. To further our understanding of the SUMOylation process, I have set out to identify SUMO-conjugated proteins from heat shock treated tissues through a multi-step purification process.

Investigating the Role of 14-3-3[zeta] SUMOylation

Investigating the Role of 14-3-3[zeta] SUMOylation
Author: Hoang Anh Phuc Nguyen
Publisher:
Total Pages: 39
Release: 2013
Genre:
ISBN:
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SUMO modification is involved in several cellular processes such as signal transduction, cell division, and regulation of protein subcellular localization, specifically including Ras signaling and protein nuclear import/export. Previous studies have demonstrated that 14-3-3[zeta], which is thought to have functions in both the nucleus and cytoplasm, is a SUMOylated protein and is required for Ras signaling. I have therefore sought to determine whether or not the SUMOylation of 14-3-3[zeta] promotes or inhibits its localization to the nucleus. Subcellular fractionation experiments fail to reveal a detectable change in the overall ratio of nuclear to cytoplasmic 14-3-3[zeta] upon knockdown of SUMO by RNAi in cultured Drosophila cells. However, immunofluorescence studies suggest that nuclear localization of this protein may increase in a subset of the SUMO knockdown cells.

SUMOylation and Ubiquitination

SUMOylation and Ubiquitination
Author: Van G. Wilson
Publisher:
Total Pages: 512
Release: 2019-09
Genre: Science
ISBN: 9781912530120
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Most proteins undergo post-translational modifications altering physical and chemical properties, folding, conformation distribution, stability, activity and function. Ubiquitin and SUMOs are related small proteins that are members of the large ubiquitin superfamily of post-translational modifiers. Written by highly respected leaders in their fields under the expert guidance of the editor, this volume covers the principles of ubiquitination and SUMOylation, presents detailed reviews of current and emerging concepts and highlights new advances in all areas of SUMOylation and ubiquitination. Topics of note include: the ubiquitin superfamily, the ubiquitin toolbox, onco viral exploitation of the SUMO system, small molecule modulators of desumoylation, mass spectrometry, global proteomic profiling of SUMO and ubiquitin, biotin-based approaches, genetic screening, SUMOylation networks in humans, targets for ubiquitin ligases, regulation of p53, protein homeostasis, miRNAs, DNA replication, DNA damage response, telomere biology, intracellular trafficking, regulation of angiogenesis, brain ischemia, autophagy, assembly and activity, antiviral defense, HIV infection, amyloid and amyloid-like proteins, plant immunity. This comprehensive and up-to-date book is the definitive reference volume on all aspects of SUMOylation and ubiquitination and is an essential acquisition for anyone involved in this area of biology.

mRNA Processing and Metabolism

mRNA Processing and Metabolism
Author: Daniel R. Schoenberg
Publisher: Humana
Total Pages: 270
Release: 2004-02-05
Genre: Science
ISBN: 9781588292254
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Cells possess a wealth of posttranscriptional control mechanisms that impact on every conceivable aspect of the life of an mRNA. These processes are intimately intertwined in an almost baroque manner, where promoter context influences the recruitment of splicing factors, where the majority of pre-mRNAs undergo alternative splicing, and where proteins deposited during nuclear processing impact distal cytoplasmic processing, translation, and decay. If there is a unifying theme to mRNA Processing and Metabolism: Methods and Protocols, it is that mRNA processing and metabolism are integrated processes. Many of the techniques used to study mRNA have been described in a previous volume of this series (RNA–Protein Interaction Protocols, Susan Haynes, ed.) and specialized methods journals. In selecting topics for mRNA Processing and Metabolism: Methods and Protocols, I sought input on new and novel techniques and approaches that build on this foundation using technological advances in microscopy, whole genome sequencing, microarrays, mass spectrometry, fluorescent detection methodologies, and RNA interference. I have tried not to bias this book toward any single model organism, and approaches described in the various chapters use yeast, Drosophila, Xenopus, mice, plants, and cultured mammalian cells.

Characterization of Arabidopsis SUMO Conjugation as Orchestrator of Nuclear Bodies and Transcription

Characterization of Arabidopsis SUMO Conjugation as Orchestrator of Nuclear Bodies and Transcription
Author: Magdalena Julita Mazur
Publisher:
Total Pages: 156
Release: 2016
Genre:
ISBN:
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Small ubiquitin-like modifier (SUMO) is a conserved post-translational modification that regulates many biological processes in animal, yeast and plant cells. SUMO can be covalently attached to its target proteins at lysine residues present in short consensus peptide motifs. To date, hundreds of proteins have been identified as bona fide SUMO targets for mammals. In Arabidopsis, however, more studies are required to fully understand the extent of SUMO regulation in plant cells. In this study we focused on analyses and further study of SUMO proteome in Arabidopsis. In chapter 2 of this thesis we analyzed the cellular processes that are regulated by sumoylation as well as we reviewed current strategies to study sumoylation. In chapter 3 we characterized the interaction interface between SUMO peptide (SUMO1) and enzymes involved in sumoylation: SCE1 and SIZ1. We demonstrated that the SUMO1∙SCE1∙SIZ1 complex resides in nuclear bodies (NBs), along with the ubiquitin E3 ligase COP1, a master regulator of photomorphogenesis. In order to identify new SUMO interactors and SUMO substrate, we performed high-throughput yeast 2-hybrid assay using SUMO peptide paralogs as well as SUMO (de)conjugation enzymes as baits. We found that SUMO machinery interacts with many transcriptional regulators belonging to many transcription factors (TFs) families (chapter 4) and well as with some important proteins involved in plant immunity (chapter 5) in nuclear bodies. We further analyze the found interactions in chapters 4 and 5. In chapter 6 we summarized the current knowledge on sub-nuclear structures and the potential role of SUMO in their biology.

Human Herpesviruses

Human Herpesviruses
Author: Ann Arvin
Publisher: Cambridge University Press
Total Pages: 1325
Release: 2007-08-16
Genre: Medical
ISBN: 1139461648
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This comprehensive account of the human herpesviruses provides an encyclopedic overview of their basic virology and clinical manifestations. This group of viruses includes human simplex type 1 and 2, Epstein–Barr virus, Kaposi's Sarcoma-associated herpesvirus, cytomegalovirus, HHV6A, 6B and 7, and varicella-zoster virus. The viral diseases and cancers they cause are significant and often recurrent. Their prevalence in the developed world accounts for a major burden of disease, and as a result there is a great deal of research into the pathophysiology of infection and immunobiology. Another important area covered within this volume concerns antiviral therapy and the development of vaccines. All these aspects are covered in depth, both scientifically and in terms of clinical guidelines for patient care. The text is illustrated generously throughout and is fully referenced to the latest research and developments.

Characterization of the Role of the Small Ubiquitin-like Modifier (SUMO) on Nuclear Localization and Proteolysis of the Thyroid Hormone Receptor (TR)

Characterization of the Role of the Small Ubiquitin-like Modifier (SUMO) on Nuclear Localization and Proteolysis of the Thyroid Hormone Receptor (TR)
Author: Amanda M. Back
Publisher:
Total Pages:
Release: 2017
Genre: Proteins
ISBN:
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The small ubiquitin-like modifier (SUMO) is involved in post-translational modification of proteins and is characterized by its role in regulation of a variety of cellular processes. The objective of this thesis was to characterize the role SUMO has in modification of the thyroid hormone receptor (TR). TR is a regulatory transcription factor that, in most cases when the ligand (T3) is not bound, represses gene expression through the recruitment of co-repressors. When T3 is bound to TR, the co-repressors are released and co-activators are recruited, resulting in positive gene expression mediated by a particular thyroid hormone response element (TRE). Previous research has identified the import and export proteins involved in nuclear localization of TR. Post-translational modification, however, has only begun to be characterized. In terms of proteolysis, TR is degraded through poly-ubiquitination; but it is unclear whether ubiquitin binding is correlated with sumoylation. SUMO sites for TR have been previously identified, and their role in TR-mediated gene expression demonstrated. Here, the role SUMO plays in nuclear localization and proteolysis of TR through its interaction with ubiquitin binding is characterized. Mutant constructs of TR that could not be sumoylated were synthesized and cloned into GFP. For nuclear localization assays, the constructs were transfected into HeLa cells and quantitatively scored for the ratio of fluorescence intensity in the nucleus versus the cytosol using region of interest (ROI) analysis. Coimmunoprecipitation followed by western analysis, was conducted in order to identify the relationship between sumoylation and ubiquitination. The nuclear localization experiments showed no changes in nuclear localization of the SUMO-deficient TR compared to the wild-type TR. Coimmunoprecipitation suggested that there may be a higher level of ubiquitination when TR was not sumoylated. However, varying levels of cellular ubiquitin make this finding inconclusive. Overall, this thesis demonstrates that SUMO is not directly involved in nuclear localization of TR; however, it may play a role in enhancing the binding of ubiquitin, ultimately suggesting that sumoylation may be involved in proteolysis of TR.