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Cellular and Immunobiology
Published in Karl H. Pang, Nadir I. Osman, James W.F. Catto, Christopher R. Chapple, Basic Urological Sciences, 2021
Masood Moghul, Sarah McClelland, Prabhakar Rajan
Post-translational modifications modify existing proteins by adding/removing molecules.Can change both structure and function of proteins.Common methods include phosphorylation, ubiquitylation, and sumoylation.
Evaluating the Interactions of Silver Nanoparticles and Mammalian Cells Based on Biomics Technologies
Published in Huiliang Cao, Silver Nanoparticles for Antibacterial Devices, 2017
After genomics and transcriptomics, proteomics is the next step in the study of biological systems. Proteomics is the large-scale study of proteins within a cell, tissue or organism, which was first defined in 1995. It is a rapidly evolving field focussed on identification and characterisation of these proteins and their proteoforms. Quantitative methods in proteomics have enabled comparative analysis of protein expression profiles, providing information of cells and proteins in different stages of bio-production (Landels et al. 2015). Verano-Braga et al. used mass spectrometry–based proteomic technologies to investigate the Ag NP–protein interaction in human LoVo cells. The data indicated that 100-nm nanoparticles played indirect effects via three pathways. Twenty-nanometre nanoparticles induced direct effects on cellular stress and up-regulated the expression of proteins involved in SUMOylation. Protein ubiquitination and degradation were triggered by both 20- and 100-nm nanoparticles (Verano-Braga et al. 2014). Miethling-Graff et al. (2014) evaluated the cellular proteomic response of the human LoVo cell line to 10 μg/mL Ag NPs (size, 20 and 100 nm) for 24 h using iTRAQ-based proteomics technology. It was found that Ag NPs down-regulated the expression of mitochondrial proteins. The influence of 20-nm Ag NPs on cell death and mitochondrial activity–related proteins and ATP synthesis was stronger than that of 100-nm Ag NPs.
Introduction to Cell Biology
Published in Anthony R. Mundy, John M. Fitzpatrick, David E. Neal, Nicholas J. R. George, The Scientific Basis of Urology, 2010
SUMO (small ubiquitin-related modifier) is a small molecular weight protein that is structurally related to ubiquitin, and indeed many similarities exist between the two in terms of ligation and lysine attachment. The role of SUMOylation appears to be substrate specific; however, it has been implicated as a negative regulator of transcription, potentially by promoting the interaction of transcription factors with corepressors. Cross talk with another mechanism of posttranslation modification, acetylation, may compete with SUMO for binding, and many have antagonistic effects. Acetylation occurs when an acetyl group (CH3CO) is covalently attached to lysine and this process is catalyzed by a group of enzymes known as acetyl transferases. Acetylation protects proteins from rapid digestion by intracellular proteases, although other functions for this modification are being revealed.
Fatty acids produced by the gut microbiota dampen host inflammatory responses by modulating intestinal SUMOylation
Published in Gut Microbes, 2022
Chaima Ezzine, Léa Loison, Nadine Montbrion, Christine Bôle-Feysot, Pierre Déchelotte, Moïse Coëffier, David Ribet
SUMOylation is a ubiquitin-like modification consisting in the covalent addition of SUMO (Small Ubiquitin-like MOdifier) peptides to target proteins. Five SUMO paralogs have been identified in humans that share 45–97% sequence identity. SUMO1, SUMO2, and SUMO3, which are the most studied paralogs, can be conjugated to both overlapping and distinct sets of proteins.12 The conjugation of SUMO to lysine residues of target proteins is catalyzed by an enzymatic machinery composed of one E1 enzyme (SAE1/SAE2), one E2 enzyme (UBC9), and several E3 enzymes.13 SUMOylation is a reversible modification as the isopeptide bond between SUMO and its target can be cleaved by specific proteases called deSUMOylases.14 The consequences of SUMO conjugation on target proteins are very diverse and include changes in protein localization, stability, activity, or interactions with other cellular components.12,15,16
Small ubiquitin-related modifier (SUMO) 3 and SUMO4 gene polymorphisms in Parkinson’s disease
Published in Neurological Research, 2020
Cem Ismail Küçükali, Burcu Salman, Hande Yüceer, Canan Ulusoy, Neslihan Abacı, Sema Sırma Ekmekci, Erdem Tüzün, Başar Bilgiç, Haşmet Ayhan Hanağası
In this context, significance of SUMO and sumoylation in neurodegenerative disorders has been recently scrutinized. Although PD cases are mostly sporadic, several genes have also been associated with familial types of disease. α-synuclein, DJ-1 and parkin are three of these genes and are target proteins for SUMO, indicating the role of this molecule in the molecular mechanisms of PD pathogenesis [21,22]. SUMO proteins bind to a large number of cellular targets. It modulates protein-protein and protein-DNA interactions, modifies intracellular localizations of proteins and protects cells from ubiquitin-induced degradation [11,12]. Sumoylation is functionally a more varied modifier than ubiquitination and unlike ubiquitination, proteins do not directly target the proteasome. Instead, sumoylation blocks proteasomal degradation by competing with ubiquitination for a common lysine residue and substrate samples are used for this process [5,23]. SUMO and ubiquitin also have a variety of functional and structural properties that play a role in the regulation and coordination of different stages of DNA damage recognition and repair, regulation of replication and replication stress, protection of genomic stability, and various other cellular events [14,23].
Patented therapeutic approaches targeting LRP/LR for cancer treatment
Published in Expert Opinion on Therapeutic Patents, 2019
Leila Vania, Gavin Morris, Tyrone C Otgaar, Monique J Bignoux, Martin Bernert, Jessica Burns, Anne Gabathuse, Elvira Singh, Eloise Ferreira, Stefan F T Weiss
Despite the extensive research on LRP/LR, there are still many avenues that can be explored to target the receptor. In particular, the formation of the mature 67 kDa LR has been of great interest. At first, sumoylation was thought to contribute to the maturation of 37 kDa LRP to LR, however due to the difficulty in obtaining tagged mature LR directly; evidence of the involvement of sumoylation in 37 kDa LRP maturation is inconclusive. Despite this, recent work has shown that sumoylation does play a significant role in regulating the life-time of 37 kDa LRP in the cell [176]. The sumoylation sites play antagonistic roles where sumoylation at K11 results in an increased 37 kDa LRP lifespan and targeted proteosomal degradation of 37 kDa LRP when K42 is sumoylated. In addition, sumoylation of several putative sumoylation sites is necessary for efficient processing of 18S, 45S, 47S and 5.8S rRNAs. This presents a novel two-pronged avenue of targeting 37 kDa LRP in a therapeutic capacity. By targeting the putative sumoylation sites it may be possible to control sumoylation of 37 kDa LRP thereby altering the life expectancy of 37 kDa LRP and potentially preventing its maturation to the oncogenic LR (Figure 7). Given this, the prevention of sumoylation may reduce rRNA processing hindering ribosomal assembly and subsequently protein synthesis rates in cancerous cells, ultimately leading to a reduction in these cancer cells.