keyword
https://read.qxmd.com/read/33099299/sumo-proteins-in-the-cardiovascular-system-friend-or-foe
#1
REVIEW
Prithviraj Manohar Vijaya Shetty, Ashraf Yusuf Rangrez, Norbert Frey
Post-translational modifications (PTMs) are crucial for the adaptation of various signalling pathways to ensure cellular homeostasis and proper adaptation to stress. PTM is a covalent addition of a small chemical functional group such as a phosphate group (phosphorylation), methyl group (methylation), or acetyl group (acetylation); lipids like hydrophobic isoprene polymers (isoprenylation); sugars such as a glycosyl group (glycosylation); or even small peptides such as ubiquitin (ubiquitination), SUMO (SUMOylation), NEDD8 (neddylation), etc...
October 24, 2020: Journal of Biomedical Science
https://read.qxmd.com/read/32961230/ubiquitination-in-rheumatoid-arthritis
#2
REVIEW
Tapan Behl, Swati Chadha, Monika Sachdeva, Arun Kumar, Abdul Hafeez, Vineet Mehta, Simona Bungau
Rheumatoid arthritis is a chronic, inflammatory joint disease leading to inflammation of synovial membrane that lines the joints. This inflammation further progresses and results in destruction of joints and surrounding cartilages. The underlying factors can be oxidative stress, pro-inflammatory mediators, imbalance and attenuation between various enzymes and proteins (like nuclear factor erythroid 2 related factor 2/Nrf2 and ubiquitin). Protein degradation pathways comprises of lysosomal, proteasomal pathway, and autophagosome (that are carried out in mammalian cells) are regulated through ubiquitin...
November 15, 2020: Life Sciences
https://read.qxmd.com/read/32957626/emerging-roles-of-usp18-from-biology-to-pathophysiology
#3
REVIEW
Ji An Kang, Young Joo Jeon
Eukaryotic proteomes are enormously sophisticated through versatile post-translational modifications (PTMs) of proteins. A large variety of code generated via PTMs of proteins by ubiquitin (ubiquitination) and ubiquitin-like proteins (Ubls), such as interferon (IFN)-stimulated gene 15 (ISG15), small ubiquitin-related modifier (SUMO) and neural precursor cell expressed, developmentally downregulated 8 (NEDD8), not only provides distinct signals but also orchestrates a plethora of biological processes, thereby underscoring the necessity for sophisticated and fine-tuned mechanisms of code regulation...
September 17, 2020: International Journal of Molecular Sciences
https://read.qxmd.com/read/32708614/regulation-of-histone-ubiquitination-in-response-to-dna-double-strand-breaks
#4
REVIEW
Lanni Aquila, Boyko S Atanassov
Eukaryotic cells are constantly exposed to both endogenous and exogenous stressors that promote the induction of DNA damage. Of this damage, double strand breaks (DSBs) are the most lethal and must be efficiently repaired in order to maintain genomic integrity. Repair of DSBs occurs primarily through one of two major pathways: non-homologous end joining (NHEJ) or homologous recombination (HR). The choice between these pathways is in part regulated by histone post-translational modifications (PTMs) including ubiquitination...
July 16, 2020: Cells
https://read.qxmd.com/read/32483380/site-specific-ubiquitination-affects-protein-energetics-and-proteasomal-degradation
#5
JOURNAL ARTICLE
Emma C Carroll, Eric R Greene, Andreas Martin, Susan Marqusee
Changes in the cellular environment modulate protein energy landscapes to drive important biology, with consequences for signaling, allostery and other vital processes. The effects of ubiquitination are particularly important because of their potential influence on degradation by the 26S proteasome. Moreover, proteasomal engagement requires unstructured initiation regions that many known proteasome substrates lack. To assess the energetic effects of ubiquitination and how these manifest at the proteasome, we developed a generalizable strategy to produce isopeptide-linked ubiquitin within structured regions of a protein...
August 2020: Nature Chemical Biology
https://read.qxmd.com/read/32385034/-research-progress-of-the-roles-of-ubiquitination-deubiquitination-in-androgen-receptor-abnormalities-and-prostate-cancer
#6
REVIEW
Wei-Yu Zhang, Jian-Hua Zhou, Huan-Rui Wang, Qing Mu, Qi Wang, Ke-Xin Xu, Tao Xu, Hao Hu
Ubiquitin is a small molecule protein consisting of 76 amino acids,widely found in eukaryotic cells. The process by which ubiquitin binding to a specific protein is called ubiquitination. Deubiquitination is the reversed process of ubiquitination. Ubiquitination stimulates downstream signal,including complex assembly,protein conformation and activity changes,proteolysis,autophagy,guilt,chromatin remodeling,and DNA repair. More than 80% of eukaryotic protein degradation is mediated by the ubiquitination system,and ubiquitin-dependent proteolysis is an extremely complex process involving many biomolecular processes...
April 28, 2020: Zhongguo Yi Xue Ke Xue Yuan Xue Bao. Acta Academiae Medicinae Sinicae
https://read.qxmd.com/read/32188728/structure-guided-mutagenesis-alters-deubiquitinating-activity-and-attenuates-pathogenesis-of-a-murine-coronavirus
#7
JOURNAL ARTICLE
Xufang Deng, Yafang Chen, Anna M Mielech, Matthew Hackbart, Kristina R Kesely, Robert C Mettelman, Amornrat O'Brien, Mackenzie E Chapman, Andrew D Mesecar, Susan C Baker
Coronaviruses express a multifunctional papain-like protease, termed papain-like protease 2 (PLP2). PLP2 acts as a protease that cleaves the viral replicase polyprotein and as a deubiquitinating (DUB) enzyme which removes ubiquitin (Ub) moieties from ubiquitin-conjugated proteins. Previous in vitro studies implicated PLP2/DUB activity as a negative regulator of the host interferon (IFN) response, but the role of DUB activity during virus infection was unknown. Here, we used X-ray structure-guided mutagenesis and functional studies to identify amino acid substitutions within the ubiquitin-binding surface of PLP2 that reduced DUB activity without affecting polyprotein processing activity...
May 18, 2020: Journal of Virology
https://read.qxmd.com/read/32009145/effects-of-chain-length-and-geometry-on-the-activation-of-dna-damage-bypass-by-polyubiquitylated-pcna
#8
JOURNAL ARTICLE
Tomio S Takahashi, Hans-Peter Wollscheid, Jonathan Lowther, Helle D Ulrich
Ubiquitylation of the eukaryotic sliding clamp, PCNA, activates a pathway of DNA damage bypass that facilitates the replication of damaged DNA. In its monoubiquitylated form, PCNA recruits a set of damage-tolerant DNA polymerases for translesion synthesis. Alternatively, modification by K63-linked polyubiquitylation triggers a recombinogenic process involving template switching. Despite the identification of proteins interacting preferentially with polyubiquitylated PCNA, the molecular function of the chain and the relevance of its K63-linkage are poorly understood...
April 6, 2020: Nucleic Acids Research
https://read.qxmd.com/read/31974276/usp14-is-required-for-spermatogenesis-and-ubiquitin-stress-responses-in-drosophila-melanogaster
#9
JOURNAL ARTICLE
Levente Kovács, Ágota Nagy, Margit Pál, Peter Deák
Deubiquitylating (DUB) enzymes free covalently linked ubiquitin moieties from ubiquitin-ubiquitin and ubiquitin-protein conjugates, and thereby maintain the equilibrium between free and conjugated ubiquitin moieties and regulate ubiquitin-mediated cellular processes. Here, we performed genetic analyses of mutant phenotypes in Drosophila melanogaster and demonstrate that loss of Usp14 function results in male sterility, with defects in spermatid individualization and reduced testicular free monoubiquitin levels...
January 23, 2020: Journal of Cell Science
https://read.qxmd.com/read/31956026/a-cycle-of-ubiquitination-regulates-adaptor-function-of-the-nedd4-family-ubiquitin-ligase-rsp5
#10
JOURNAL ARTICLE
Chris MacDonald, S Brookhart Shields, Charlotte A Williams, Stanley Winistorfer, Robert C Piper
In yeast, the main ubiquitin ligase responsible for the sorting of proteins to the lysosomal vacuole is Rsp5, a member of the Nedd4 family of ligases whose distinguishing features are a catalytic homologous to E6AP C terminus (HECT) domain and 3 central WW domains that bind PY motifs in target proteins. Many substrates do not bind Rsp5 directly and instead rely on PY-containing adaptor proteins that interact with Rsp5. Recent studies indicate that the activities of these adaptors are elevated when they undergo ubiquitination, yet the mechanism whereby ubiquitination activates the adaptors and how this process is regulated remain unclear...
February 3, 2020: Current Biology: CB
https://read.qxmd.com/read/31931110/ubiquitination-and-e3-ubiquitin-ligases-in-rare-neurological-diseases-with-comorbid-epilepsy
#11
REVIEW
Jiuhe Zhu, Nien-Pei Tsai
Ubiquitination is a post-translational modification that can dynamically alter the function, degradation and transport of a protein, as well as its interaction with other proteins, and activity of an enzyme. Dysfunctional ubiquitination is detrimental to normal cellular functions, and can result in severe diseases. Over the last decade, although much research has focused on deciphering the role of the ubiquitination/ubiquitin proteasome system (UPS) in the onset and progression of various neurological disorders, the specific relationship between ubiquitination and various epilepsies has not been carefully reviewed...
January 21, 2020: Neuroscience
https://read.qxmd.com/read/31840790/dictyostelium-as-model-for-studying-ubiquitination-and-deubiquitination
#12
JOURNAL ARTICLE
Barbara Pergolizzi, Salvatore Bozzaro, Enrico Bracco
By protein quality control and degradation, the ubiquitin system drives many essential regulatory processes such as cell cycle and division, signalling, DNA replication and repair. Therefore, dysfunctions in the ubiquitin system lead to many human disease states. However, despite the immense progress made over the last couple of decades, it appears that the ubiquitin system is more complex and multi-faced than formerly expected. In addition to a rich repertoire of ubiquitin, ubiquitin conjugating and de-ubiquitylating enzymes, the social amoeba Dictyostelium discoideum genome encodes also for a wide array of ubiquitin binding domain-containing proteins, thus offering the possibility to explore the biology of the ubiquitin system from cell and molecular biology points of view...
2019: International Journal of Developmental Biology
https://read.qxmd.com/read/31705877/the-identification-of-potential-therapeutic-targets-for-cutaneous-squamous-cell-carcinoma
#13
JOURNAL ARTICLE
Angela McHugh, Kenneth Fernandes, Nerime Chinner, Adel F M Ibrahim, Amit K Garg, Garry Boag, Lydia A Hepburn, Charlotte M Proby, Irene M Leigh, Mark K Saville
We performed a small interfering RNA screen to identify targets for cutaneous squamous cell carcinoma (cSCC) therapy in the ubiquitin/ubiquitin-like system. We provide evidence for selective anti-cSCC activity of knockdown of the E3 ubiquitin ligase MARCH4, the ATPase p97/VCP, the deubiquitinating enzyme USP8, the cullin-RING ligase (CRL) 4 substrate receptor CDT2/DTL, and components of the anaphase-promoting complex/cyclosome (APC/C). Specifically attenuating CRL4CDT2 by CDT2 knockdown can be more potent in killing cSCC cells than targeting CRLs or CRL4s in general by RBX1 or DDB1 depletion...
June 2020: Journal of Investigative Dermatology
https://read.qxmd.com/read/31329620/cullin-4b-e3-ubiquitin-ligase-mediates-apaf-1-ubiquitination-to-regulate-caspase-9-activity
#14
JOURNAL ARTICLE
Eri Ohta, Masanori Itoh, Masashi Ueda, Yoko Hida, Miao-Xing Wang, Miki Hayakawa-Ogura, Shimo Li, Emika Nishida, Kazunori Ohta, Tana, Saiful Islam, Kiyomi Nakagawa, Tomomi Sunayama, Huayue Chen, So Hirata, Masashi Endo, Yoya Ohno, Toshiyuki Nakagawa
Apoptotic protease-activating factor 1 (Apaf-1) is a component of apoptosome, which regulates caspase-9 activity. In addition to apoptosis, Apaf-1 plays critical roles in the intra-S-phase checkpoint; therefore, impaired expression of Apaf-1 has been demonstrated in chemotherapy-resistant malignant melanoma and nuclear translocation of Apaf-1 has represented a favorable prognosis of patients with non-small cell lung cancer. In contrast, increased levels of Apaf-1 protein are observed in the brain in Huntington's disease...
2019: PloS One
https://read.qxmd.com/read/31271238/defective-ribosomal-products-challenge-nuclear-function-by-impairing-nuclear-condensate-dynamics-and-immobilizing-ubiquitin
#15
JOURNAL ARTICLE
Laura Mediani, Jordina Guillén-Boixet, Jonathan Vinet, Titus M Franzmann, Ilaria Bigi, Daniel Mateju, Arianna D Carrà, Federica F Morelli, Tatiana Tiago, Ina Poser, Simon Alberti, Serena Carra
Nuclear protein aggregation has been linked to genome instability and disease. The main source of aggregation-prone proteins in cells is defective ribosomal products (DRiPs), which are generated by translating ribosomes in the cytoplasm. Here, we report that DRiPs rapidly diffuse into the nucleus and accumulate in nucleoli and PML bodies, two membraneless organelles formed by liquid-liquid phase separation. We show that nucleoli and PML bodies act as dynamic overflow compartments that recruit protein quality control factors and store DRiPs for later clearance...
August 1, 2019: EMBO Journal
https://read.qxmd.com/read/31097444/unanchored-ubiquitin-chains-do-not-lead-to-marked-alterations-in-gene-expression-in-drosophila-melanogaster
#16
JOURNAL ARTICLE
Jessica R Blount, Danielle N Meyer, Camille Akemann, Sean L Johnson, Katherine Gurdziel, Tracie R Baker, Sokol V Todi
The small protein modifier, ubiquitin regulates various aspects of cellular biology through its chemical conjugation onto proteins. Ubiquitination of proteins presents itself in numerous iterations, from a single mono-ubiquitination event to chains of poly-ubiquitin. Ubiquitin chains can be attached onto other proteins or can exist as unanchored species - i.e. free from another protein. Unanchored ubiquitin chains are thought to be deleterious to the cell and rapidly disassembled into mono-ubiquitin. We recently examined the toxicity and utilization of unanchored poly-ubiquitin in Drosophila melanogaster We found that free poly-ubiquitin species are largely innocuous to flies and that free poly-ubiquitin can be controlled by being degraded by the proteasome or by being conjugated onto another protein as a single unit...
May 16, 2019: Biology Open
https://read.qxmd.com/read/30850048/methods-to-measure-ubiquitin-chain-length-and-linkage
#17
JOURNAL ARTICLE
Fumiaki Ohtake, Hikaru Tsuchiya, Keiji Tanaka, Yasushi Saeki
To understand the biological roles of different ubiquitin chains, it is important to determine the types of ubiquitin linkages, the lengths of the polymers, and the combinations of ubiquitin chains attached to substrates. In this chapter, we describe a mass spectrometry-based quantification method of ubiquitin chains, named Ub-AQUA/PRM (ubiquitin-absolute quantification/parallel reaction monitoring), for direct and highly sensitive measurement of the stoichiometry of all eight ubiquitin-ubiquitin linkage types simultaneously...
2019: Methods in Enzymology
https://read.qxmd.com/read/30783160/elevated-ubiquitinated-proteins-in-brain-and-blood-of-individuals-with-schizophrenia
#18
JOURNAL ARTICLE
Chad A Bousman, Sandra Luza, Serafino G Mancuso, Dali Kang, Carlos M Opazo, Md Shaki Mostaid, Vanessa Cropley, Patrick McGorry, Cynthia Shannon Weickert, Christos Pantelis, Ashley I Bush, Ian P Everall
Dysregulation of the ubiquitin proteasome system (UPS) has been linked to schizophrenia but it is not clear if this dysregulation is detectable in both brain and blood. We examined free mono-ubiquitin, ubiquitinated proteins, catalytic ubiquitination, and proteasome activities in frozen postmortem OFC tissue from 76 (38 schizophrenia, 38 control) matched individuals, as well as erythrocytes from 181 living participants, who comprised 30 individuals with recent onset schizophrenia (mean illness duration = 1 year), 63 individuals with 'treatment-resistant' schizophrenia (mean illness duration = 17 years), and 88 age-matched participants without major psychiatric illness...
February 19, 2019: Scientific Reports
https://read.qxmd.com/read/30543854/the-stability-and-oncogenic-function-of-lin28a-are-regulated-by-usp28
#19
JOURNAL ARTICLE
Saba Haq, Soumyadip Das, Dong-Ho Kim, Arun Pandian Chandrasekaran, Seok-Ho Hong, Kye-Seong Kim, Suresh Ramakrishna
RNA-binding protein LIN28A is often highly expressed in human malignant tumors and is involved in tumor metastasis and poor prognosis. Knowledge about post-translational regulatory mechanisms governing LIN28A protein stability and function is scarce. Here, we investigated the role of ubiquitination and deubiquitination on LIN28A protein stability and report that LIN28A protein undergoes ubiquitination. Ubiquitin-specific protease 28 (USP28), a deubiquitinating enzyme, interacts with and stabilizes LIN28A protein to extend its half-life...
March 1, 2019: Biochimica et Biophysica Acta. Molecular Basis of Disease
https://read.qxmd.com/read/30456385/specificity-for-deubiquitination-of-monoubiquitinated-fancd2-is-driven-by-the-n-terminus-of-usp1
#20
JOURNAL ARTICLE
Connor Arkinson, Viduth K Chaugule, Rachel Toth, Helen Walden
The Fanconi anemia pathway for DNA interstrand crosslink repair and the translesion synthesis pathway for DNA damage tolerance both require cycles of monoubiquitination and deubiquitination. The ubiquitin-specific protease-1 (USP1), in complex with USP1-associated factor 1, regulates multiple DNA repair pathways by deubiquitinating monoubiquitinated Fanconi anemia group D2 protein (FANCD2), Fanconi anemia group I protein (FANCI), and proliferating cell nuclear antigen (PCNA). Loss of USP1 activity gives rise to chromosomal instability...
October 2018: Life Science Alliance
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