Review
Biochemistry & Molecular Biology
Sara Martin-Villanueva, Gabriel Gutierrez, Dieter Kressler, Jesus de la Cruz
Summary: Ubiquitin is a highly conserved small protein in eukaryotes that functions as a post-translational modifier through ubiquitination. It plays a crucial role in ribosome biogenesis and function, along with other ubiquitin-like proteins such as SUMO. The fusion of ubiquitin moieties to specific ribosomal proteins is evolutionarily significant and helps regulate cellular processes.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Review
Cell Biology
Dragana Ilic, Helge M. Magnussen, Marilyn Tirard
Summary: Stress is crucial for cellular and organismal evolution, but failure to adapt or restore homeostasis can lead to severe diseases or death. Protein post-translational modifications, especially SUMO modification, play a key role in the adaptive response to stress.
SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY
(2022)
Article
Biochemistry & Molecular Biology
Adi Ulman, Tal Levin, Bareket Dassa, Aaron Javitt, Assaf Kacen, Merav D. Shmueli, Avital Eisenberg-Lerner, Daoud Sheban, Simon Fishllevich, Emmanuel D. Levy, Yifat Merbl
Summary: Protein modification by ubiquitin or SUMO can alter protein function, stability and activity. This study identified sites in the human proteome where proteins were modified by both ubiquitin and SUMO, termed SAMs. SAM-containing proteins are associated with various biological functions, and comparison with non-overlapping modification sites revealed altered properties such as cellular localization or abundance of host proteins. Mutating the SAM motif in a protein can influence its ubiquitination, localization, and abundance, as demonstrated in S. cerevisiae.
JOURNAL OF MOLECULAR BIOLOGY
(2021)
Article
Chemistry, Medicinal
Dexiang Hua, Xiaoxing Wu
Summary: SUMOylation is a key post-translational modification process that is essential for normal cellular functions. Dysregulation of SUMOylation is associated with various diseases, and small-molecular inhibitors targeting this pathway have been discovered.
EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY
(2022)
Article
Biochemistry & Molecular Biology
Ting Ling, Siyi Li, Huan Chen, Qiuping Wang, Jing Shi, Yirong Li, Wenjun Bao, Kunming Liang, Hai-long Piao
Summary: This study reveals the discovery of a GS SUMOylation deficient mutant that exhibits reduced response under glutamine starvation. The SUMOylation impairs the protein stability and enzymatic activity of GS. SAE1, Ubc9, and PIAS1 are identified as the assembly enzymes of GS SUMOylation, while Senp1/2 functions as a SUMO-specific protease to reverse the SUMOylation of GS.
Article
Plant Sciences
M. Masoabi, N. F. V. Burger, A. -M. Botha, M. L. Le Roux, M. Vlok, S. Snyman, C. Van der Vyver
Summary: In this study, sugarcane was genetically transformed with the OTS1 gene from Arabidopsis thaliana to enhance drought tolerance. The transgenic plants showed improved drought tolerance and delayed leaf senescence, maintaining high moisture content and photosynthesis rate under water deficit. Additionally, they were able to maintain higher stomatal conductance and chlorophyll content under moderate stress and exhibited reduced oxidative damage under severe water deficit. The SUMOylation of proteins and protease activity were lower in the transgenic plants, suggesting that SUMO-related post-translational modifications played a role in enhancing drought tolerance in sugarcane.
Review
Cell Biology
Mounira K. Chelbi-Alix, Pierre Thibault
Summary: Interferon is a critical defense mechanism against viral infections, enhancing cellular antiviral capabilities by inducing ISGs. SUMO and ISG15 act as important Ubl modifiers in this process. The crosstalk between poly-SUMOylation and ISG15 further strengthens the cell's antiviral functions.
FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY
(2021)
Article
Chemistry, Multidisciplinary
Tian Wang, Chuntong Li, Meijing Wang, Jiachen Zhang, Qingyun Zheng, Lujun Liang, Guochao Chu, Xiaolin Tian, Haiteng Deng, Wei He, Lei Liu, Jinghong Li
Summary: ISG15 protein tools are crucial for studying innate immunity and antiviral responses. This study discovered that the leader protease from foot-and-mouth disease virus can facilitate ligation reactions between ISG15 and synthetic compounds, resulting in the generation of necessary ISG15 protein tools.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2022)
Article
Biochemistry & Molecular Biology
Weber Beringui Feitosa, Patricia L. Morris
Summary: Mammalian oocytes undergo morphological, structural, and molecular changes during a process called oocyte aging. The SUMO pathway, specifically SUMO-2/3 and the SUMO-specific protease SENP-2, are involved in spindle morphology changes and chromosome movements during oocyte aging. Decreased UBC9 and differential ubiquitination patterns also correlate with in vitro oocyte aging. These findings suggest that age-related changes in SUMOylation and the deSUMOylation of key target proteins may contribute to spindle and chromosome alignment defects during mammalian oocyte postovulatory aging, with implications for ART-related human oocyte aging and fertilization success.
Review
Cell Biology
Fredrik Trulsson, Alfred C. O. Vertegaal
Summary: This review discusses the biological importance of site-specific modifications by ubiquitin and SUMO in regulating the DNA damage response, protein quality control, and cell cycle progression. The review also explores the machinery responsible for these modifications and methods to identify ubiquitin and SUMO modified sites. The authors emphasize the need for further innovation in the field to address challenges and long-standing questions.
SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY
(2022)
Article
Surgery
Yuxiang Lin, Qingshui Wang, Yingying Lin, Meichen Jiang, Han Xiao, Jie Zhang, Rongrong Guo, Shaohong Kang, Yao Lin, Chuangui Song
Summary: Elevated levels of SUMO1/2/3 were associated with poorer survival outcomes for TNBC patients. A classifier was developed based on this association to predict chemotherapy response, and a nomogram was created to identify patients who may benefit from chemotherapy. The study also suggested that the activation of the SUMOylation pathway in TNBC might be induced by MYC signaling.
Review
Biochemistry & Molecular Biology
Jin-Taek Hwang, Ahyoung Lee, Changwon Kho
Summary: Post-translational modification (PTM) is an essential mechanism for enhancing the functional diversity of proteins and adjusting their signaling networks. The reversible conjugation of ubiquitin (Ub) and ubiquitin-like proteins (Ubls) to cellular proteins is among the most prevalent PTM, which modulates various cellular and physiological processes by altering the activity, stability, localization, trafficking, or interaction networks of its target molecules. The dysregulation of Ub/Ubl modifications is associated with various diseases, providing new targets for drug development.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2022)
Review
Biochemistry & Molecular Biology
Hengsen Zhang, Bin Chen, A. S. M. Waliullah, Shuhei Aramaki, Yashuang Ping, Yusuke Takanashi, Chi Zhang, Qing Zhai, Jing Yan, Soho Oyama, Tomoaki Kahyo, Mitsutoshi Setou
Summary: Ubiquitin-like proteins (Ubls) play a role in protein modification and are associated with various diseases, particularly cancer. Ubiquitin-like protein 3 (UBL3) has been identified as a key factor in small extracellular vesicle protein sorting and ubiquitination. Studies have shown that UBL3 expression affects cancer cell growth and prognosis. This review provides an overview of the relationship between Ubls and cancer, with a focus on UBL3 and its potential as a therapeutic target.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2023)
Article
Biology
Heesun Kim, Yue-He Ding, Shan Lu, Mei-Qing Zuo, Wendy Tan, Darryl Conte, Meng-Qiu Dong, Craig C. Mello
Summary: Germlines play a crucial role in maintaining germline fate and surveillance in adult germlines. Research has found that PIE-1 plays a key role in integrating and regulating genetic information, engaging in SUMO pathway and capturing HDAC SUMOylation.
Article
Biochemical Research Methods
Julius T. Dongdem, Simon P. Dawson, Robert Layfield
Summary: The study revealed a previously unappreciated complexity in ubiquitin modification, involving SUMO2 modification and phosphorylation of unanchored polyubiquitin chains.