Review
Plant Sciences
Ying Chen, Dirk Inze, Hannes Vanhaeren
Summary: Plants play a crucial role as a primary food source and potential renewable energy resource. The final size of plant organs is determined by the coordination between cell proliferation and expansion, with the protease DA1 playing a key role in regulating cell proliferation duration and final organ size. The complex molecular mechanisms involving DA1 and its interacting proteins provide insights into fine-tuning organ size and hold potential for identifying substrate cleavage events in a biological context.
JOURNAL OF EXPERIMENTAL BOTANY
(2021)
Article
Cell Biology
Sangkyeong Eom, Jongjin Peak, Jongyeun Park, Seung Hyun Ahn, You Kyung Cho, Yeahji Jeong, Hye-Sook Lee, Jung Lee, Elizaveta Ignatova, Sung Eun Lee, Yunji Hong, Dowoon Gu, Geun-Woo D. Kim, Dong Chan Lee, Ja Young Hahm, Jaemin Jeong, Dongho Choi, Eun-Sook Jang, Sung Wook Chi
Summary: Oxidative stress contributes to tumourigenesis by altering gene expression. One modification, 8-oxoguanine, can change RNA-RNA interactions, but its regulatory roles are not well understood. Sequencing analysis revealed widespread position-specific 8-oxoguanine in tumour microRNAs, which are associated with lower-grade gliomas and liver hepatocellular carcinoma. Specific 8-oxoguanine modifications were found to suppress or promote the malignancy of cancer, suggesting its potential importance in cancer treatment.
NATURE CELL BIOLOGY
(2023)
Review
Biochemistry & Molecular Biology
Eugene Varfolomeev, Domagoj Vucic
Summary: Receptor interacting protein 1 (RIP1) kinase is a critical regulator of inflammation and cell death signaling, and its post-translational modifications, such as ubiquitination, phosphorylation, and cleavage, greatly impact its function in signaling pathways.
BIOCHEMICAL JOURNAL
(2022)
Review
Multidisciplinary Sciences
Ji Min Lee, Henrik M. Hammaren, Mikhail M. Savitski, Sung Hee Baek
Summary: Post-translational modifications (PTMs) on specific amino acids control the stability of target proteins. These PTM-regulated degrons act as signals for protein degradation or stabilization. This review summarizes the current knowledge of PTM-mediated protein stability regulation to enhance the identification of novel drug targets.
NATURE COMMUNICATIONS
(2023)
Article
Biochemistry & Molecular Biology
Kuo-Feng Hsu, Sarah E. Wilkins, Richard J. Hopkinson, Rok Sekirnik, Emily Flashman, Akane Kawamura, James S. O. McCullagh, Louise J. Walport, Christopher J. Schofield
Summary: Hypoxia affects histone modifications, but synthetic hypoxia mimetics may not accurately replicate these effects. Liquid chromatography-mass spectrometry is a simple and robust method for investigating potential drug effects on histone modifications. The findings suggest caution should be used in interpreting data from chemically-induced hypoxia.
Article
Pharmacology & Pharmacy
Juan Facundo Chrestia, Ornella Turani, Noelia Rodriguez Araujo, Guillermina Hernando, Maria del Carmen Esandi, Cecilia Bouzat
Summary: Nicotinic acetylcholine receptors (nAChRs) are widely distributed in the central and peripheral nervous system and play crucial roles in vital physiological processes. Post-translational modifications (PTMs) have been shown to regulate different aspects of nAChR life cycle, but our knowledge in this field is still limited and many important aspects remain unknown.
PHARMACOLOGICAL RESEARCH
(2023)
Article
Neurosciences
Shujing Zhang, Ruowei Zhu, Buyan Pan, Hong Xu, Modupe F. Olufemi, Ronald J. Gathagan, Yuanxi Li, Luyan Zhang, Jasmine Zhang, Wenxuan Xiang, Eliot Masahiro Kagan, Xingjun Cao, Chaoxing Yuan, Soo-Jung Kim, Christopher K. Williams, Shino Magaki, Harry V. Vinters, Hilal A. Lashuel, Benjamin A. Garcia, E. James Petersson, John Q. Trojanowski, Virginia M. -Y. Lee, Chao Peng
Summary: Pathological alpha-synuclein spreading is critical for the progression of neurodegenerative diseases. The authors demonstrate that soluble alpha-synuclein post-translational modifications (PTMs) influence the amplification and transmission of pathological alpha-synuclein. Phosphorylation and acetylation of soluble alpha-synuclein affect the conformation and seeding properties of pathological alpha-synuclein. This study provides a systematic analysis on how soluble alpha-synuclein PTMs affect disease progression.
NATURE NEUROSCIENCE
(2023)
Article
Multidisciplinary Sciences
Luca Perico, Marina Morigi, Anna Pezzotta, Daniela Corna, Valerio Brizi, Sara Conti, Cristina Zanchi, Fabio Sangalli, Piera Trionfini, Sara Butto, Christodoulos Xinaris, Susanna Tomasoni, Carlamaria Zoja, Giuseppe Remuzzi, Ariela Benigni, Barbara Imberti
Summary: The study reveals a novel role for the NAD(+)-dependent deacylase SIRT3 in kidney development, controlling early renal development through the regulation of epigenetics and metabolic processes. Deficiency of SIRT3 leads to decreased nephron progenitors, impaired nephrogenesis, and a reduced number of nephrons in the developing kidney.
SCIENTIFIC REPORTS
(2021)
Article
Medicine, Research & Experimental
Qiong Wang, Danping Fan, Ya Xia, Qinbin Ye, Xiaoyu Xi, Guoqiang Zhang, Cheng Xiao
Summary: The review discusses the structure, functions, and importance of RIPK1 in disease pathogenesis, highlighting the impact of activation conditions and post-translational modifications on its functions.
BIOMEDICINE & PHARMACOTHERAPY
(2021)
Review
Physiology
Kelsey S. Kalous, Sarah L. Wynia-Smith, Brian C. Smith
Summary: Increased sirtuin deacylase activity is associated with longer lifespan and lower susceptibility to aging-related diseases in eukaryotes, while decreased activity is linked to higher disease risk. Oxidative post-translational modifications such as cysteine nitrosation and glutathionylation can inhibit sirtuin deacylase activity, potentially providing a mechanistic link between cellular oxidants and age-related disease development.
FRONTIERS IN PHYSIOLOGY
(2021)
Article
Chemistry, Multidisciplinary
Julia Kraxner, Charlotta Lorenz, Julia Menzel, Iwan Parfentev, Ivan Silbern, Manuela Denz, Henning Urlaub, Blanche Schwappach, Sarah Koester
Summary: The mechanical properties of biological cells are influenced by the cytoskeleton, with phosphorylation serving as a fast mechanism for mechanical modulation. Phosphorylation can soften filaments, and the binding of 14-3-3 protein to phosphorylated filaments further enhances this effect, potentially preserving the softening and altering cell mechanics in the cell.
Article
Biochemistry & Molecular Biology
Elise Loppinet, Harrison A. Besser, Agnele Sylvia Sewa, Fu-Chen Yang, Bana Jabri, Chaitan Khosla
Summary: Celiac disease is caused by gluten-derived antigens triggering inflammation through presenting to CD4+ T cells. In this study, we propose a mechanism for the deamidation and concentration of gluten peptides in the lysosomes of antigen-presenting cells, which explains the high concentration of gluten peptides required for an inflammatory response in CeD patients. We found that a ternary complex formed between a gluten peptide, transglutaminase-2 (TG2), and a2-macroglobulin, which was endocytosed by LRP-1. The covalent TG2-peptide adduct underwent endolysosomal decoupling, resulting in the expected deamidated epitope. Our findings suggest a pathogenic role for dendritic cells and/or macrophages in CeD and implicate TG2 in the lysosomal clearance of unwanted proteins.
CELL CHEMICAL BIOLOGY
(2023)
Article
Cell Biology
Mohd Shariq, Neha Quadir, Javaid Ahmad Sheikh, Alok Kumar Singh, William R. Bishai, Nasreen Z. Ehtesham, Seyed E. Hasnain
Summary: The host utilizes ubiquitin pathway to combat intracellular pathogens, while pathogens like Mycobacterium tuberculosis exploit this pathway to dampen host innate immune response.
Review
Cell Biology
Li Chen, Anna Kashina
Summary: Post-translational modifications (PTM) involve enzyme-mediated covalent addition of functional groups to proteins during or after synthesis, greatly increasing biological complexity and playing a crucial role in biological regulation.
FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY
(2021)
Article
Biochemistry & Molecular Biology
Leonard A. Daly, Philip J. Brownridge, Michael Batie, Sonia Rocha, Violaine See, Claire E. Eyers
Summary: Cellular adaptation to low-oxygen environments is partially mediated by hypoxia-inducible factors (HIFs), whose stability and activity are regulated by post-translational modifications (PTMs) and protein-protein interactions. Hypoxia alters the complexity and composition of HIF alpha protein interaction networks, particularly for HIF-2 alpha, with the networks enriched for mitochondrial proteins. Additionally, both HIF alpha isoforms undergo heavy covalent modifications, with a majority of newly identified PTMs exhibiting oxygen dependency.