Significance: High-mobility group protein 1 (HMGB1) is an evolutionarily conserved and multifunctional protein. The biological function of HMGB1 depends on its cellular locations, binding partners, and redox states. Extracellular HMGB1 is a mediator of inflammation during infection or tissue injury. Immune cells actively release HMGB1 in response to infection, which in turn orchestrates both innate and adaptive immune responses.
Recent Advances: Hyperacetylation of HMGB1 within its nuclear localization sequences mobilizes HMGB1 from the nucleus to the cytoplasm and subsequently promotes HMGB1 release. The redox states of the cysteines in positions 23, 45, and 106 determine the biological activity of the extracellular HMGB1.
Critical Issues: The full picture and the detailed molecular mechanisms of how cells regulate the posttranslational modifications and the redox status of HMGB1 during immune responses or under stress not only unravel the molecular mechanisms by which cells regulate the release and the biological function of HMGB1 but may also provide novel therapeutic targets to treat inflammatory diseases.
Future Directions: It is important to identify the signaling pathways that regulate the posttranslational modifications and the redox status of HMGB1 and find their roles in host immune responses and pathogenesis of diseases.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5349223 | PMC |
| http://dx.doi.org/10.1089/ars.2015.6409 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Protein prenylation in mechanotransduction: implications for disease and therapy.
Trends Pharmacol Sci
January 2025
Department of Cardiology, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310003, China. Electronic address:
The process by which cells translate external mechanical cues into intracellular biochemical signals involves intricate mechanisms that remain unclear. In recent years, research into post-translational modifications (PTMs) has offered valuable insights into this field, spotlighting protein prenylation as a crucial mechanism in cellular mechanotransduction and various human diseases. Protein prenylation, which involves the covalent attachment of isoprenoid groups to specific substrate proteins, profoundly affects the functions of key mechanotransduction proteins such as Rho, Ras, and lamins.
View Article and Find Full Text PDFCharacterization by LC-MS/MS analysis of KLH vaccine conjugated with a tick antigen peptide.
Analyst
January 2025
Department of Proteomics, Mass Spectrometry Laboratory, Center for Genetic Engineering and Biotechnology, 31 Avenue, Cubanacan, Playa, Havana, Cuba.
Keyhole limpet haemocyanins (KLH1 and KLH2) from , are multi-subunit oxygen-carrying metalloproteins of approximately 3900 amino acids, that are widely used as carrier proteins in conjugate vaccines and in immunotherapy. KLHs and their derived conjugate vaccines are poorly characterized by LC-MS/MS due to their very stable supramolecular structures with megadalton molecular mass, and their resistance to efficient digestion with standard protocols. KLH1 and KLH2 proteins were conjugated to the conserved P0 peptide (pP0), derived from the P0 acidic ribosomal protein of sp.
View Article and Find Full Text PDFDistinct structural and functional heterochromatin partitioning of lamin B1 and lamin B2 revealed using genome-wide nicking enzyme epitope targeted DNA sequencing.
Nucleic Acids Res
January 2025
Molecular Genetics and Genomics, New England Biolabs, Inc, 240 County Road, Ipswich, MA 01938, USA.
Gene expression is regulated by chromatin DNA methylation and other features, including histone post-translational modifications (PTMs), chromatin remodelers and transcription factor occupancy. A complete understanding of gene regulation will require the mapping of these chromatin features in small cell number samples. Here we describe a novel genome-wide chromatin profiling technology, named as Nicking Enzyme Epitope targeted DNA sequencing (NEED-seq).
View Article and Find Full Text PDFManipulation of mitochondrial poly(A) polymerase family proteins in impacts mRNA termini processing.
Front Parasitol
January 2024
Department of Biomedical Sciences, University of Minnesota Medical School, Duluth, MN, United States.
RNA-specific nucleotidyltransferases (rNTrs) add nontemplated nucleotides to the 3 end of RNA. Two noncanonical rNTRs that are thought to be poly(A) polymerases (PAPs) have been identified in the mitochondria of trypanosomes - KPAP1 and KPAP2. KPAP1 is the primary polymerase that adds adenines (As) to trypanosome mitochondrial mRNA 3 tails, while KPAP2 is a non-essential putative polymerase whose role in the mitochondria is ambiguous.
View Article and Find Full Text PDFIlluminating the impact of N-terminal acetylation: from protein to physiology.
Nat Commun
January 2025
Department of Biomedicine, University of Bergen, Bergen, Norway.
N-terminal acetylation is a highly abundant protein modification in eukaryotic cells. This modification is catalysed by N-terminal acetyltransferases acting co- or post-translationally. Here, we review the eukaryotic N-terminal acetylation machinery: the enzymes involved and their substrate specificities.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!