Protein Modification and Mistranslation in Cells and Human Disease

A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Cell Nuclei: Function, Transport and Receptors".

Deadline for manuscript submissions: closed (30 April 2024) | Viewed by 4919

Special Issue Editors


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Guest Editor
Departments of Biochemistry and Chemistry, Schulich School of Medicine & Dentistry, Faculty of Science, Western University, London, ON, Canada
Interests: aminoacyl-tRNA synthetases; biochemistry; cancer; cell biology; chemical biology; genetic code expansion; mistranslation; molecular biology; neurodegeneration; protein synthesis; RNA biology; translation fidelity; transfer RNA (tRNA); synthetic biology

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Guest Editor
Department of Biochemistry, Schulich School of Medicine & Dentistry, Western University, London, ON, Canada
Interests: RNA editing; molecular biology; protein biochemistry; RNA binding proteins; transcriptomics; RNA decay; synthetic biology
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Special Issue Information

Dear Colleagues,

The central dogma of molecular biology outlines the information flow from the nucleic acid sequences of genes in the genome to messenger RNAs (mRNAs) in the transcriptome and ultimately to the defined sequences of amino acids, which are the building blocks of all proteins in every living cell. Mutations in protein-coding genes can cause the production of proteins that differ from the wild-type sequences and that, in some cases, lead to defects in cells or cause disease. Two additional major routes generate changes in the protein sequence, even in the absence of mutations in the gene itself. One route involves the post-translational modification of proteins with a wide array of non-canonical amino acids, including acetylated, phosphorylated, or methylated amino acids that can have a dramatic impact on protein function. Indeed, there are many examples of hyper- or hypo-modified proteins associated with diverse human diseases. Another route to alter protein sequences involves mutations in transfer RNAs (tRNAs) or aminoacyl-tRNA synthetases that cause mistakes in protein synthesis or mistranslation of the genetic code. Mistranslation leads to the incorporation of the wrong amino acid at a codon or set of codons throughout the entire proteome. This Special Issue of Cells focuses on how protein modification and mistranslation alter the nature of proteins produced from otherwise wild-type genes. For this Special Issue, we welcome the submission of original research articles and reviews that highlight the impact of protein modification and errors in protein synthesis on normal cellular behaviour, protein homeostasis, and human disease.

Dr. Patrick O'Donoghue
Dr. Ilka Heinemann
Guest Editors

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Keywords

  • acetylation
  • aminoacyl-tRNA syntheses
  • genetic code expansion
  • methylation
  • missense suppression
  • mistranslation
  • nonsense suppression
  • phosphorylation
  • posttranslational modification
  • protein synthesis
  • transfer RNA (tRNA)
  • translation fidelity

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Published Papers (1 paper)

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Review

27 pages, 6866 KiB  
Review
Diverse Roles of Protein Palmitoylation in Cancer Progression, Immunity, Stemness, and Beyond
by Mingli Li, Leisi Zhang and Chun-Wei Chen
Cells 2023, 12(18), 2209; https://doi.org/10.3390/cells12182209 - 5 Sep 2023
Cited by 6 | Viewed by 4493
Abstract
Protein S-palmitoylation, a type of post-translational modification, refers to the reversible process of attachment of a fatty acyl chain—a 16-carbon palmitate acid—to the specific cysteine residues on target proteins. By adding the lipid chain to proteins, it increases the hydrophobicity of proteins and [...] Read more.
Protein S-palmitoylation, a type of post-translational modification, refers to the reversible process of attachment of a fatty acyl chain—a 16-carbon palmitate acid—to the specific cysteine residues on target proteins. By adding the lipid chain to proteins, it increases the hydrophobicity of proteins and modulates protein stability, interaction with effector proteins, subcellular localization, and membrane trafficking. Palmitoylation is catalyzed by a group of zinc finger DHHC-containing proteins (ZDHHCs), whereas depalmitoylation is catalyzed by a family of acyl-protein thioesterases. Increasing numbers of oncoproteins and tumor suppressors have been identified to be palmitoylated, and palmitoylation is essential for their functions. Understanding how palmitoylation influences the function of individual proteins, the physiological roles of palmitoylation, and how dysregulated palmitoylation leads to pathological consequences are important drivers of current research in this research field. Further, due to the critical roles in modifying functions of oncoproteins and tumor suppressors, targeting palmitoylation has been used as a candidate therapeutic strategy for cancer treatment. Here, based on recent literatures, we discuss the progress of investigating roles of palmitoylation in regulating cancer progression, immune responses against cancer, and cancer stem cell properties. Full article
(This article belongs to the Special Issue Protein Modification and Mistranslation in Cells and Human Disease)
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