Regulation of NCX1 by palmitoylation [PDF]
Cell Calcium, 2020 Palmitoylation (S-acylation) is the reversible conjugation of a fatty acid (usually C16 palmitate) to intracellular cysteine residues of proteins via a thioester linkage. Palmitoylation anchors intracellular regions of proteins to membranes because the palmitoylated cysteine is recruited to the lipid bilayer.
Caglar Gok, William Fuller
exaly +12 more sources
Protein palmitoylation and cancer [PDF]
EMBO Reports, 2018 Protein S-palmitoylation is a reversible post-translational modification that alters the localization, stability, and function of hundreds of proteins in the cell. S-palmitoylation is essential for the function of both oncogenes (e.g., NRAS and EGFR) and tumor suppressors (e.g., SCRIB, melanocortin 1 receptor).
Scott Dixon
exaly +3 more sources
Palmitoylation landscapes across human cancers reveal a role of palmitoylation in tumorigenesis
Journal of Translational Medicine, 2023 Background Protein palmitoylation, which is catalyzed by palmitoyl-transferase and de-palmitoyl-transferase, plays a crucial role in various biological processes. However, the landscape and dynamics of protein palmitoylation in human cancers are not well
Yue Kong +8 more
doaj +3 more sources
On the mechanism of protein palmitoylation [PDF]
EMBO Reports, 2004 Protein palmitoylation or, more specifically, S-acylation is a reversible post-translational lipid modification. Despite the identification of several proteins that are altered in this way, our understanding of the enzymology of this process has been hampered by the lack of well-characterized acyltransferases.
Lars Dietrich, Christian Ungermann
exaly +3 more sources
The functional roles and therapeutic potential of protein palmitoylation in hepatocellular carcinoma [PDF]
Discover OncologyObjective Protein palmitoylation is a reversible lipid post-translational modification that influences protein stability, membrane association, and signal transduction.
Fang Wei +5 more
doaj +2 more sources
Recent advances in S-palmitoylation and its emerging roles in human diseases
Journal of Hematology and OncologyS-palmitoylation, one reversible post-translational modification (PTM) involving the binding of palmitate to proteins, influences protein stability, localization and interactions.
Xiangxiang Zhou, Juanjuan Shang
exaly +2 more sources
The Roles of Protein S-Palmitoylation in Cancers: From Dynamic Modulation to Therapeutic Potential [PDF]
Cancer CommunicationsProtein S-palmitoylation is a highly conserved posttranslational lipid modification that occurs on cysteine residues and critically influences protein maturation, subcellular localization, trafficking, and stability. Owing to its unique reversibility and
Haonan Zheng +7 more
doaj +2 more sources
The role of protein palmitoylation in disease pathogenesis and therapeutic innovation [PDF]
Annals of MedicineBackground Protein palmitoylation is a significant post-translational modification that influences protein stability, localization, and signaling through the addition of palmitoyl groups to cysteine, serine/threonine, or lysine residues.
Xinyue Lin +7 more
doaj +2 more sources
From lipid modification to cell death: the diverse roles of S-palmitoylation in cell fate decisions [PDF]
Cell Communication and SignalingS-palmitoylation is a dynamic, reversible lipid modification that plays a crucial role in the regulation of various types of cell death. However, systematic insights into how S-palmitoylation modifications integrate and mediate crosstalk among diverse ...
Yue Zhu +5 more
doaj +2 more sources
ZDHHC18‐Mediated Palmitoylation of ORF3a Promotes SARS‐CoV‐2 Pathogenesis by Antagonizing TRIM16‐Mediated Ubiquitination and Proteasomal Degradation [PDF]
Advanced ScienceSARS‐CoV‐2 accessory protein ORF3a contributes to viral pathogenesis through membrane remodeling, immune evasion, and inflammation induction. However, the molecular mechanisms underlying ORF3a‐mediated pathogenesis remain poorly characterized, and no ...
Sidi Yang +17 more
doaj +2 more sources