Review
Immunology
Yuqi Zhang, Ziran Qin, Wenhuan Sun, Feng Chu, Fangfang Zhou
Summary: Protein S-palmitoylation is a crucial lipid modification that regulates protein function in various biological processes. Recent studies have shown that palmitoylation plays significant roles in immune function by targeting immune-related proteins to the cellular membrane and lipid rafts. Aberrant protein acylation and changes in palmitoylation levels are linked to human immunologic diseases, making targeting palmitoylation a novel therapeutic approach for treating such disorders.
FRONTIERS IN IMMUNOLOGY
(2021)
Review
Immunology
Charneal L. Dixon, Katrina Mekhail, Gregory D. Fairn
Summary: Phagocytosis is a process used by cells to engulf particles, with proteins modified by lipids to regulate signal transduction and immune functions. S-acylation, specifically S-palmitoylation, is a reversible modification that plays a role in regulating phagocytosis and phagosome biology in macrophages.
FRONTIERS IN IMMUNOLOGY
(2021)
Review
Biochemical Research Methods
Yang Wang, Wei Yang
Summary: Protein S-acylation, also known as palmitoylation, is a crucial reversible lipid modification that regulates protein functions. Recent advances in proteomic analysis of S-acylation have significantly improved our understanding of its biological processes. This research field is expected to play a key role in discovering new disease mechanisms and therapeutic targets.
JOURNAL OF PROTEOME RESEARCH
(2021)
Article
Biochemistry & Molecular Biology
Jozsef Gal, Vimala Bondada, Charles B. Mashburn, David W. Rodgers, Dorothy E. Croall, James W. Geddes
Summary: CAPN5 is a calcium-activated neutral thiol protease that is partly membrane associated. S-acylation of CAPN5 is critical for its membrane localization and enzymatic activity.
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS
(2022)
Article
Biochemical Research Methods
Wouter W. Kallemeijn, Thomas Lanyon-Hogg, Nattawadee Panyain, Andrea Goya Grocin, Paulina Ciepla, Julia Morales-Sanfrutos, Edward W. Tate
Summary: Protein lipidation is a widespread post-translational modification in nature that regulates protein function, structure, and subcellular localization. Lipid transferases and their substrate proteins are of interest as drug targets due to their dysregulation in disease. The hydrophobic and dynamic nature of lipid modifications poses challenges for detection, but chemical proteomics offers a powerful approach to identify and quantify them.
Article
Cell Biology
Savannah J. West, Goutham Kodakandla, Qioachu Wang, Ritika Tewari, Michael X. Zhu, Darren Boehning, Askar M. Akimzhanov
Summary: The study highlights the importance of S-acylation of Orai1 in mediating calcium entry and recruitment to STIM1. Rapid and transient S-acylation of Orai1 at cysteine 143 upon ER Ca2+ store depletion is essential for recruitment to ER-PM junctions and subsequent channel activation.
JOURNAL OF CELL SCIENCE
(2022)
Review
Biochemistry & Molecular Biology
Sandra Nitsch, Lara Zorro Shahidian, Robert Schneider
Summary: Post-translational modifications of histone proteins can alter chromatin architecture and gene expression. Cellular metabolites can affect histone acylations, linking cell metabolism with chromatin structure and cellular adaptation. However, technical challenges currently hinder a full understanding of the impact of these modifications on chromatin dynamics.
Article
Biochemistry & Molecular Biology
Eric Soupene, Frans A. Kuypers
Summary: The transfer of acyl chains to proteins and lipids is achieved by ACBD6 and NMT enzymes, which play an essential role in protecting acyl donor from competitive inhibition. The absence of ACBD6/NMT complex leads to increased sensitivity to inhibitors and reduced myristoylation. ACBD6 also interacts with LPLAT enzymes, contributing to lipid acylation processes.
Review
Biochemistry & Molecular Biology
Keith T. Woodley, Mark O. Collins
Summary: Protein palmitoylation is important in cellular processes, with the palmitoyltransferase ZDHHC5 being a unique member of the PAT family that plays a vital role in different cell types. Recent research has revealed several mechanisms to control the activity, localization, and function of ZDHHC5.
Article
Biochemistry & Molecular Biology
Jarrett R. Remsberg, Radu M. Suciu, Noemi A. Zambetti, Thomas W. Hanigan, Ari J. Firestone, Anagha Inguva, Amanda Long, Nhi Ngo, Kenneth M. Lum, Cassandra L. Henry, Stewart K. Richardson, Marina Predovic, Ben Huang, Melissa M. Dix, Amy R. Howell, Micah J. Niphakis, Kevin Shannon, Benjamin F. Cravatt
Summary: The covalent inhibitor ABD957 selectively impairs N-Ras depalmitoylation in AML cells, showing potential as a targeted therapy for NRAS-mutant cancers. It acts on dynamically palmitoylated proteins at the plasma membrane, causing partial effects on N-Ras palmitoylation with greater proteome selectivity compared to Palmostatin M. Additionally, ABD957 inhibits N-Ras signaling and AML cell growth, synergizing with MEK inhibition.
NATURE CHEMICAL BIOLOGY
(2021)
Article
Biochemistry & Molecular Biology
Ritika Tewari, Bieerkehazhi Shayahati, Ying Fan, Askar M. Akimzhanov
Summary: The study identified previously uncharacterized lipidation of ZAP-70, which is crucial for its interaction with protein substrates in the TCR signaling pathway. While this posttranslational modification does not affect its enzymatic activity, it plays a critical role in T cell activation and function. The findings suggest that TCR-induced S-acylation of ZAP-70 serves as a vital regulator of T cell-mediated immunity.
JOURNAL OF BIOLOGICAL CHEMISTRY
(2021)
Review
Cell Biology
Muhammad U. Anwar, F. Gisou van der Goot
Summary: S-acylation is an important posttranslational modification that regulates cellular processes. This reversible lipid modification affects cellular pathways and physiological processes, and the enzymes and proteins involved in S-acylation are still being discovered and studied.
JOURNAL OF CELL BIOLOGY
(2023)
Article
Biochemistry & Molecular Biology
Francisco S. Mesquita, Laurence Abrami, Arthur Samurkas, F. Gisou van Der Goot
Summary: S-acylation is a covalent modification of proteins with fatty acids, allowing dynamic control of protein properties and functions in association with cell membranes. It regulates a substantial portion of the human proteome and has increasingly recognized roles in protein lifespan. Recent advancements have provided new insights into its mechanisms and implications. This review focuses on the importance of S-acylation in the homeostasis, function, and coordination of integral membrane proteins.
Review
Plant Sciences
Jincheng Li, Manqi Zhang, Lijuan Zhou
Summary: Protein S-acylation, also known as palmitoylation, is a vital lipid post-translational modification in eukaryotes, playing critical roles in plant development and responses to various stresses. The dynamic and reversible nature of S-acylation allows membrane-associated proteins to undergo cycling and trafficking, acting as a switch in signaling transductions. While numerous S-acylated proteins have been identified in plants, the understanding of the regulatory mechanisms controlling this process remains incomplete.
FRONTIERS IN PLANT SCIENCE
(2022)
Review
Physiology
Savannah J. West, Darren Boehning, Askar M. Akimzhanov
Summary: S-acylation is a reversible lipidation process that plays a crucial role in regulating T cell function by controlling protein localization, stability, and interactions.
FRONTIERS IN PHYSIOLOGY
(2022)
Review
Plant Sciences
Charlotte H. Hurst, Piers A. Hemsley
JOURNAL OF EXPERIMENTAL BOTANY
(2015)
Article
Multidisciplinary Sciences
Manoj Kumar, Raymond Wightman, Ivan Atanassov, Anjali Gupta, Charlotte H. Hurst, Piers A. Hemsley, Simon Turner
Review
Plant Sciences
Piers A. Hemsley
JOURNAL OF EXPERIMENTAL BOTANY
(2017)
Article
Plant Sciences
Graham H. Cowan, Alison G. Roberts, Susan Jones, Pankaj Kumar, Pruthvi B. Kalyandurg, Jose F. Gil, Eugene I. Savenkov, Piers A. Hemsley, Lesley Torrance
Article
Plant Sciences
Charlotte H. Hurst, Dionne Turnbull, Sally M. Myles, Kerry Leslie, Nana F. Keinath, Piers A. Hemsley
Review
Plant Sciences
Piers A. Hemsley
Article
Plant Sciences
Dionne Turnbull, Haixia Wang, Susan Breen, Marek Malec, Shaista Naqvi, Lina Yang, Lydia Welsh, Piers Hemsley, Tian Zhendong, Frederic Brunner, Eleanor M. Gilroy, Paul R. J. Birch
Article
Multidisciplinary Sciences
Charlotte H. Hurst, Kathryn M. Wright, Dionne Turnbull, Kerry Leslie, Susan Jones, Piers A. Hemsley
SCIENTIFIC REPORTS
(2019)
Review
Biochemistry & Molecular Biology
Piers A. Hemsley
BIOCHEMICAL SOCIETY TRANSACTIONS
(2020)
Article
Biology
Anna Veprik, Geoffrey Denwood, Dong Liu, Rula Bany Bakar, Valentin Morfin, Kara McHugh, Nchimunya N. Tebeka, Laurene Vetterli, Ekaterina Yonova-Doing, Fiona Gribble, Frank Reimann, Kyle L. Hoehn, Piers A. Hemsley, Jonas Ahnfelt-Ronne, Patrik Rorsman, Quan Zhang, Heidi de Wet, James Cantley
Summary: Acetyl-CoA-carboxylase 1 (ACC1) is involved in the regulation of glucagon secretion and the S-acylation of glucose-sensing proteins. Loss of ACC1 in alpha-cells impairs glucagon secretion and function, and also affects pancreatic and gastrointestinal endocrine cells.
COMMUNICATIONS BIOLOGY
(2022)
Article
Biochemistry & Molecular Biology
Charlotte H. Hurst, Dionne Turnbull, Kaltra Xhelilaj, Sally Myles, Robin L. Pflughaupt, Michaela Kopischke, Paul Davies, Susan Jones, Silke Robatzek, Cyril Zipfel, Julien Gronnier, Piers A. Hemsley
Summary: Plant receptor kinases play a crucial role in transducing extracellular stimuli and are regulated by post-translational modifications. This study demonstrates the essential role of S-acylation in plant receptor kinases FLS24 and EFR for their function in immune signaling and resistance to bacterial infection. S-acylation stabilizes and promotes retention of activated receptor kinase complexes at the plasma membrane to increase signaling efficiency.
Article
Biochemical Research Methods
Sophia S. S. Puliasis, Dominika Lewandowska, Piers A. A. Hemsley, Runxuan Zhang
Summary: Many tools have been developed to generate in silico proteome digests for selecting optimal digest schemes. However, there is a need for a tool that evaluates digest schemes beyond protein and amino acid coverages. ProtView is a versatile workflow that maps digested peptides to protein and genome references, allowing the identification of observable portions of the proteome. It can examine various regulations in silico and estimate performances among digest schemes accurately.
JOURNAL OF PROTEOME RESEARCH
(2023)
Article
Biochemistry & Molecular Biology
Haixia Wang, Shumei Wang, Wei Wang, Lin Xu, Lydia R. J. Welsh, Marek Gierlinski, Stephen C. Whisson, Piers A. Hemsley, Petra C. Boevink, Paul R. J. Birch
Summary: Cytoplasmic RXLR effectors from Phytophthora infestans enter plant host cells via clathrin-mediated endocytosis. Transient silencing of clathrin heavy chain or the endosome marker gene attenuated P. infestans infection and reduced translocation of RXLR effectors into host cells. Co-localization of RXLR effectors with clathrin-coated vesicles and immunoprecipitation experiments confirmed the uptake of RXLR effectors via clathrin-mediated endocytosis.
Review
Plant Sciences
Dionne Turnbull, Piers A. Hemsley
CURRENT OPINION IN PLANT BIOLOGY
(2017)
Article
Biochemical Research Methods
Charlotte H. Hurst, Dionne Turnbull, Fiona Plain, William Fuller, Piers A. Hemsley