scholarly journals Dynamic Protein S-Acylation in Plants

2019 ◽  
Vol 20 (3) ◽  
pp. 560 ◽  
Author(s):  
Lihua Zheng ◽  
Peng Liu ◽  
Qianwen Liu ◽  
Tao Wang ◽  
Jiangli Dong
Keyword(s):  
Protein S ◽  
Acyl Transferase ◽  
Lipid Modification ◽  
Post Translational Modification ◽  
Lipid Modifications ◽  
Acylated Proteins

Lipid modification is an important post-translational modification. S-acylation is unique among lipid modifications, as it is reversible and has thus attracted much attention. We summarize some proteins that have been shown experimentally to be S-acylated in plants. Two of these S-acylated proteins have been matched to the S-acyl transferase. More importantly, the first protein thioesterase with de-S-acylation activity has been identified in plants. This review shows that S-acylation is important for a variety of different functions in plants and that there are many unexplored aspects of S-acylation in plants.

scholarly journals The gene encoding vitamin K-dependent anticoagulant protein C is expressed in human male reproductive tissues.

1995 ◽  
Vol 43 (6) ◽  
pp. 563-570 ◽  
Author(s):  
X He ◽  
L Shen ◽  
A Bjartell ◽  
J Malm ◽  
H Lilja ◽  
...  
Keyword(s):  
Vitamin K ◽  
Leydig Cells ◽  
Protein C ◽  
Protein S ◽  
Northern Blotting ◽  
Human Testis ◽  
Post Translational Modification ◽  
Reproductive Tissues ◽  
Human Male ◽  
Dependent Protein

Protein C is a vitamin K-dependent protein circulating in plasma as a zymogen to an anticoagulant serine protease. After its activation, protein C cleaves and inactivates coagulation factors Va and VIIIa. Human protein C is synthesized in liver and undergoes extensive post-translational modification during its synthesis. Recently, the protein C inhibitor was demonstrated to be synthesized in several organs of the human male reproductive tract. Moreover, vitamin K-dependent protein S, which functions as a co-factor to activated protein C, was found to be synthesized in the Leydig cells of human testis. The aim of this study was to elucidate whether the protein C gene is also expressed in the male reproductive system. Specific immunostaining of protein C was found in Leydig cells of human testis, in the excretory epithelium of epididymis, and in some epithelial glands of the prostate, whereas no immunostaining was detected in seminal vesicles. Northern blotting and non-radioactive in situ hybridization demonstrated protein C mRNA in Leydig cells, in the excretory epithelium of epididymis, and in some of the epithelial glands of the prostate. The mRNA was distributed perinuclearly and the localization was in accordance with the specific immunostaining for protein C. The epithelium of epididymis was also found to contain both protein S mRNA and immunoreactivity. The demonstration of both protein C and protein S immunoreactivities, as well as their mRNAs, in male reproductive tissues suggests as yet unknown local functions for these proteins.

Abstract 15523: Dynamic Protein S-palmitoylation Contributes to Cardiac Remodeling During Aging With Chronic Hypertension

Circulation ◽  
2020 ◽  
Vol 142 (Suppl_3) ◽  
Author(s):  
Madeleine R Miles ◽  
John Seo ◽  
Zachary Wilson ◽  
Min Jiang ◽  
Gea-ny Tseng
Keyword(s):  
Heart Failure ◽  
Protein Function ◽  
Ventricular Myocytes ◽  
Wide Spectrum ◽  
Enrichment Analysis ◽  
Protein S ◽  
Ventricular Myocardium ◽  
Chronic Hypertension ◽  
Post Translational Modification ◽  
Α Subunit

Introduction: More that 10% of human proteins can be S-palmitoylated, a post-translational modification (PTM) whereby palmitoyl chains are covalently linked to cysteine thiol groups. S-palmitoylation influences protein trafficking, distribution and function. There is no information on the scope of protein S-palmitoylation in the heart, or how this enzyme-mediated reversible PTM is regulated. Hypothesis: S-palmitoylation occurs to a wide spectrum of proteins in cardiomyocytes, and is coordinated by membrane-embedded palmitoylating (DHHC) enzymes. DHHC enzymes are subject to remodeling during chronic hypertension. Methods: We used resin-assisted capture to purify S-palmitoylated proteins from ventricular myocardium of 3 species: human, dog, and rat. We used global unbiased proteomic search to identify S-palmitoylated proteins. We validated DHHC antibodies and used them to monitor protein level and subcellular distribution of native DHHC enzymes in ventricular myocytes. Results: We built a 'composite' cardiac palmitome composed of 462 S-palmitoylatable proteins identified in ≥ 2 species-specific cardiac palmitomes. Enrichment analysis based on GO term 'cellular component' indicated that they are mainly involved in cell-cell and cell-substrate associations, sarcolemma and sarcomere organization, vesicular trafficking, G-protein function, ATP-dependent transmembrane transport, and mitochondria inner and outer membrane organization. Among the 23 DHHC enzymes, we detected ten in hearts across species. In ventricular myocytes with well-defined subcellular compartments, DHHC enzymes exhibited distinct distribution patterns: peripheral sarcolemma (DHHC1), M-lines (DHHC2), Z-lines (DHHC5), vesicles (DHHC7) and intercalated disc (DHHC9). In aging spontaneously hypertensive rats (a model of chronic hypertension, some in heart failure), seven DHHC enzymes were upregulated in the heart, accompanied by a higher degree of S-palmitoylation of CaMK II, caveolin3, Na/Ca exchanger, and Na/K pump α-subunit. Conclusion: S-palmitoylation is involved in most, if not all, aspects of cardiomyocyte function. Palmitoylation dysregulation may contribute to pathological progression in hypertrophy leading to heart failure.

scholarly journals Antioxidant Properties of S-Nitrosoglutathione and Nanotechnologies

Proceedings ◽  
2019 ◽  
Vol 11 (1) ◽  
pp. 15
Author(s):  
Parent ◽  
Zhou ◽  
Bonetti ◽  
Perrin-Sarrado ◽  
Lartaud ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Nitric Oxide ◽  
Cardiovascular Diseases ◽  
Sustained Release ◽  
Antioxidant Properties ◽  
Protein S ◽  
Post Translational Modification ◽  
Antioxidant Power

Cardiovascular diseases are associated with oxidative stress and a reduced bioavailability of nitric oxide (NO). To counteract both processes, the administration of S-nitrosoglutathione (GSNO) can be envisaged. GSNO is able to induce protein S-nitrosation (Pr-SNO), which is a post-translational modification of proteins, participating in the storage of NO in tissues, and protect thiol functions from oxidation. However, GSNO antioxidant power is poorly studied, which is probably linked to its low stability. This low stability can be addressed by nanotechnologies that will increase GSNO protection and provide a sustained release of the drug.

PGluS: prediction of protein S-glutathionylation sites with multiple features and analysis

2015 ◽  
Vol 11 (3) ◽  
pp. 923-929 ◽  
Author(s):  
Xiaowei Zhao ◽  
Qiao Ning ◽  
Meiyu Ai ◽  
Haiting Chai ◽  
Minghao Yin
Keyword(s):  
Protein Stability ◽  
Redox Regulation ◽  
Protein S ◽  
Cysteine Residues ◽  
Post Translational Modification ◽  
Multiple Features ◽  
Mixed Disulfides

S-Glutathionylation is a reversible protein post-translational modification, which generates mixed disulfides between glutathione (GSH) and cysteine residues, playing an important role in regulating protein stability, activity, and redox regulation.

scholarly journals eNOS-dependent S-nitrosylation of the NF-κB subunit p65 has neuroprotective effects

2020 ◽  
Author(s):  
Ariel Caviedes ◽  
Barbara Maturana ◽  
Katherina Corvalán ◽  
Alexander Engler ◽  
Felipe Gordillo ◽  
...  
Keyword(s):  
Cortical Neurons ◽  
Hippocampal Neurons ◽  
Protein S ◽  
Subcellular Fractionation ◽  
Glutamate Excitotoxicity ◽  
Luciferase Reporter ◽  
Biological Processes ◽  
Post Translational Modification ◽  
Neuroprotective Effects ◽  
Biotin Switch

AbstractCell death by glutamate excitotoxicity, mediated by N-methyl-D-aspartate (NMDA) receptors, negatively impacts brain function, including but not limited to hippocampal neurons. The NF-κB transcription factor (composed mainly of p65/p50 subunits) contributes to neuronal death in excitotoxicity, while its inhibition should improve cell survival. Using the biotin switch method, subcellular fractionation, immunofluorescence and luciferase reporter assays, we found that NMDA stimulated NF-κB activity selectively in hippocampal neurons, while endothelial nitric oxide synthase (eNOS), an enzyme expressed in neurons, is involved in the S-nitrosylation of p65 and consequent NF-κB inhibition in cerebrocortical, i.e., resistant neurons. The S-nitro proteomes of cortical and hippocampal neurons revealed that different biological processes are regulated by S-nitrosylation in susceptible and resistant neurons, bringing to light that protein S-nitrosylation is a ubiquitous post-translational modification, able to influence a variety of biological processes including the homeostatic inhibition of the NF-κB transcriptional activity in cortical neurons exposed to NMDA receptor overstimulation.

scholarly journals SwissPalm: Protein Palmitoylation database

F1000Research ◽  
2015 ◽  
Vol 4 ◽  
pp. 261 ◽  
Author(s):  
Mathieu Blanc ◽  
Fabrice David ◽  
Laurence Abrami ◽  
Daniel Migliozzi ◽  
Florence Armand ◽  
...  
Keyword(s):  
Protein S ◽  
Biological Processes ◽  
Post Translational Modification ◽  
Chemical Methods ◽  
Post Translational Modifications ◽  
P Protein ◽  
Multiple Alignments ◽  
Protein Palmitoylation ◽  
Recent Developments ◽  
Pathway Analyses

Protein S-palmitoylation is a reversible post-translational modification that regulates many key biological processes, although the full extent and functions of protein S-palmitoylation remain largely unexplored. Recent developments of new chemical methods have allowed the establishment of palmitoyl-proteomes of a variety of cell lines and tissues from different species.  As the amount of information generated by these high-throughput studies is increasing, the field requires centralization and comparison of this information. Here we present SwissPalm (http://swisspalm.epfl.ch), our open, comprehensive, manually curated resource to study protein S-palmitoylation. It currently encompasses more than 5000 S-palmitoylated protein hits from seven species, and contains more than 500 specific sites of S-palmitoylation. SwissPalm also provides curated information and filters that increase the confidence in true positive hits, and integrates predictions of S-palmitoylated cysteine scores, orthologs and isoform multiple alignments. Systems analysis of the palmitoyl-proteome screens indicate that 10% or more of the human proteome is susceptible to S-palmitoylation. Moreover, ontology and pathway analyses of the human palmitoyl-proteome reveal that key biological functions involve this reversible lipid modification. Comparative analysis finally shows a strong crosstalk between S-palmitoylation and other post-translational modifications. Through the compilation of data and continuous updates, SwissPalm will provide a powerful tool to unravel the global importance of protein S-palmitoylation.

scholarly journals Recent advances in the regulation of plant immunity by S-nitrosylation

2020 ◽  
Author(s):  
Jibril Lubega ◽  
Saima Umbreen ◽  
Gary J Loake
Keyword(s):  
Plant Immunity ◽  
Protein S ◽  
Cellular Protein ◽  
Effector Proteins ◽  
Host Cells ◽  
Immune Functions ◽  
Post Translational Modification ◽  
No Donor ◽  
Reactive Protein ◽  
Recent Advances

Abstract S-nitrosylation, the addition of a nitric oxide (NO) moiety to a reactive protein cysteine (Cys) thiol, to form a protein S-nitrosothiol (SNO), is emerging as a key regulatory post-translational modification (PTM) to control the plant immune response. NO also S-nitrosylates the antioxidant tripeptide, glutathione, to form S-nitrosoglutathione (GSNO), both a storage reservoir of NO bioactivity and a natural NO donor. GSNO and, by extension, S-nitrosylation, are controlled by GSNO reductase1 (GSNOR1). The emerging data suggest that GSNOR1 itself is a target of NO-mediated S-nitrosylation, which subsequently controls its selective autophagy, regulating cellular protein SNO levels. Recent findings also suggest that S-nitrosylation may be deployed by pathogen-challenged host cells to counteract the effect of delivered microbial effector proteins that promote pathogenesis and by the pathogens themselves to augment virulence. Significantly, it also appears that S-nitrosylation may regulate plant immune functions by controlling SUMOylation, a peptide-based PTM. In this context, global SUMOylation is regulated by S-nitrosylation of SUMO conjugating enzyme 1 (SCE1) at Cys139. This redox-based PTM has also been shown to control the function of a key zinc finger transcriptional regulator during the establishment of plant immunity. Here, we provide an update of these recent advances.

scholarly journals A Single Protein S-acyl Transferase Acts through Diverse Substrates to Determine Cryptococcal Morphology, Stress Tolerance, and Pathogenic Outcome

2015 ◽  
Vol 11 (5) ◽  
pp. e1004908 ◽  
Author(s):  
Felipe H. Santiago-Tirado ◽  
Tao Peng ◽  
Meng Yang ◽  
Howard C. Hang ◽  
Tamara L. Doering
Keyword(s):  
Stress Tolerance ◽  
Protein S ◽  
Acyl Transferase ◽  
Single Protein

scholarly journals Tomato Root Growth Inhibition by Salinity and Cadmium Is Mediated By S-Nitrosative Modifications of ROS Metabolic Enzymes Controlled by S-Nitrosoglutathione Reductase

Biomolecules ◽  
2019 ◽  
Vol 9 (9) ◽  
pp. 393 ◽  
Author(s):  
Jedelská ◽  
Kraiczová ◽  
Berčíková ◽  
Činčalová ◽  
Luhová ◽  
...  
Keyword(s):  
Abiotic Stress ◽  
Root Growth ◽  
Growth Inhibition ◽  
Protein S ◽  
Cadmium Stress ◽  
Root Growth Inhibition ◽  
Post Translational Modification ◽  
Tomato Root ◽  
Wild Tomato Species ◽  
Ros Metabolism

S-nitrosoglutathione reductase (GSNOR) exerts crucial roles in the homeostasis of nitric oxide (NO) and reactive nitrogen species (RNS) in plant cells through indirect control of S-nitrosation, an important protein post-translational modification in signaling pathways of NO. Using cultivated and wild tomato species, we studied GSNOR function in interactions of key enzymes of reactive oxygen species (ROS) metabolism with RNS mediated by protein S-nitrosation during tomato root growth and responses to salinity and cadmium. Application of a GSNOR inhibitor N6022 increased both NO and S-nitrosothiol levels and stimulated root growth in both genotypes. Moreover, N6022 treatment, as well as S-nitrosoglutathione (GSNO) application, caused intensive S-nitrosation of important enzymes of ROS metabolism, NADPH oxidase (NADPHox) and ascorbate peroxidase (APX). Under abiotic stress, activities of APX and NADPHox were modulated by S-nitrosation. Increased production of H2O2 and subsequent oxidative stress were observed in wild Solanum habrochaites, together with increased GSNOR activity and reduced S-nitrosothiols. An opposite effect occurred in cultivated S. lycopersicum, where reduced GSNOR activity and intensive S-nitrosation resulted in reduced ROS levels by abiotic stress. These data suggest stress-triggered disruption of ROS homeostasis, mediated by modulation of RNS and S-nitrosation of NADPHox and APX, underlies tomato root growth inhibition by salinity and cadmium stress.

Mechanism and function of DHHC S-acyltransferases

2013 ◽  
Vol 41 (1) ◽  
pp. 29-34 ◽  
Author(s):  
Maurine E. Linder ◽  
Benjamin C. Jennings
Keyword(s):  
Fatty Acids ◽  
Protein S ◽  
Enzyme Mechanism ◽  
Long Chain Fatty Acids ◽  
Post Translational Modification ◽  
Rich Domain ◽  
Cytoplasmic Face ◽  
Protein Membrane ◽  
And Function ◽  
Cysteine Rich Domain

Protein S-palmitoylation is a reversible post-translational modification of proteins with fatty acids. In the last 5 years, improved proteomic methods have increased the number of proteins identified as substrates for palmitoylation from tens to hundreds. Palmitoylation regulates protein membrane interactions, activity, trafficking and stability and can be constitutive or regulated by signalling inputs. A family of PATs (protein acyltransferases) is responsible for modifying proteins with palmitate or other long-chain fatty acids on the cytoplasmic face of cellular membranes. PATs share a signature DHHC (Asp-His-His-Cys) cysteine-rich domain that is the catalytic centre of the enzyme. The biomedical importance of members of this family is underscored by their association with intellectual disability, Huntington's disease and cancer in humans, and raises the possibility of DHHC PATs as targets for therapeutic intervention. In the present paper, we discuss recent progress in understanding enzyme mechanism, regulation and substrate specificity.

Sign in / Sign up

Export Citation Format

Share Document