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38 results for “palmitoylation”
NAMD Trajectory of a Palmitoyl Sphingomyelin Bilayer
<p>All-atom PSM bilayer simulated in NPT ensemble with NAMD and the CHARMM36 force field from Doktorova et al. 2020 J. Phys. Chem. B. article (DOI 10.1021/acs.jpcb.0c03389). The trajectory represents the last 117 ns used for analysis where the area per lipid is equilibrated (the file has 5874 frames output every 20 ps). The bilayer has 200 lipids total (100 lipids per leaflet) and is hydrated with 45 waters/lipid. The simulation was done at 55C (328.15K) and the trajectory is centered on the bilayer midplane.</p>
Allosteric Modulation of YAP/TAZ-TEAD Interaction by Palmitoylation and Small Molecule Inhibitors
<p>The tar file contains 3 directories, each of which contains all of the simulation input files (pdb, prmtop, inpcrd) and trajectory files (nc) for the simulations run. </p><ol><li>TEAD_Only: Simulations of the TEAD protein in the apo, inhibitor(inh)-bound, palmitate(plt)-bound, or palmitic acid(plm)-bound form </li><li>YAP-TEAD: Simulations of the YAP-TEAD heterodimer in the apo, inhibitor(inh)-bound, palmitate(plt)-bound, or palmitic acid(plm)-bound form </li><li>TAZ-TEAD: Simulations of the TAZ-TEAD heterodimer in the apo, inhibitor(inh)-bound, palmitate(plt)-bound, or palmitic acid(plm)-bound form </li></ol>
"Palmitoylation Mediates Membrane Association of Hepatitis E Virus ORF3 Protein and is Required for Infectious Particle Secretion"
<p><strong>Hepatitis E virus (HEV) is a positive-strand RNA virus encoding 3 open reading frames (ORF). HEV ORF3 protein is a small, hitherto poorly characterized protein involved in viral particle secretion and possibly other functions. Here, we show that HEV ORF3 protein forms membrane-associated oligomers. Immunoblot analyses of ORF3 protein expressed in cell-free <em>vs</em>. cellular systems suggested a posttranslational modification. Further analyses revealed that HEV ORF3 protein is palmitoylated at cysteine residues in its N-terminal region, as corroborated by <sup>3</sup>H-palmitate labeling, the investigation of cysteine-to-alanine substitution mutants and treatment with the palmitoylation inhibitor 2-bromopalmitate (2-BP). Abrogation of palmitoylation by site-directed mutagenesis or 2-BP treatment altered the subcellular localization of ORF3 protein, reduced the stability of the protein and strongly impaired the secretion of infectious particles. </strong><strong>Moreover, selective membrane permeabilization coupled with immunofluorescence microscopy revealed that HEV ORF3 protein is entirely exposed to the cytosolic side of the membrane, allowing to propose a model for its membrane topology and interactions required in the viral life cycle. </strong><strong>In conclusion, palmitoylation determines the subcellular localization, membrane topology and function of HEV ORF3 protein in the HEV life cycle. </strong></p>
Syntaxin 1A Transmembrane Domain Palmitoylation Induces a Fusogenic Conformation
<p>All parameter files to repeat simulations and the code for extract and analyze simulation data in the manuscript titled 'Syntaxin 1A Transmembrane Domain Palmitoylation Induces a Fusogenic Conformation' are included here. Simulation data was extracted by either <em>gromacs</em> or <em>mdtraj</em> package from simulation xtc trajectory files which are too large to provide here. Rather, they will be provided upon reasonable request.</p> <p>All simulations are performed by GROMACS 2021 in Triton supercomputer from Frost Institute for Data Science and Computing (IDSC) in University of Miami.</p> <p>All code files for extract and analyze simulation data are written in python on Jupyter notebooks and notebook files to make plots are run on Google Colab. </p> <p>The version of <em>matplotlib</em> to make plots is 3.7.3, <em>seaborn</em> is 0.11, and the <em>statannotations</em> is 0.6.0.</p>
Data from: Proteolytic processing of palmitoylated Hedgehog peptides specifies the 3-4 intervein region of the Drosophila wing
Cell fate determination during development often requires morphogen transport from producing to distant responding cells. Hedgehog (Hh) morphogens present a challenge to this concept, as all Hhs are synthesized as terminally lipidated molecules that form insoluble clusters at the surface of producing cells. While several proposed Hh transport modes tie directly into these unusual properties, the crucial step of Hh relay from producing cells to receptors on remote responding cells remains unresolved. Using wing development in Drosophila melanogaster as a model, we show that Hh relay and direct patterning of the 3-4 intervein region strictly depend on proteolytic removal of lipidated N-terminal membrane anchors. Site-directed modification of the N-terminal Hh processing site selectively eliminated the entire 3-4 intervein region, and additional targeted removal of N-palmitate restored its formation. Hence, palmitoylated membrane anchors restrict morphogen spread until site-specific processing switches membrane-bound Hh into bioactive forms with specific patterning functions.
Unconventional secretion of alpha-synuclein mediated by palmitoylated DNAJC5 oligomers
<p>Alpha-synuclein (α-syn), a major component of Lewy bodies found in Parkinson’s disease (PD) patients, has been found exported outside of cells and may mediate its toxicity via cell-to-cell transmission. Here, we reconstituted soluble, monomeric α-syn secretion by the expression of DnaJ homolog subfamily C member 5 (DNAJC5) in HEK293T cells. DNAJC5 undergoes palmitoylation and anchors on the membrane. Palmitoylation is essential for DNAJC5-induced α-syn secretion, and the secretion is not limited by substrate size or unfolding. Cytosolic α-syn is actively translocated and sequestered in an endosomal membrane compartment in a DNAJC5-dependent manner. Reduction of α-syn secretion caused by a palmitoylation-deficient mutation in DNAJC5 can be reversed by a membrane-targeting peptide fusion-induced oligomerization of DNAJC5. The secretion of endogenous α-syn mediated by DNAJC5 is also found in a human neuroblastoma cell line, SH-SY5Y, differentiated into neurons in the presence of retinoic acid, and in human-induced pluripotent stem cell-derived midbrain dopamine neurons. We propose that DNAJC5 forms a palmitoylated oligomer to accommodate and export α-syn.</p>
Data from: Proteolytic processing of palmitoylated Hedgehog peptides specifies the 3-4 intervein region of the Drosophila wing
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Protein palmitoylation and sphingolipid metabolism control regulated exocytosis in cytotoxic lymphocytes
GEO Series GSE307513. Homo sapiens. 7 samples. Type: Other.
Next Generation Sequencing Quantitative Analysis of TEAD Palmitoylation Inhibitor MGH-CP1 in Breast Cancer Cell Line
GEO Series GSE140396. Homo sapiens. 4 samples. Type: Expression profiling by high throughput sequencing.
Palmitoylation prevents B7-H4 lysosomal degradation sustaining tumor immune evasion
GEO Series GSE272492. Homo sapiens. 6 samples. Type: Expression profiling by high throughput sequencing.
A palmitoylation-depalmitoylation relay spatiotemporally controls GSDMD activation in pyroptosis [II]
GEO Series GSE252911. Mus musculus. 18 samples. Type: Expression profiling by high throughput sequencing.
Rac1 palmitoylation is required for cardiac stress adaptation and regulation of Protein Kinase A signaling
GEO Series GSE305462. Mus musculus. 18 samples. Type: Expression profiling by high throughput sequencing.
Spatial Transcriptomics Unravels Palmitoylation and Zonation-Dependent Gene Regulation by AEG-1 in Mouse Liver
GEO Series GSE261057. Mus musculus. 2 samples. Type: Other.
Palmitoyl acyltransferase ZDHHC7 suppresses prostate cancer through inhibiting androgen receptor expression
GEO Series GSE222592. Homo sapiens. 24 samples. Type: Expression profiling by high throughput sequencing.
A palmitoylation-depalmitoylation relay spatiotemporally controls GSDMD activation in pyroptosis [I]
GEO Series GSE252893. Mus musculus. 72 samples. Type: Expression profiling by high throughput sequencing.
Dynamic nitrosation - palmitoylation of CD36 regulates serum lipids
GEO Series GSE260897. Homo sapiens. 12 samples. Type: Expression profiling by high throughput sequencing.
ZDHHC20-Mediated S-Palmitoylation of YTHDF3 Stabilizes MYC mRNA to Promote Pancreatic Cancer Progression
GEO Series GSE235516. Homo sapiens. 6 samples. Type: Expression profiling by high throughput sequencing.
ZDHHC15 mediates Hippo/YAP pathway palmitoylation and regulates tumor progression [HCC1954]
GEO Series GSE235258. Homo sapiens. 4 samples. Type: Expression profiling by high throughput sequencing.
The expression of genes encoding palmitoylated proteins in axonal and synaptic compartments is affected in CLN1/PPT1 transfected neuronal cells
GEO Series GSE98834. Homo sapiens. 12 samples. Type: Expression profiling by high throughput sequencing.
Deficiency of the palmitoyl acyltransferase ZDHHC7 modulates gene expression in mice after a mild chronic stress paradigm
GEO Series GSE281404. Mus musculus. 80 samples. Type: Expression profiling by high throughput sequencing.
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