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766 results for “phosphorylation”
The structural basis of PTEN regulation by multi-site phosphorylation
<p>PTEN is a phosphatidylinositol-3,4,5-triphosphate (PIP<sub>3</sub>) phospholipid phosphatase that is commonly mutated or silenced in cancer. PTEN's catalytic activity, cellular membrane localization, and stability are orchestrated by a cluster of C-terminal phosphorylation events on Ser380, Thr382, Thr383, and Ser385, but the molecular details of this multifaceted regulation have remained uncertain. Here we use a combination of protein semisynthesis, biochemical analysis, NMR, X-ray crystallography, and computational simulations on human PTEN and its sea squirt homolog VSP to obtain a detailed picture of how the phospho-C-tail belts around PTEN's C2 and phosphatase domains. We also visualize a previously proposed dynamic N-terminal alpha-helix and show it is key for PTEN catalysis but disordered upon phospho-C-tail interaction. This structural model provides a comprehensive framework for how C-tail phosphorylation can impact PTEN's cellular functions. </p>
Mapping of phosphorylation modifications of insect cell derived huntingtin (2017/10/04)
<p>Huntingtin structure-function open lab notebook project</p>
Mapping of phosphorylation modifications of insect cell derived huntingtin (2017/10/05)
<p>Huntingtin structure-function open lab notebook project</p>
Mapping of phosphorylation modifications of insect cell derived huntingtin (2017/11/06)
<p>Huntingtin structure function open lab notebook</p>
Analysis of RNA polymerase II phosphorylation in two-color STED microscopy images
<p>This data set includes the raw image data and MatLab analysis scripts to assess the relative distribution of RNA polymerase II C-terminal domain serine 5 and serine 2 phosphorylation in zebrafish embryos. Phosphorylated polymerase II was labeled by immunofluorescence, microscopy images were acquired by STED microscopy and analyzed using MatLab scripts. This extended version now contains image data and analysis scripts to two alternative sets of antibodies.</p>
Influence of YES1 kinase and tyrosine phosphorylation on the activity of OCT1
<p>Organic cation transporter 1 (OCT1) is a transporter that regulates the hepatic uptake and subsequent elimination of diverse cationic compounds. Although OCT1 has been involved in drug-drug interactions and causes pharmacokinetic variability of many prescription drugs, details of the molecular mechanisms that regulate the activity of OCT1 remain incompletely understood. Based on an unbiased phospho-proteomics screen, we identified OCT1 as a tyrosine-phosphorylated transporter, and functional validation studies using genetic and pharmacological approaches revealed that OCT1 is highly sensitive to small molecules that target the protein kinase YES1, such as dasatinib. In addition, we found that dasatinib can inhibit hepatic OCT1 function in mice as evidenced from its ability to modulate levels of isobutyryl L-carnitine, a hepatic OCT1 biomarker identified from a targeted metabolomics analysis. These findings provide novel insight into the post-translational regulation of OCT1 and suggest that caution is warranted with polypharmacy regimes involving the combined use of OCT1 substrates and kinase inhibitors that target YES1.</p>
Hedgehog induced oxidative phosphorylation rescues the neuronal differentiation defect of human enteric neural crest cells underlying Hirschsprung disease
<p>Hedgehog induced oxidative phosphorylation rescues the neuronal differentiation defect of human enteric neural crest cells underlying Hirschsprung disease</p>
Phosphorylated Tau Levels in Donated Blood
ClinicalTrials.gov study NCT07157839. IPD Sharing: NO. Countries: 1. Publications: 0.
Fetuin-A Phosphorylation Status in Insulin Resistance and Metabolic Syndrome
ClinicalTrials.gov study NCT03478046. IPD Sharing: NO. Countries: 1. Publications: 1.
Platelet Acetyl Coenzyme A Carboxylase Phosphorylation in Coronary Artery Disease
ClinicalTrials.gov study NCT03034148. IPD Sharing: NO. Countries: 1. Publications: 2.
Capacitation-associated Protein Tyrosine Phosphorylation As a Possible Biomarker of Sperm Selection
ClinicalTrials.gov study NCT04962100. IPD Sharing: YES. Countries: 1. Publications: 13.
Quantification of Phosphorylated Alpha-synuclein in Cutaneous Biopsies as a Prospective Biomarker in Parkinson's Disease
ClinicalTrials.gov study NCT06621602. IPD Sharing: UNDECIDED. Countries: 1. Publications: 1.
Data from: Oxidative stress-mediated NFκB phosphorylation upregulates p62/SQSTM1 and promotes retinal pigmented epithelial cell survival through increased autophagy
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The structural basis of PTEN regulation by multi-site phosphorylation
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Data from: Oxidative phosphorylation gene transcription in whitefish species pairs reveals patterns of parallel and non-parallel physiological divergence
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Data from: eIF4E S209 phosphorylation licenses myc- and stress-driven oncogenesis
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Influence of YES1 kinase and tyrosine phosphorylation on the activity of OCT1
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Evaluating the inhibition of ALK2 phosphorylation of SMAD1/5 by M4K lead compounds in DIPG patient-derived cells (SU-DIPG-IV, HSJD-DIPG-007, HSJD-DIPG-018 and SU-DIPG-XXI)
<p>The binding potency of M4K compounds to ALK2 has been assayed in biochemical assay and cellular assays in HEK293 or C2C12 myoblast cell lines. However, the potency of ALK2 inhibition by M4K compounds has not determined directly in DIPG patient-derived cell lines. While no major deviation from existing assay data is expected, direct experimental evidence is essential.</p> <p>DIPG cells will be trypsinized and resuspended in TSM-base medium without any growth factor for one-hour starvation. Subsequently, equal volume of TSM-base with 2X Activin A (200ng/mL) and M4K compounds or DMSO vehicle control will be added. After one-hour treatment, the cells will be pelleted and lysed in buffer with protease and phosphatase inhibitors for Western Blot analysis.</p> <p>For other related studies, please refer to my opennotebook blog.</p> <p><a href="https://openlabnotebooks.org/evaluating-the-inhibition-of-alk2-phosphorylation-of-smad1-5-by-m4k-lead-compounds-in-dipg-patient-derived-cells-su-dipg-iv-hsjd-dipg-007-hsjd-dipg-018-and-su-dipg-xxi/">https://openlabnotebooks.org/evaluating-the-inhibition-of-alk2-phosphorylation-of-smad1-5-by-m4k-lead-compounds-in-dipg-patient-derived-cells-su-dipg-iv-hsjd-dipg-007-hsjd-dipg-018-and-su-dipg-xxi/</a></p>
Data from: Meta-analysis of Arabidopsis thaliana phospho-proteomics data reveals compartmentalization of phosphorylation motifs
Protein (de)phosphorylation plays an important role in plants. To provide a robust foundation for subcellular phosphorylation signaling network analysis and kinase-substrate relationships, we performed a meta-analysis of 27 published and unpublished in-house mass spectrometry–based phospho-proteome data sets for Arabidopsis thaliana covering a range of processes, (non)photosynthetic tissue types, and cell cultures. This resulted in an assembly of 60,366 phospho-peptides matching to 8141 nonredundant proteins. Filtering the data for quality and consistency generated a set of medium and a set of high confidence phospho-proteins and their assigned phospho-sites. The relation between single and multiphosphorylated peptides is discussed. The distribution of p-proteins across cellular functions and subcellular compartments was determined and showed overrepresentation of protein kinases. Extensive differences in frequency of pY were found between individual studies due to proteomics and mass spectrometry workflows. Interestingly, pY was underrepresented in peroxisomes but overrepresented in mitochondria. Using motif-finding algorithms motif-x and MMFPh at high stringency, we identified compartmentalization of phosphorylation motifs likely reflecting localized kinase activity. The filtering of the data assembly improved signal/noise ratio for such motifs. Identified motifs were linked to kinases through (bioinformatic) enrichment analysis. This study also provides insight into the challenges/pitfalls of using large-scale phospho-proteomic data sets to nonexperts.
Data from: Arabidopsis MKK10-MPK6 mediates red-light-regulated opening of seedling cotyledons through phosphorylation of PIF3
Photomorphogenesis is an important process in which seedlings emerge from soil and begin autotrophic growth. Photomorphogenesis mechanisms include light signal perception, signal transduction, and the modulation of light-responsive genes expression, ultimately leading to cellular and developmental changes. Phytochrome-interacting factors (PIFs) play pivotal roles in negatively regulating photomorphogenesis. Light-induced activation of phytochromes triggers the rapid phosphorylation and degradation of PIFs, but the kinases responsible for the phosphorylation of PIFs are largely unknown. Here, we show that Arabidopsis MPK6 is a kinase involved in phosphorylating PIF3 and regulating red (R) light-induced cotyledon opening, a crucial process during seedling photomorphogenesis. MPK6 was activated by R light, and cotyledon opening angle in R light was reduced in mpk6 seedlings. MKK10, a MAPKK whose function is currently unclear, appears to act as a kinase upstream of MPK6 in regulating cotyledon opening. The activation of MPK6 by MKK10 led to the phosphorylation of PIF3 and accelerated its turnover in transgenic seedlings. Accordingly, the overexpression of PIF3 suppressed the MKK10-induced cotyledon opening. MKK10-MPK6 function downstream of phyB in regulating seedlings cotyledon opening in R light. Therefore, MKK10-MPK6 cascade appears to mediate the regulation of R light-controlled seedling photomorphogenesis,via a mechanism that might involve the phosphorylation of PIF3.
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Allen Brain Atlas
Allen Brain Atlas is an Allen Institute collection of brain map atlases, datasets, APIs, and analysis tools covering mouse, human, and non-human primate brain resources.
Annotated Behaviour and Observability Dataset (ABODe)
ABODe is a University of Edinburgh DataShare dataset for behavior classification in group-housed mice using home-cage video, identities, bounding boxes, ground-plate positions, and annotator labels.
DANDI Archive for NWB datasets
DANDI is a BRAIN Initiative archive for publishing and sharing neurophysiology data, including electrophysiology, optophysiology, and behavioral data packaged as NWB and related standards.
International Brain Laboratory public data
The International Brain Laboratory public data releases expose standardized mouse decision-making experiments, including Neuropixels recordings, widefield calcium imaging, behavior, and session metadata accessed through the ONE API.
OpenNeuro
OpenNeuro is a free, open platform for sharing neuroimaging datasets, with public search, dataset pages, and download paths for web, S3, DataLad, and the OpenNeuro CLI.