A5086344868- Cell Adhesion Molecules Research
- Plant Virus Research Studies
- Cellular Mechanics and Interactions
- Insect Resistance and Genetics
- Transgenic Plants and Applications
- Viral gastroenteritis research and epidemiology
- CRISPR and Genetic Engineering
- Bacteriophages and microbial interactions
- Hippo pathway signaling and YAP/TAZ
- RNA and protein synthesis mechanisms
- Protein Kinase Regulation and GTPase Signaling
- Nerve injury and regeneration
- Peptidase Inhibition and Analysis
- Cellular transport and secretion
- Sleep and Wakefulness Research
- Insect-Plant Interactions and Control
- Signaling Pathways in Disease
- Plant and Fungal Interactions Research
- Viral Infections and Immunology Research
- NF-κB Signaling Pathways
- Glycosylation and Glycoproteins Research
- Enzyme Structure and Function
- Animal Virus Infections Studies
- Neuroscience and Neuropharmacology Research
- Microtubule and mitosis dynamics
Inserm
2001-2022
Sorbonne Université
2002-2022
Institut du Fer à Moulin
2002-2022
Université Libre de Bruxelles
2001
Institut Jacques Monod
1992-1999
Focal adhesion kinase (FAK) is activated following integrin engagement or stimulation of transmembrane receptors. Autophosphorylation FAK on Tyr-397 a critical event, allowing binding Src family kinases and activation signal transduction pathways. Tissue-specific alternative splicing generates several isoforms with different autophosphorylation rates. Despite its importance, the mechanisms basis for differences between are not known. We addressed these questions using expressed in brain....
Ezrin, a membrane-cytoskeleton linker, is required for cell morphogenesis, motility, and survival through molecular mechanisms that remain to be elucidated. Using the N-terminal domain of ezrin as bait, we found p125 focal adhesion kinase (FAK) interacts with ezrin. We show two proteins coimmunoprecipitate from cultured lysates. However, FAK does not interact full-length <i>in vitro</i>, indicating binding site on cryptic. Mapping experiments showed entire (amino acids 1–376) optimal...
Focal adhesion kinase (FAK) is a protein tyrosine enriched in focal adhesions, which plays critical role integrin-dependent cell motility and survival. The crucial step its activation autophosphorylation on Tyr-397, promotes the recruitment of several enzymes including Src family kinases multiple signaling pathways. We found yeast two-hybrid screen that N-terminal domain FAK interacted with inhibitor activated STAT1 (PIAS1). This interaction was confirmed shown to be direct using vitro...
Abstract Multidomain kinases use many ways to integrate and process diverse stimuli. Here, we investigated the mechanism by which protein tyrosine kinase 2-beta (PYK2) functions as a sensor effector of cellular calcium influx. We show that linker between PYK2 FAT domains (KFL) encompasses an unusual calmodulin (CaM) binding element. KFL is disordered engages CaM through ensemble transient events. Calcium increases association promoting structural changes in expose auxiliary interaction...
In hippocampus endocannabinoids modulate synaptic function and plasticity increase tyrosine phosphorylation of several proteins, including focal adhesion kinase (FAK). Autophosphorylation FAK on Tyr-397 is generally a critical step for its activation, allowing the recruitment Src family kinases, associated proteins. We have examined mechanisms regulation by cannabinoids in rat mouse hippocampal slices. Anandamide 2-arachidonoylglycerol, two endocannabinoids, Δ9-tetrahydrocannabinol,...
Proline-rich tyrosine kinase 2 (PYK2) is a non-receptor expressed in many cell types and enriched neurons. PYK2 cytoplasmic enzyme activated by increases cytosolic free Ca(2+) through an unknown mechanism. We report that depolarization or electrical stimulation of hippocampal slices induced rapid transient nuclear accumulation PYK2. Depolarization cultured neurons PC12 cells also triggered Ca(2+)-dependent PYK2, much more pronounced than blockade export with leptomycin B. Src-family...
The large non-structural polyprotein (206 kDa) of turnip yellow mosaic tymovirus (TYMV) undergoes auto-cleavage, producing N- and C-terminal proteins. Here we show that the viral proteinase responsible for this event is active when produced in Escherichia coli, as monitored Western blots by examining generation cleavage product after induction IPTG. outer boundaries critical amino acids domain were characterized deletion analysis site-directed mutagenesis. A miniproteinase 273 residues...
The 206-kDa protein of turnip yellow mosaic virus belongs to an expanding group proteins containing a domain which includes the consensus nucleotide binding site GxxxxGKS/T. A portion this (amino acids [aa] 916 1259) was expressed in Escherichia coli and purified by affinity chromatography near homogeneity. In absence any other viral factors, it exhibited ATPase GTPase activities vitro. mutant with single amino acid substitution (Lys-982 Ser) only low levels both activities, implying that...
Total nucleotide sequencing of the RNA genome various tymoviruses has demonstrated that overall organization these viruses is identical. Furthermore, strategies expression turnip yellow mosaic virus (TYMV) have been established by in vitro translation studies; include synthesis a subgenomic RNA, utilization overlapping open reading frames (ORFs) and maturation polyprotein. In experiments described here, other tymovirus (eggplant virus, ononis belladonna mottle physalis virus) genomes...