New partners and phosphorylation sites of focal adhesion kinase identified by mass spectrometry
| Autor: | Jesús M. Ureña, Maria del Mar Masdeu, Ferran Burgaya, Beatriz G. Armendáriz, Eduardo Soriano |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Protein subunit PTK2 Biophysics Plasma protein binding Biochemistry Plakophilin Focal adhesion Mice 03 medical and health sciences Seizures Tandem Mass Spectrometry Catalytic Domain Animals Immunoprecipitation Phosphorylation Molecular Biology Binding Sites Neuronal Plasticity Kinase Chemistry Brain Cell biology Enzyme Activation Disease Models Animal 030104 developmental biology Animals Newborn Focal Adhesion Kinase 1 Pentylenetetrazole Signal transduction Chromatography Liquid Protein Binding Signal Transduction |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - General Subjects. 1860:1388-1394 |
| ISSN: | 0304-4165 |
| Popis: | The regulation of focal adhesion kinase (FAK) involves phosphorylation and multiple interactions with other signaling proteins. Some of these pathways are relevant for nervous system functions such as branching, axonal guidance, and plasticity. In this study, we screened mouse brain to identify FAK-interactive proteins and phosphorylatable residues as a first step to address the neuronal functions of this kinase. Using mass spectrometry analysis, we identified new phosphorylated sites (Thr 952, Thr 1048, and Ser 1049), which lie in the FAT domain; and putative new partners for FAK, which include cytoskeletal proteins such as drebrin and MAP 6, adhesion regulators such as neurabin-2 and plakophilin 1, and synapse-associated proteins such as SynGAP and a NMDA receptor subunit. Our findings support the participation of brain-localized FAK in neuronal plasticity. |
| Databáze: | OpenAIRE |
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