Tyrosine phosphorylation of paxillin, FAK, and p130CAS: effects on cell spreading and migration.
@article{Panetti2002TyrosinePO, title={Tyrosine phosphorylation of paxillin, FAK, and p130CAS: effects on cell spreading and migration.}, author={Tracee Scalise Panetti}, journal={Frontiers in bioscience : a journal and virtual library}, year={2002}, volume={7}, pages={ d143-50 } }
Integrins are transmembrane receptors that mediate cell attachment to the substrate. At the cytoplasmic surface of the integrin, cytoskeletal proteins cluster into focal adhesions. The focal adhesions contain multiple proteins that provide a structural and signaling complex inside the cell. This review focuses on three of the cytoskeletal components of the focal adhesion, paxillin, FAK, and p130CAS, that are phosphorylated and play a regulatory role in cell spreading and cell migration. A brief…
152 Citations
A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions
- BiologyJournal of Cell Science
- 2007
Tyrosine phosphorylation of the adaptor protein paxillin functions as a major switch, regulating the adhesive phenotype of cells, and a mathematical model recapitulates the salient features of the measured dynamics is created.
Defining the phospho-adhesome through the phosphoproteomic analysis of integrin signalling
- BiologyNature communications
- 2015
A proteomic and phosphoproteomic analysis of adhesion complexes isolated from cells spread on fibronectin identifies 1,174 proteins, 499 of which are phosphorylated (1,109 phosphorylation sites), including both well-characterized and novel adhesion-regulated phosphorylate events.
Upregulation of paxillin and focal adhesion signaling follows Dystroglycan Complex deletions and promotes a hypertensive state of differentiation.
- BiologyEuropean journal of cell biology
- 2011
Low M r Phosphotyrosine Protein Phosphatase Associates and Dephosphorylates p125 Focal Adhesion Kinase, Interfering with Cell Motility and Spreading*
- BiologyThe Journal of Biological Chemistry
- 2002
It is demonstrated that low M r phosphotyrosine protein phosphatase-overexpressing fibroblasts are, indeed, less spread than controls and display a significantly decreased number of focal adhesions and increased cell motility, and that p125 focal adhesion kinase is associated to, and dephosphorylated by, lowM r phospholipase bothin vitro and in vivo.
Tyrosine phosphorylation of type Iγ phosphatidylinositol phosphate kinase by Src regulates an integrin–talin switch
- Biology, ChemistryThe Journal of cell biology
- 2003
A novel phosphotyrosine-binding site on the talin F3 domain and a “molecular switch” for talin binding between PIPKIγ661 and β-integrin that may regulate dynamic FA turnover are defined.
Protein tyrosine phosphatases in cell adhesion
- BiologyThe Biochemical journal
- 2021
This review will focus on human PTPs and discuss their individual roles in major adhesion complexes, as well as Hippo signalling, which reveal extensive connections between P TPs and cell adhesions that are relatively unexplored.
Endothelial paxillin and focal adhesion kinase (FAK) play a critical role in neutrophil transmigration
- Biology, MedicineEuropean journal of immunology
- 2012
A novel role is revealed for endothelial focal adhesion proteins paxillin and FAK in regulating neutrophil transmigration and disruption of the FAK protein or FAK signaling decreased neutrophIL transmigration.
Regulation of focal adhesions by flightless i involves inhibition of paxillin phosphorylation via a Rac1-dependent pathway.
- BiologyThe Journal of investigative dermatology
- 2011
It is shown that Flii modulation of focal adhesions and filamentous actin stress fibers is Rac1-dependent and overexpression of constitutively active Rac1 GTPase restores the spreading ability of Flii(Tg/Tg) fibroblasts and may explain the reduced adhesion, migration, and proliferation observed in Flii’s mice and their impaired wound healing.
Characterization of the Phospho-Adhesome by Mass Spectrometry-Based Proteomics.
- BiologyMethods in molecular biology
- 2017
Compared to phosphoproteomic analyses of cell lysates, the workflow described here enables an improved detection of phosphorylation sites from well-defined IAC proteins, including many known components of the signaling pathways activated by adhesion to the ECM.
Revealing the three dimensional architecture of focal adhesion components to explain Ca2+-mediated turnover of focal adhesions.
- Biology, MedicineBiochimica et biophysica acta. General subjects
- 2017
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