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
        }
}
  • T. S. Panetti
  • Published 2002
  • Chemistry, Medicine
  • Frontiers in bioscience : a journal and virtual library
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… Expand
View on PubMed
bioscience.org
151 Citations
Highly Influential Citations
6
Background Citations
74
Methods Citations
2
Results Citations
2

151 Citations

Citation Type

Citation Type

A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions
TLDR
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. Expand
Defining the phospho-adhesome through the phosphoproteomic analysis of integrin signalling
TLDR
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. Expand
Upregulation of paxillin and focal adhesion signaling follows Dystroglycan Complex deletions and promotes a hypertensive state of differentiation.
TLDR
Hypertension that results from upregulation of integrin adhesions is thus a natural and treatable outcome of Dystroglycan Complex down-regulation. Expand
Low M r Phosphotyrosine Protein Phosphatase Associates and Dephosphorylates p125 Focal Adhesion Kinase, Interfering with Cell Motility and Spreading*
TLDR
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. Expand
Tyrosine phosphorylation of type Iγ phosphatidylinositol phosphate kinase by Src regulates an integrin–talin switch
TLDR
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. Expand
Protein tyrosine phosphatases in cell adhesion
TLDR
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. Expand
Endothelial paxillin and focal adhesion kinase (FAK) play a critical role in neutrophil transmigration
TLDR
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. Expand
Regulation of focal adhesions by flightless i involves inhibition of paxillin phosphorylation via a Rac1-dependent pathway.
TLDR
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. Expand
Characterization of the Phospho-Adhesome by Mass Spectrometry-Based Proteomics.
TLDR
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. Expand
Revealing the three dimensional architecture of focal adhesion components to explain Ca2+-mediated turnover of focal adhesions.
TLDR
Three-dimensional fluorescence imaging and immunoblotting demonstrated that outer FA molecules were more sensitive to calpain-mediated proteolysis than internal FA molecules, and suggested that cell contraction is not involved in degradation of FA. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 69 REFERENCES
Focal adhesion kinase in integrin-mediated signaling.
  • L. Cary, J. Guan
  • Medicine
  • Frontiers in bioscience : a journal and virtual library
  • 1999
TLDR
Focal adhesion kinase's roles in the regulation of several integrin-mediated cellular events are discussed, including the promotion of cell migration, proliferation and spreading, and the prevention of cell apoptosis. Expand
Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly
TLDR
A role for integrin- mediated tyrosine phosphorylation in the organization of the cytoskeleton as cells adhere to the extracellular matrix is suggested. Expand
Fibronectin and Integrins in Cell Adhesion, Signaling, and Morphogenesis
TLDR
Fibronectin and integrins trigger a hierarchy of signaling responses involved in regulating processes crucial for normal morphogenesis, including cell adhesion, migration, and specific gene expression. Expand
Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice
TLDR
Surprisingly, the number of focal adhesions was increased in FAK-deficient cells, suggesting that FAK may be involved in the turnover of focalAdhesion contacts during cell migration. Expand
Focal Adhesion Kinase: a regulator of focal adhesion dynamics and cell movement
TLDR
The role of the focal complex associated protein tyrosine kinase, Focal Adhesion Kinase (FAK), is considered in the regulation of cell movement with the emphasis on how FAK regulates the flow of signals from the ECM to the actin cytoskeleton. Expand
Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn.
TLDR
It is reported here that overexpression of FAK in CHO cells increased their migration on fibronectin, and a mutation of the major autophosphorylation site Y397 in FAK abolished its ability to stimulate cell migration, while phosphorylation in a kinase-defective FAK by endogenous FAK led to increased migration. Expand
Integrin-mediated signal transduction pathways.
Integrins serve as adhesion receptors for extracellular matrix proteins and also transduce biochemical signals into the cell. They regulate a variety of cellular functions, including spreading,… Expand
Paxillin alpha and Crk-associated substrate exert opposing effects on cell migration and contact inhibition of growth through tyrosine phosphorylation.
  • H. Yano, H. Uchida, +5 authors H. Sabe
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 2000
TLDR
It is proposed that tyrosine phosphorylation of paxillin alpha and p130(Cas) exerts opposing effects on several integrin-mediated cellular events, possibly through different signaling pathways. Expand
Paxillin interactions.
TLDR
Paxillin binds to many proteins that are involved in effecting changes in the organization of the actin cytoskeleton, which are necessary for cell motility events associated with embryonic development, wound repair and tumor metastasis. Expand
Tyrosine phosphorylation is involved in reorganization of the actin cytoskeleton in response to serum or LPA stimulation.
TLDR
The findings suggest that the response to serum is complex and that although FAK phosphorylation is important, other tyrosine kinases may also be involved. Expand
...
1
2
3
4
5
...