Roles of protein tyrosine phosphatases in cell migration and adhesion

1999 ◽  
Vol 77 (6) ◽  
pp. 493-505 ◽  
Author(s):  
Alexandre Angers-Loustau ◽  
Jean-François Côté ◽  
Michel L Tremblay
Keyword(s):  
Tyrosine Kinases ◽  
Protein Tyrosine Phosphatases ◽  
Cellular Migration ◽  
Tyrosine Phosphatases ◽  
Integrin Receptors ◽  
Protein Tyrosine ◽  
Kinase C ◽  
Cell Adhesion And Migration ◽  
And Migration ◽  
The Individual

Signal transduction pathways are often seen as cascades of kinases, whereas phosphatases are relinquished to the housekeeping function of resetting the individual elements to a resting state. However, critical biological processes such as cellular migration require a coordinated and constant remodeling of the actin cytoskeleton as well as a rapid turnover of the cell-substratum linkages that necessitate the concomitant action of antagonistic enzymes. Tyrosine phosphorylation was long known to be involved in adhesion and de-adhesion mediated via the integrin receptors. As the roles of tyrosine kinases such as focal adhesion kinase, c-Src, and Csk in this pathway are being extensively studied, increasing evidence is emerging about the importance of protein tyrosine phosphatases (PTP). In this review we discuss examples of PTPs that were recently shown to play a role in cell adhesion and migration and their mechanism of action.Key words: protein tyrosine phosphatases (PTP), migration, adhesion, FAK, p130Cas, Src.

scholarly journals Protein tyrosine phosphatases and signalling

2005 ◽  
Vol 185 (1) ◽  
pp. 19-33 ◽  
Author(s):  
Andrew W Stoker
Keyword(s):  
Tyrosine Kinases ◽  
Current Knowledge ◽  
Insulin Signalling ◽  
Cell Signalling ◽  
Protein Tyrosine Phosphatases ◽  
Protein Tyrosine Kinases ◽  
Tyrosine Phosphatases ◽  
Large Protein ◽  
Protein Tyrosine ◽  
Wide Range

A cornerstone of many cell-signalling events rests on reversible phosphorylation of tyrosine residues on proteins. The reversibility relies on the coordinated actions of protein tyrosine kinases and protein tyrosine phosphatases (PTPs), both of which exist as large protein families. This review focuses on the rapidly evolving field of the PTPs. We now know that rather than simply scavenging phosphotyrosine, the PTPs specifically regulate a wide range of signalling pathways. To illustrate this and to highlight current areas of agreement and contention in the field, this review will present our understanding of PTP action in selected areas and will present current knowledge surrounding the regulatory mechanisms that control PTP enzymes themselves. It will be seen that PTPs control diverse processes such as focal adhesion dynamics, cell–cell adhesion and insulin signalling, and their own actions are in turn regulated by dimerisation, phosphorylation and reversible oxidation.

Characterization of hematopoietic intracellular protein tyrosine phosphatases: description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences

1992 ◽  
Vol 12 (5) ◽  
pp. 2396-2405
Author(s):  
R J Matthews ◽  
D B Bowne ◽  
E Flores ◽  
M L Thomas
Keyword(s):  
Signal Transduction ◽  
Glutamic Acid ◽  
Tyrosine Kinases ◽  
Protein Tyrosine Phosphatases ◽  
Sh2 Domain ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine ◽  
Sh2 Domains

Protein tyrosine phosphatases (PTPases) are a family of enzymes important in cellular regulation. Characterization of two cDNAs encoding intracellular PTPases expressed primarily in hematopoietic tissues and cell lines has revealed proteins that are potential regulators of signal transduction. One of these, SHP (Src homology region 2 [SH2]-domain phosphatase), possesses two tandem SH2 domains at the amino terminus of the molecule. SH2 domains have previously been described in proteins implicated in signal transduction, and SHP may be one of a family of nonreceptor PTPases that can act as direct antagonists to the nonreceptor protein tyrosine kinases. The SH2 domains of SHP preferentially bind a 15,000-Mr protein expressed by LSTRA cells. LSTRA cells were shown to express SHP protein by immunoprecipitation, thus demonstrating a potential physiological interaction. The other PTPase, PEP (proline-, glutamic acid-, serine-, and threonine-rich [PEST]-domain phosphatase), is distinguished by virtue of a large carboxy-terminal domain of approximately 500 amino acids that is rich in PEST residues. PEST sequences are found in proteins that are rapidly degraded. Both proteins have been expressed by in vitro transcription and translation and in bacterial expression systems, and both have been demonstrated to have PTPase activity. These two additional members of the PTPase family accentuate the variety of PTPase structures and indicate the potential diversity of function for intracellular tyrosine phosphatases.

scholarly journals Modulation of intercellular adherens-type junctions and tyrosine phosphorylation of their components in RSV-transformed cultured chick lens cells.

1991 ◽  
Vol 2 (2) ◽  
pp. 105-120 ◽  
Author(s):  
T Volberg ◽  
B Geiger ◽  
R Dror ◽  
Y Zick
Keyword(s):  
Tyrosine Kinases ◽  
Protein Tyrosine Phosphatases ◽  
Transformed Cells ◽  
Permissive Temperature ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine ◽  
Cell Substrate ◽  
Lens Cells ◽  
Sites Of Action ◽  
Chick Lens

Transformation of cultured chick lens epithelial cells with a temperature-sensitive mutant of Rous sarcoma virus (tsRSV) leads to radical changes in cell shape and interactions. When cultured at the restrictive temperature (42 degrees C), the transformed cells largely retained epithelial morphology and intercellular adherens junctions (AJ), whereas on switch to the permissive temperature (37 degrees C) they rapidly became fibroblastoid, their AJ deteriorated, and cell adhesion molecules (A-CAM) (N-cadherin) largely disappeared from intercellular contact sites. The microfilament system that was primarily associated with these junctions was markedly rearranged on shift to 37 degrees C and remained associated mainly with cell-substrate focal contacts. These apparent changes in intercellular AJ were not accompanied by significant alterations in the cellular content of several junction-associated molecules, including A-CAM, vinculin, and talin. Immunolabeling with phosphotyrosine-specific antibodies indicated that both cell-substrate and intercellular AJ were the major cellular targets for the pp60v-src tyrosine-specific protein kinase. It was further shown that intercellular AJ components serve as substrates to tyrosine kinases also in nontransformed lens cells, because the addition of a combination of vanadate and H2O2--which are potent inhibitors of protein tyrosine phosphatases--leads to a remarkable accumulation of immunoreactive phosphotyrosine-containing proteins in these junctions. This finding suggests that intercellular junctions are major sites of action of protein tyrosine kinases and that protein tyrosine phosphatases play a major role in the regulation of phosphotyrosine levels in AJ of both normal and RSV-transformed cells.

scholarly journals Protein-tyrosine Kinases Activate while Protein-tyrosine Phosphatases Inhibit L-type Calcium Channel Activity in Pituitary GH Cells

1996 ◽  
Vol 271 (16) ◽  
pp. 9441-9446 ◽  
Author(s):  
Mauro Cataldi ◽  
Maurizio Taglialatela ◽  
Salvatore Guerriero ◽  
Salvatore Amoroso ◽  
Gaetano Lombardi ◽  
...  
Keyword(s):  
Calcium Channel ◽  
Tyrosine Kinases ◽  
Protein Tyrosine Phosphatases ◽  
Protein Tyrosine Kinases ◽  
Channel Activity ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine ◽  
Gh Cells

scholarly journals Protein tyrosine phosphatases in cell adhesion

2021 ◽  
Vol 478 (5) ◽  
pp. 1061-1083
Author(s):  
Katherine A. Young ◽  
Laura Biggins ◽  
Hayley J. Sharpe
Keyword(s):  
Cell Adhesion ◽  
Tyrosine Kinases ◽  
Protein Tyrosine Phosphatases ◽  
Tyrosine Phosphatases ◽  
Post Translational Modifications ◽  
Protein Tyrosine ◽  
Surrounding Matrix ◽  
Cell Adhesions ◽  
Multicellular Organisms ◽  
Extracellular Environment

Adhesive structures between cells and with the surrounding matrix are essential for the development of multicellular organisms. In addition to providing mechanical integrity, they are key signalling centres providing feedback on the extracellular environment to the cell interior, and vice versa. During development, mitosis and repair, cell adhesions must undergo extensive remodelling. Post-translational modifications of proteins within these complexes serve as switches for activity. Tyrosine phosphorylation is an important modification in cell adhesion that is dynamically regulated by the protein tyrosine phosphatases (PTPs) and protein tyrosine kinases. Several PTPs are implicated in the assembly and maintenance of cell adhesions, however, their signalling functions remain poorly defined. The PTPs can act by directly dephosphorylating adhesive complex components or function as scaffolds. In this review, we will focus on human PTPs and discuss their individual roles in major adhesion complexes, as well as Hippo signalling. We have collated PTP interactome and cell adhesome datasets, which reveal extensive connections between PTPs and cell adhesions that are relatively unexplored. Finally, we reflect on the dysregulation of PTPs and cell adhesions in disease.

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