Protein Tyrosine Phosphatases Involved in Lymphocyte Signal Transduction

2015 ◽  
pp. 40-61 ◽  
Author(s):  
Ellen Cahir McFarland ◽  
Edwin Flores ◽  
R. James Matthews ◽  
Matthew L. Thomas
Keyword(s):  
Signal Transduction ◽  
Protein Tyrosine Phosphatases ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine

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.

249 Leishmania promastigotes modulate macrophage signal transduction by targeting host protein tyrosine phosphatases in a GP63-dependent manner

Cytokine ◽  
2008 ◽  
Vol 43 (3) ◽  
pp. 298-299
Author(s):  
Maria Adelaida Gomez ◽  
Irazu Contreras ◽  
Laleh Alisaraie ◽  
Maxime Halle ◽  
Michel L. Tremblay ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Protein Tyrosine Phosphatases ◽  
Host Protein ◽  
Dependent Manner ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine ◽  
Leishmania Promastigotes

scholarly journals Inactivation of Protein-tyrosine Phosphatases as Mechanism of UV-induced Signal Transduction

1999 ◽  
Vol 274 (37) ◽  
pp. 26378-26386 ◽  
Author(s):  
Steffen Groß ◽  
Axel Knebel ◽  
Tencho Tenev ◽  
Armin Neininger ◽  
Matthias Gaestel ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Protein Tyrosine Phosphatases ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine ◽  
Induced Signal
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