scholarly journals Recruitment of the Protein-tyrosine Phosphatase SHP-2 to the C-terminal Tyrosine of the Prolactin Receptor and to the Adaptor Protein Gab2

2000 ◽  
Vol 275 (50) ◽  
pp. 39073-39080 ◽  
Author(s):  
Samir Ali ◽  
Suhad Ali
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Prolactin Receptor ◽  
Adaptor Protein ◽  
Protein Tyrosine

The zyxin-related protein TRIP6 interacts with PDZ motifs in the adaptor protein RIL and the protein tyrosine phosphatase PTP-BL

2000 ◽  
Vol 79 (4) ◽  
pp. 283-293 ◽  
Author(s):  
Edwin Cuppen ◽  
Marco van Ham ◽  
Derick G. Wansink ◽  
Anuradha de Leeuw ◽  
Bé Wieringa ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Adaptor Protein ◽  
Related Protein ◽  
Protein Tyrosine

scholarly journals Adaptor Protein GRB2 Promotes Src Tyrosine Kinase Activation and Podosomal Organization by Protein-tyrosine Phosphatase ϵ in Osteoclasts

2014 ◽  
Vol 289 (52) ◽  
pp. 36048-36058 ◽  
Author(s):  
Einat Levy-Apter ◽  
Eynat Finkelshtein ◽  
Vidyasiri Vemulapalli ◽  
Shawn S.-C. Li ◽  
Mark T. Bedford ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Adaptor Protein ◽  
Src Tyrosine Kinase ◽  
Kinase Activation ◽  
Protein Tyrosine

scholarly journals Regulation of interleukin-3-induced substrate phosphorylation and cell survival by SHP-2 (Src-homology protein tyrosine phosphatase 2)

2003 ◽  
Vol 376 (1) ◽  
pp. 147-157 ◽  
Author(s):  
Helen WHEADON ◽  
Christine EDMEAD ◽  
Melanie J. WELHAM
Keyword(s):  
Signal Transduction ◽  
Cell Survival ◽  
Tyrosine Phosphorylation ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Adaptor Protein ◽  
Functional Responses ◽  
Protein Tyrosine ◽  
Interleukin 3 ◽  
Src Homology

The cytosolic SHP-2 (Src homology protein tyrosine phosphatase 2) has previously been implicated in IL-3 (interleukin-3) signalling [Bone, Dechert, Jirik, Schrader and Welham (1997) J. Biol. Chem. 272, 14470 –14476; Craddock and Welham (1997) J. Biol. Chem. 272, 29281–29289; Welham, Dechert, Leslie, Jirik and Schrader (1994) J. Biol. Chem. 269, 23764–23768; Qu, Nguyen, Chen and Feng (2001) Blood 97, 911–914]. To investigate the role of SHP-2 in IL-3 signalling in greater detail, we have inducibly expressed WT (wild-type) or two potentially substrate-trapping mutant forms of SHP-2, generated by mutation of Asp-425 to Ala (D425A) or Cyst-459 to Ser (C459S), in IL-3-dependent BaF/3 cells. Effects on IL-3-induced tyrosine phosphorylation, signal transduction and functional responses were examined. Expression of C459S SHP-2 protected the β-chain of the murine IL-3R (IL-3 receptor), the adaptor protein Gab2 (Grb2-associated binder 2), and a cytosolic protein of 48 kDa from tyrosine dephosphorylation, consistent with them being bona fide substrates of SHP-2 in IL-3 signalling. The tyrosine phosphorylation of a 135 kDa transmembrane protein was also protected upon expression of C459S SHP-2. We have identified the inhibitory immunoreceptor PECAM-1 (platelet endothelial cell adhesion molecule-1)/CD31 (cluster determinant 31) as a component of this 135 kDa substrate and also show that IL-3 can induce tyrosine phosphorylation of PECAM-1. Expression of WT, C459S and D425A forms of SHP-2 had little effect on IL-3-driven proliferation or STAT5 (signal transduction and activators of transcription) phosphorylation or activation of protein kinase B. However, expression of WT SHP-2 increased ERK (extracellular-signal-regulated kinase) activation. Interestingly, expression of C459S SHP-2 decreased ERK activation at later times after IL-3 stimulation, but potentiated IL-3-induced activation of Jun N-terminal kinases. In addition, expression of C459S SHP-2 decreased cell survival in suboptimal IL-3 and upon IL-3 withdrawal. These findings indicate that SHP-2 plays an important role in mediating the anti-apoptotic effect of IL-3 and raises the possibility that PECAM-1 participates in the modulation of cytokine-induced signals.

scholarly journals CD150 Association with Either the SH2-Containing Inositol Phosphatase or the SH2-Containing Protein Tyrosine Phosphatase Is Regulated by the Adaptor Protein SH2D1A

2001 ◽  
Vol 166 (9) ◽  
pp. 5480-5487 ◽  
Author(s):  
Larysa M. Shlapatska ◽  
Svitlana V. Mikhalap ◽  
Anna G. Berdova ◽  
Oleksander M. Zelensky ◽  
Theodore J. Yun ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Adaptor Protein ◽  
Protein Tyrosine ◽  
Inositol Phosphatase

scholarly journals Interaction of the protein tyrosine phosphatase PTPL1 with the PtdIns(3,4)P2-binding adaptor protein TAPP1

2003 ◽  
Vol 376 (2) ◽  
pp. 525-535 ◽  
Author(s):  
Wendy A. KIMBER ◽  
Maria DEAK ◽  
Alan R. PRESCOTT ◽  
Dario R. ALESSI
Keyword(s):  
Plasma Membrane ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Pdz Domain ◽  
Adaptor Protein ◽  
Adaptor Proteins ◽  
Ph Domain ◽  
Hek 293 ◽  
Protein Tyrosine ◽  
Junction Protein

It has been postulated that PtdIns(3,4)P2, one of the immediate breakdown products of PtdIns(3,4,5)P3, functions as a signalling molecule in insulin- and growth-factor-stimulated pathways. To date, the tandem-PH-domain-containing protein-1 (TAPP1) and related TAPP2 are still the only known PH-domain-containing proteins that interact strongly and specifically with PtdIns(3,4)P2. In this study we demonstrate that endogenously expressed TAPP1, is constitutively associated with the protein-tyrosine-phosphatase-like protein-1 (PTPL1 also known as FAP-1). We show that PTPL1 binds to TAPP1 and TAPP2, principally though its first PDZ domain [where PDZ is postsynaptic density protein (PSD-95)/Drosophila disc large tumour suppressor (dlg)/tight junction protein (ZO1)] and show that this renders PTPL1 capable of associating with PtdIns(3,4)P2in vitro. Our data suggest that the binding of TAPP1 to PTPL1 does not influence PTPL1 phosphatase activity, but instead functions to maintain PTPL1 in the cytoplasm. Following stimulation of cells with hydrogen peroxide to induce PtdIns(3,4)P2 production, PTPL1, complexed to TAPP1, translocates to the plasma membrane. This study provides the first evidence that TAPP1 and PtdIns(3,4)P2 could function to regulate the membrane localization of PTPL1. We speculate that if PTPL1 was recruited to the plasma membrane by increasing levels of PtdIns(3,4)P2, it could trigger a negative feedback loop in which phosphoinositide-3-kinase-dependent or other signalling pathways could be switched off by the phosphatase-catalysed dephosphorylation of receptor tyrosine kinases or tyrosine phosphorylated adaptor proteins such as IRS1 or IRS2. Consistent with this notion we observed RNA-interference-mediated knock-down of TAPP1 in HEK-293 cells, enhanced activation and phosphorylation of PKB following IGF1 stimulation.

SHP-1 protein tyrosine phosphatase associates with the adaptor protein CrkL

2012 ◽  
Vol 40 (12) ◽  
pp. 1055-1059 ◽  
Author(s):  
Sevan Evren ◽  
Xue-Zhong Ma ◽  
Darinka Sakac ◽  
Donald R. Branch
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Adaptor Protein ◽  
Protein Tyrosine

1742-P: Targeting the Low Molecular Weight Protein Tyrosine Phosphatase for Obesity-Associated Diabetes Therapy

Diabetes ◽  
2020 ◽  
Vol 69 (Supplement 1) ◽  
pp. 1742-P
Author(s):  
STEPHANIE M. STANFORD ◽  
MICHAEL A. DIAZ ◽  
JIWEN J. ZOU ◽  
ROBERT J. ARDECKY ◽  
ANTHONY PINKERTON ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Low Molecular Weight ◽  
Molecular Weight Protein ◽  
Diabetes Therapy ◽  
Protein Tyrosine ◽  
Weight Protein ◽  
Low Molecular Weight Protein
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