Peptide binding studies of GST and 6His-cmyc tagged forms of the Fas binding PDZ domain of the protein tyrosine phosphatase FAP-1

2000 ◽  
Vol 28 (5) ◽  
pp. A429-A429
Author(s):  
H. R. Have ◽  
D. P. Blowers ◽  
I. P. Hampton ◽  
I. W. Taylor ◽  
C. Grundy ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Pdz Domain ◽  
Peptide Binding ◽  
Binding Studies ◽  
Protein Tyrosine

scholarly journals ZRP-1, a Zyxin-related Protein, Interacts with the Second PDZ Domain of the Cytosolic Protein Tyrosine Phosphatase hPTP1E

1999 ◽  
Vol 274 (29) ◽  
pp. 20679-20687 ◽  
Author(s):  
Kishore K. Murthy ◽  
Kristopher Clark ◽  
Yves Fortin ◽  
Shi-Hsiang Shen ◽  
Denis Banville
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Pdz Domain ◽  
Related Protein ◽  
Protein Tyrosine ◽  
Cytosolic Protein

scholarly journals Association of protein-tyrosine phosphatase PTP-BAS with the transcription-factor-inhibitory protein IκBα through interaction between the PDZ1 domain and ankyrin repeats

1999 ◽  
Vol 337 (2) ◽  
pp. 179-184 ◽  
Author(s):  
Kazuhiko MAEKAWA ◽  
Noriko IMAGAWA ◽  
Akira NAITO ◽  
Shigenori HARADA ◽  
Osamu YOSHIE ◽  
...  
Keyword(s):  
Tyrosine Phosphorylation ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Pdz Domain ◽  
Dominant Negative ◽  
Ankyrin Repeats ◽  
Inhibitory Protein ◽  
Protein Tyrosine ◽  
Homology Region ◽  
High Oxidative Stress

PTP-BAS is a membrane-associated protein tyrosine phosphatase containing a band-4.1 homology region and five PDZ (PSD-95 Dlg ZO-1) [discs-large homology region (‘DHR’)/Gly-Leu-Gly-Phe (‘GLGF’)] domains. The second and fourth PDZ domains were reported to associate with Fas/CD95. By using the first PDZ domain as a bait in yeast two-hybrid screening, we have identified IκBα as a binding protein. IκBα associated with PDZ1 through the stretch of the N-terminal three ankyrin repeats. The association was also confirmed in HeLa cells by co-immunoprecipitation experiments. Inhibition of PTP-BAS by expression of dominant-negative PTP-BAS mutant resulted in tyrosine-phosphorylation of IκBα. Tyrosine-phosphorylation of IκBα is a key event in activation of nuclear factor (NF)-κB during reoxygenation. PTP-BAS may thus play a regulatory role in activation of NF-κB under high oxidative stress.

scholarly journals Protein tyrosine phosphatase H1 is a target of the E6 oncoprotein of high-risk genital human papillomaviruses

2007 ◽  
Vol 88 (11) ◽  
pp. 2956-2965 ◽  
Author(s):  
Stephanie Töpffer ◽  
Andreas Müller-Schiffmann ◽  
Konstantin Matentzoglu ◽  
Martin Scheffner ◽  
Gertrud Steger
Keyword(s):  
High Risk ◽  
Cervical Carcinoma ◽  
Protein Tyrosine Phosphatase ◽  
Carcinoma Cell ◽  
Tyrosine Phosphatase ◽  
Pdz Domain ◽  
Human Papillomaviruses ◽  
Binding Motif ◽  
Protein Tyrosine ◽  
Pdz Domain Proteins

The E6 proteins of high-risk genital human papillomaviruses (HPV), such as HPV types 16 and 18, possess a conserved C-terminal PDZ-binding motif, which mediates interaction with some cellular PDZ domain proteins. The binding of E6 usually results in their ubiquitin-mediated degradation. The ability of E6 to bind to PDZ domain proteins correlates with the oncogenic potential. Using a yeast two-hybrid system, GST pull-down experiments and coimmunoprecipitations, we identified the protein tyrosine phosphatase H1 (PTPH1/PTPN3) as a novel target of the PDZ-binding motif of E6 of HPV16 and 18. PTPH1 has been suggested to function as tumour suppressor protein, since mutational analysis revealed somatic mutations in PTPH1 in a minor fraction of various human tumours. We show here that HPV16 E6 accelerated the proteasome-mediated degradation of PTPH1, which required the binding of E6 to the cellular ubiquitin ligase E6-AP and to PTPH1. The endogenous levels of PTPH1 were particularly low in HPV-positive cervical carcinoma cell lines. The reintroduction of the E2 protein into the HPV16-positive cervical carcinoma cell line SiHa, known to lead to a sharp repression of E6 expression and to induce growth suppression, resulted in an increase of the amount of PTPH1. Our data suggest that reducing the level of PTPH1 may contribute to the oncogenic activity of high-risk genital E6 proteins.

scholarly journals Receptor protein tyrosine phosphatase PTPmu associates with cadherins and catenins in vivo.

1995 ◽  
Vol 130 (4) ◽  
pp. 977-986 ◽  
Author(s):  
S M Brady-Kalnay ◽  
D L Rimm ◽  
N K Tonks
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Receptor Protein ◽  
Immunocytochemical Staining ◽  
Beta Catenin ◽  
Binding Studies ◽  
Intracellular Domain ◽  
Protein Tyrosine ◽  
Immunoglobulin Domain

The extracellular segment of the receptor-type type protein tyrosine phosphatase PTPmu, possesses an MAM domain, an immunoglobulin domain, and four fibronectin type-III repeats. It binds homophilically, i.e., PTPmu on the surface of one cell binds to PTPmu on an apposing cell, and the binding site lies within the immunoglobulin domain. The intracellular segment of PTPmu has two PTP domains and a juxtamembrane segment that is homologous to the conserved intracellular domain of the cadherins. In cadherins, this segment interacts with proteins termed catenins to mediate association with the actin cytoskeleton. In this article, we demonstrate that PTPmu associates with a complex containing cadherins, alpha- and beta-catenin in mink lung (MvLu) cells, and in rat heart, lung, and brain tissues. Greater than 80% of the cadherin in the cell is cleared from Triton X-100 lysates of MvLu cells after immunoprecipitation with antibodies to PTPmu; however, the complex is dissociated when lysates are prepared in more stringent, SDS-containing RIPA buffer. In vitro binding studies demonstrated that the intracellular segment of PTPmu binds directly to the intracellular domain of E-cadherin, but not to alpha- or beta-catenin. Consistent with their ability to interact in vivo, PTPmu, cadherins, and catenins all localized to points of cell-cell contact in MvLu cells, as assessed by immunocytochemical staining. After pervanadate treatment of MvLu cells, which inhibits cellular tyrosine phosphatase activity including PTPmu, the cadherins associated with PTPmu are now found in a tyrosine-phosphorylated form, indicating that the cadherins may be an endogenous substrate for PTPmu. These data suggest that PTPmu may be one of the enzymes that regulates the dynamic tyrosine phosphorylation, and thus function, of the cadherin/catenin complex in vivo.

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.

scholarly journals A Novel GTPase-activating Protein for Rho Interacts with a PDZ Domain of the Protein-tyrosine Phosphatase PTPL1

1997 ◽  
Vol 272 (39) ◽  
pp. 24333-24338 ◽  
Author(s):  
Jan Saras ◽  
Petra Franzén ◽  
Pontus Aspenström ◽  
Ulf Hellman ◽  
Leonel Jorge Gonez ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Pdz Domain ◽  
Gtpase Activating Protein ◽  
Protein Tyrosine
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