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.

Several adaptor proteins promote intracellular localisation of the transporter MRP4/ABCC4 in platelets and haematopoietic cells

2017 ◽  
Vol 117 (01) ◽  
pp. 105-115 ◽  
Author(s):  
Yvonne Schaletzki ◽  
Marie-Luise Kromrey ◽  
Susanne Bröderdorf ◽  
Elke Hammer ◽  
Markus Grube ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Protein Interactions ◽  
Pdz Domain ◽  
Adaptor Protein ◽  
Adaptor Proteins ◽  
Apical Plasma Membrane ◽  
Dense Granules ◽  
Haematopoietic Cells ◽  
And Function

SummaryThe multidrug resistance protein 4 (MRP4/ABCC4) has been identified as an important transporter for signalling molecules including cyclic nucleotides and several lipid mediators in platelets and may thus represent a novel target to interfere with platelet function. Besides its localisation in the plasma membrane, MRP4 has been also detected in the membrane of dense granules in resting platelets. In polarised cells it is localised at the basolateral or apical plasma membrane. To date, the mechanism of MRP4 trafficking has not been elucidated; protein interactions may regulate both the localisation and function of this transporter. We approached this issue by searching for interacting proteins by in vitro binding assays, followed by immunoblotting and mass spectrometry, and by visualising their co-localisation in platelets and haematopoietic cells. We identified the PDZ domain containing scaffold proteins ezrin-binding protein 50 (EBP50/NHERF1), postsynaptic density protein 95 (PSD95), and sorting nexin 27 (SNX27), but also the adaptor protein complex 3 subunit β3A (AP3B1) and the heat shock protein HSP90 as putative interaction partners of MRP4. The knockdown of SNX27, PSD95, and AP3B1 by siRNA in megakaryoblastic leuk aemia cells led to a redistribution of MRP4 from intracellular structures to the plasma membrane. Inhibition of HSP90 led to a diminished expression and retention of MRP4 in the endoplasmic reticulum. These results indicate that MRP4 localisation and function are regulated by multiple protein interactions. Changes in the adaptor proteins can hence lead to altered localisation and function of the transporter.Supplementary Material to this article is available at www.thrombosis-online.com.

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 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

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 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 Receptor Type Protein Tyrosine Phosphatase ζ-Pleiotrophin Signaling Controls Endocytic Trafficking of DNER That Regulates Neuritogenesis

2008 ◽  
Vol 28 (14) ◽  
pp. 4494-4506 ◽  
Author(s):  
Nobuna Fukazawa ◽  
Seisuke Yokoyama ◽  
Mototsugu Eiraku ◽  
Mineko Kengaku ◽  
Nobuaki Maeda
Keyword(s):  
Plasma Membrane ◽  
Tyrosine Phosphorylation ◽  
Purkinje Cells ◽  
Protein Tyrosine Phosphatase ◽  
Transmembrane Protein ◽  
Tyrosine Phosphatase ◽  
Receptor Type ◽  
Protein Tyrosine ◽  
Tyrosine Residues ◽  
Type Protein

ABSTRACT Protein tyrosine phosphatase ζ (PTPζ) is a receptor type protein tyrosine phosphatase that uses pleiotrophin as a ligand. Pleiotrophin inactivates the phosphatase activity of PTPζ, resulting in the increase of tyrosine phosphorylation levels of its substrates. We studied the functional interaction between PTPζ and DNER, a Notch-related transmembrane protein highly expressed in cerebellar Purkinje cells. PTPζ and DNER displayed patchy colocalization in the dendrites of Purkinje cells, and immunoprecipitation experiments indicated that these proteins formed complexes. Several tyrosine residues in and adjacent to the tyrosine-based and the second C-terminal sorting motifs of DNER were phosphorylated and were dephosphorylated by PTPζ, and phosphorylation of these tyrosine residues resulted in the accumulation of DNER on the plasma membrane. DNER mutants lacking sorting motifs accumulated on the plasma membrane of Purkinje cells and Neuro-2A cells and induced their process extension. While normal DNER was actively endocytosed and inhibited the retinoic-acid-induced neurite outgrowth of Neuro-2A cells, pleiotrophin stimulation increased the tyrosine phosphorylation level of DNER and suppressed the endocytosis of this protein, which led to the reversal of this inhibition, thus allowing neurite extension. These observations suggest that pleiotrophin-PTPζ signaling controls subcellular localization of DNER and thereby regulates neuritogenesis.

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