Protein tyrosine phosphatase ζ/RPTPβ interacts with PSD-95/SAP90 family

Kawachi, Hiroyuki; Tamura, Hiroshi; Watakabe, Ikuko; Shintani, Takafumi; Maeda, Nobuaki; Noda, Masaharu

doi:10.1016/s0169-328x(99)00204-1

Cited by 50 publications

(38 citation statements)

References 49 publications

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“…In the case of RPTPβ such a signaling complex may consist of a mesh of several distinct scaffolding proteins including members of the MAGI and PSD95 families. Accordingly, it was shown that the MAGI-3-related S-SCAM/MAGI-2 interacts with PSD95 and β-catenin, two proteins that are found in a complex with RPTPβ (Dobrosotskaya and James, 2000;Kawachi et al, 1999). Our results suggest that the association of RPTPβ with MAGI-3 may allow the recruitment of p130 and additional substrates of this phosphatase.…”

Section: Discussionmentioning

confidence: 54%

Junctional protein MAGI-3 interacts with receptor tyrosine phosphataseβ (RPTPβ) and tyrosine-phosphorylated proteins

Adamsky

Arnold

Sabanay

et al. 2003

Journal of Cell Science

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Receptor protein tyrosine phosphatase β (RPTPβ) mediates cell-cell and cell-matrix interactions. By searching for intracellular proteins that interact with the cytoplasmic region of this phosphatase using the two-hybrid method, we identified several proteins containing PDZ domains. One of these proteins, MAGI-3, contains a guanylate-kinase-like region, six PDZ and two WW domains. The interaction between RPTPβ and MAGI-3 was confirmed by co-immunoprecipitation and pulldown experiments in transfected cells. Immunofluorescence and immunoelectron microscopy revealed that MAGI-3 is concentrated in specific sites at the plasma membrane and in the nucleus. In epithelial cells, MAGI-3 was localized with ZO-1 and cingulin at tight junctions, whereas in primary cultured astrocytes it was found in E-cadherin-based cell-cell contacts and in focal adhesion sites. Although MAGI-3 itself was not phosphorylated on tyrosine residues, it became associated with tyrosine-phosphorylated proteins following a short treatment of the cells with vanadate. In glioblastoma SF763T cells MAGI-3 was associated with a tyrosine-phosphorylated protein with the apparent molecular weight of 130 kDa, whereas in Caco2 cells it was associated with a 90 kDa protein. Finally, we show that p130 served as a substrate for RPTPβ and that its dephosphorylation required the C-terminal sequence of the phosphatase, which mediated the interaction with MAGI-3. These findings suggest a possible role for MAGI-3 as a scaffolding molecule that links receptor tyrosine phosphatase with its substrates at the plasma membrane.

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Section: Discussionmentioning

confidence: 54%

Junctional protein MAGI-3 interacts with receptor tyrosine phosphataseβ (RPTPβ) and tyrosine-phosphorylated proteins

Adamsky

Arnold

Sabanay

et al. 2003

Journal of Cell Science

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“…To date, little is known about the intracellular signaling of RPTPz. Recent studies revealed a potential interaction with members of the catenin family, PSD-90 family, sodium channel, and G-protein-coupled receptor kinase interactor (Kawachi et al, 1999(Kawachi et al, , 2001. With the goal of identifying and characterizing immunotherapeutic antibody targets, we focused our functional studies on the role of RPTPz and Ptn signaling.…”

Section: Discussionmentioning

confidence: 99%

A role for receptor tyrosine phosphataseζ in glioma cell migration

Müller¹,

Kunkel²,

et al. 2003

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“…Plasmid pBD-G␤1G␥13 was created by subcloning PCRamplified G␤1 and G␥13 DNAs into the vector pBridge (Clontech). pGAD424 plasmids containing various PDZ domains from PSD95 (pGAD424-PDZ1, pGAD424-PDZ2, pGAD424-PDZ3, pGAD424-PDZ12, pGAD424-PDZ23, and pGAD424-PDZ123;, see Table 1) were the kind gifts of Dr. M. Noda and have been described previously (21). The third PDZ domain of SAP97 was amplified by PCR and subcloned into pGADT7 (Clontech).…”

Section: Methodsmentioning

confidence: 99%

Gγ13 Interacts with PDZ Domain-containing Proteins

Benard

Margolskee

2006

Journal of Biological Chemistry

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The G protein ␥13 subunit (G␥13) is expressed in taste and retinal and neuronal tissues and plays a key role in taste transduction. We identified PSD95, Veli-2, and other PDZ domain-containing proteins as binding partners for G␥13 by yeast two-hybrid and pulldown assays. In two-hybrid assays, G␥13 interacted specifically with the third PDZ domain of PSD95, the sole PDZ domain of Veli-2, and the third PDZ domain of SAP97, a PSD95-related protein. G␥13 did not interact with the other PDZ domains of PSD95. Coexpression of G␥13 with its G␤1 partner did not interfere with these two-hybrid interactions. The physical interaction of G␥13 with PSD95 in the cellular milieu was confirmed in pull-down assays following heterologous expression in HEK293 cells. The interaction of G␥13 with the PDZ domain of PSD95 was via the C-terminal CAAX tail of G␥13 (where AA indicates the aliphatic amino acid); alanine substitution of the CTAL sequence at the C terminus of G␥13 abolished its interactions with PSD95 in twohybrid and pull-down assays. Veli-2 and SAP97 were identified in taste tissue and in G␥13-expressing taste cells. Coimmunoprecipitation of G␥13 and PSD95 from brain and of G␥13 and SAP97 from taste tissue indicates that G␥13 interacts with these proteins endogenously. This is the first demonstration that PDZ domain proteins interact with heterotrimeric G proteins via the CAAX tail of G␥ subunits. The interaction of G␥13 with PDZ domain-containing proteins may provide a means to target particular G␤␥ subunits to specific subcellular locations and/or macromolecular complexes involved in signaling pathways.A sophisticated and ordered protein network is essential to the proper functioning of cells. Precise assembly of individual components, through targeting and anchoring of proteins within designated subcellular compartments, ensures the integrity of these networks (1, 2). Specific protein-protein interactions are important for accomplishing this complex task. For example, PSD95 (postsynaptic density protein 95, also called SAP90), a member of the MAGUK (membrane-associated guanylate kinase) protein family (3), helps to assemble a complex postsynaptic protein network via its interactions with several different proteins. Some of these interactions rely on three PDZ domains (named after PSD95, Disc-large, and ZO-1) located in the N-terminal half of PSD95. PDZ domains function as protein-protein interaction modules and consist of about 90 amino acids (4 -6).PDZ domains typically bind to the extreme C terminus of a target protein in a sequence-specific manner. The PDZ domains of PSD95 recognize a canonical -X(S/T)XA motif (where X represents any amino acid and A represents an aliphatic amino acid). PDZ domains have been identified in proteins in bacteria, yeast, Drosophila, metazoans, and plants and comprise the most common protein module identified in the sequenced genome (4, 6). In addition to their affinity for C-terminal motifs, PDZ domains can also bind to internal sequences that mimic free C termini. Finally, PDZ domains c...

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Protein tyrosine phosphatase ζ/RPTPβ interacts with PSD-95/SAP90 family

Cited by 50 publications

References 49 publications

Junctional protein MAGI-3 interacts with receptor tyrosine phosphataseβ (RPTPβ) and tyrosine-phosphorylated proteins

Junctional protein MAGI-3 interacts with receptor tyrosine phosphataseβ (RPTPβ) and tyrosine-phosphorylated proteins

A role for receptor tyrosine phosphataseζ in glioma cell migration

Gγ13 Interacts with PDZ Domain-containing Proteins

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