Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding

1994 ◽  
Vol 14 (1) ◽  
pp. 1-9
Author(s):  
J Sap ◽  
Y P Jiang ◽  
D Friedlander ◽  
M Grumet ◽  
J Schlessinger
Keyword(s):  
Tyrosine Phosphatase ◽  
Extracellular Domain ◽  
Cell Contact ◽  
Intercellular Interaction ◽  
Homophilic Binding ◽  
Fibronectin Type Iii ◽  
Immunoglobulin Domain ◽  
Receptor Tyrosine Phosphatases ◽  
Receptor Tyrosine Phosphatase ◽  
Cellular Aggregates

Receptor tyrosine phosphatases (R-PTPases) feature PTPase domains in the context of a receptor-like transmembrane topology. The R-PTPase R-PTP-kappa displays an extracellular domain composed of fibronectin type III motifs, a single immunoglobulin domain, as well as a recently defined MAM domain (Y.-P. Jiang, H. Wang, P. D'Eustachio, J.M. Musacchio, J. Schlessinger, and J. Sap, Mol. Cell. Biol. 13:2942-2951, 1993). We report here that R-PTP-kappa can mediate homophilic intercellular interaction. Inducible expression of the R-PTP-kappa protein in heterologous cells results in formation of stable cellular aggregates strictly consisting of R-PTP-kappa-expressing cells. Moreover, the purified extracellular domain of R-PTP-kappa functions as a substrate for adhesion by cells expressing R-PTP-kappa and induces aggregation of coated synthetic beads. R-PTP-kappa-mediated intercellular adhesion does not require PTPase activity or posttranslational proteolytic cleavage of the R-PTP-kappa protein and is calcium independent. The results suggest that R-PTPases may provide a link between cell-cell contact and cellular signaling events involving tyrosine phosphorylation.

scholarly journals Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding.

1994 ◽  
Vol 14 (1) ◽  
pp. 1-9 ◽  
Author(s):  
J Sap ◽  
Y P Jiang ◽  
D Friedlander ◽  
M Grumet ◽  
J Schlessinger
Keyword(s):  
Tyrosine Phosphatase ◽  
Extracellular Domain ◽  
Cell Contact ◽  
Intercellular Interaction ◽  
Homophilic Binding ◽  
Fibronectin Type Iii ◽  
Immunoglobulin Domain ◽  
Receptor Tyrosine Phosphatases ◽  
Receptor Tyrosine Phosphatase ◽  
Cellular Aggregates

Receptor tyrosine phosphatases (R-PTPases) feature PTPase domains in the context of a receptor-like transmembrane topology. The R-PTPase R-PTP-kappa displays an extracellular domain composed of fibronectin type III motifs, a single immunoglobulin domain, as well as a recently defined MAM domain (Y.-P. Jiang, H. Wang, P. D'Eustachio, J.M. Musacchio, J. Schlessinger, and J. Sap, Mol. Cell. Biol. 13:2942-2951, 1993). We report here that R-PTP-kappa can mediate homophilic intercellular interaction. Inducible expression of the R-PTP-kappa protein in heterologous cells results in formation of stable cellular aggregates strictly consisting of R-PTP-kappa-expressing cells. Moreover, the purified extracellular domain of R-PTP-kappa functions as a substrate for adhesion by cells expressing R-PTP-kappa and induces aggregation of coated synthetic beads. R-PTP-kappa-mediated intercellular adhesion does not require PTPase activity or posttranslational proteolytic cleavage of the R-PTP-kappa protein and is calcium independent. The results suggest that R-PTPases may provide a link between cell-cell contact and cellular signaling events involving tyrosine phosphorylation.

scholarly journals Identification of a carbonic anhydrase-like domain in the extracellular region of RPTP gamma defines a new subfamily of receptor tyrosine phosphatases.

1993 ◽  
Vol 13 (3) ◽  
pp. 1497-1506 ◽  
Author(s):  
G Barnea ◽  
O Silvennoinen ◽  
B Shaanan ◽  
A M Honegger ◽  
P D Canoll ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Transmembrane Domain ◽  
Tyrosine Phosphatase ◽  
Extracellular Domain ◽  
Suppressor Gene ◽  
Tyrosine Phosphatases ◽  
Candidate Tumor Suppressor Gene ◽  
Extracellular Region ◽  
Receptor Tyrosine Phosphatases

The tyrosine phosphatase RPTP gamma is a candidate tumor suppressor gene since it is located on human chromosome 3p14.2-p21 in a region frequently deleted in certain types of renal and lung carcinomas. In order to evaluate its oncogenic potential and to explore its normal in vivo functions, we have isolated cDNAs and deduced the complete sequences of both human and murine RPTP gamma. The murine RPTP gamma gene has been localized to chromosome 14 to a region syntenic to the location of the human gene. Northern (RNA) blot analysis reveals the presence of two major transcripts of 5.5 and 8.5 kb in a variety of murine tissues. In situ hybridization analysis reveals that RPTP gamma mRNA is expressed in specific regions of the brain and that the localization of RPTP gamma changes during brain development. RPTP gamma is composed of a putative extracellular domain, a single transmembrane domain, and a cytoplasmic portion with two tandem catalytic tyrosine phosphatase domains. The extracellular domain contains a stretch of 266 amino acids with striking homology to the zinc-containing enzyme carbonic anhydrase (CAH), indicating that RPTP gamma and RPTP beta (HPTP zeta) represent a subfamily of receptor tyrosine phosphatases. We have constructed a model for the CAH-like domain of RPTP gamma based upon the crystal structure of CAH. It appears that 11 of the 19 residues that form the active site of CAH are conserved in RPTP gamma. Yet only one of the three His residues that ligate the zinc atom and are required for catalytic activity is conserved. On the basis of this model we propose that the CAH-like domain of RPTP gamma may have a function other than catalysis of hydration of metabolic CO2.

Teneurin 2 is expressed by the neurons of the thalamofugal visual system in situ and promotes homophilic cell-cell adhesion in vitro

Development ◽  
2002 ◽  
Vol 129 (20) ◽  
pp. 4697-4705
Author(s):  
Beatrix P. Rubin ◽  
Richard P. Tucker ◽  
Marianne Brown-Luedi ◽  
Doris Martin ◽  
Ruth Chiquet-Ehrismann
Keyword(s):  
Visual System ◽  
Neuroblastoma Cells ◽  
Cell Aggregation ◽  
Extracellular Domain ◽  
Cell Contact ◽  
Cortical Actin ◽  
Homophilic Binding ◽  
Transmembrane Glycoprotein ◽  
Cell Cell

The transmembrane glycoprotein teneurin 2 is expressed by neurons in the developing avian thalamofugal visual system at periods that correspond with target recognition and synaptogenesis. Partial and full-length teneurin 2 constructs were expressed in cell lines in vitro. Expression of the cytoplasmic domain is required for the induction of filopodia, the transport of teneurin 2 into neurites and the co-localization of teneurin 2 with the cortical actin cytoskeleton. In addition, expression of the extracellular domain of teneurin 2 by HT1080 cells induced cell aggregation, and the extracellular domain of teneurin 2 became concentrated at sites of cell-cell contact in neuroblastoma cells. These observations indicate that the homophilic binding of teneurin 2 may play a role in the development of specific neuronal circuits in the developing visual system.

scholarly journals Regulation of CNS and motor axon guidance in Drosophila by the receptor tyrosine phosphatase DPTP52F

Development ◽  
2001 ◽  
Vol 128 (21) ◽  
pp. 4371-4382 ◽  
Author(s):  
Benno Schindelholz ◽  
Matthias Knirr ◽  
Rahul Warrior ◽  
Kai Zinn
Keyword(s):  
Axon Guidance ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine Phosphatases ◽  
Genomic Analysis ◽  
Motor Axon ◽  
Phosphatase Domain ◽  
C Elegans ◽  
Fibronectin Type Iii ◽  
Motor Nerves ◽  
Receptor Tyrosine Phosphatase

Receptor-linked protein tyrosine phosphatases (RPTPs) regulate axon guidance and synaptogenesis in Drosophila embryos and larvae. We describe DPTP52F, the sixth RPTP to be discovered in Drosophila. Our genomic analysis indicates that there are likely to be no additional RPTPs encoded in the fly genome. Five of the six Drosophila RPTPs have C. elegans counterparts, and three of the six are also orthologous to human RPTP subfamilies. DPTP52F, however, has no clear orthologs in other organisms. The DPTP52F extracellular domain contains five fibronectin type III repeats and it has a single phosphatase domain. DPTP52F is selectively expressed in the CNS of late embryos, as are DPTP10D, DLAR, DPTP69D and DPTP99A. To define developmental roles of DPTP52F, we used RNA interference (RNAi)-induced phenotypes as a guide to identify Ptp52F alleles among a collection of EMS-induced lethal mutations. Ptp52F single mutant embryos have axon guidance phenotypes that affect CNS longitudinal tracts. This phenotype is suppressed in Dlar Ptp52F double mutants, indicating that DPTP52F and DLAR interact competitively in regulating CNS axon guidance decisions. Ptp52F single mutations also cause motor axon phenotypes that selectively affect the SNa nerve. DPTP52F, DPTP10D and DPTP69D have partially redundant roles in regulation of guidance decisions made by axons within the ISN and ISNb motor nerves.

Identification of a carbonic anhydrase-like domain in the extracellular region of RPTP gamma defines a new subfamily of receptor tyrosine phosphatases

1993 ◽  
Vol 13 (3) ◽  
pp. 1497-1506
Author(s):  
G Barnea ◽  
O Silvennoinen ◽  
B Shaanan ◽  
A M Honegger ◽  
P D Canoll ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Transmembrane Domain ◽  
Tyrosine Phosphatase ◽  
Extracellular Domain ◽  
Suppressor Gene ◽  
Tyrosine Phosphatases ◽  
Candidate Tumor Suppressor Gene ◽  
Extracellular Region ◽  
Receptor Tyrosine Phosphatases

The tyrosine phosphatase RPTP gamma is a candidate tumor suppressor gene since it is located on human chromosome 3p14.2-p21 in a region frequently deleted in certain types of renal and lung carcinomas. In order to evaluate its oncogenic potential and to explore its normal in vivo functions, we have isolated cDNAs and deduced the complete sequences of both human and murine RPTP gamma. The murine RPTP gamma gene has been localized to chromosome 14 to a region syntenic to the location of the human gene. Northern (RNA) blot analysis reveals the presence of two major transcripts of 5.5 and 8.5 kb in a variety of murine tissues. In situ hybridization analysis reveals that RPTP gamma mRNA is expressed in specific regions of the brain and that the localization of RPTP gamma changes during brain development. RPTP gamma is composed of a putative extracellular domain, a single transmembrane domain, and a cytoplasmic portion with two tandem catalytic tyrosine phosphatase domains. The extracellular domain contains a stretch of 266 amino acids with striking homology to the zinc-containing enzyme carbonic anhydrase (CAH), indicating that RPTP gamma and RPTP beta (HPTP zeta) represent a subfamily of receptor tyrosine phosphatases. We have constructed a model for the CAH-like domain of RPTP gamma based upon the crystal structure of CAH. It appears that 11 of the 19 residues that form the active site of CAH are conserved in RPTP gamma. Yet only one of the three His residues that ligate the zinc atom and are required for catalytic activity is conserved. On the basis of this model we propose that the CAH-like domain of RPTP gamma may have a function other than catalysis of hydration of metabolic CO2.

scholarly journals Homophilic binding of PTP mu, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation

1993 ◽  
Vol 122 (4) ◽  
pp. 961-972 ◽  
Author(s):  
SM Brady-Kalnay ◽  
AJ Flint ◽  
NK Tonks
Keyword(s):  
Fusion Protein ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Recombinant Baculovirus ◽  
Sf9 Cells ◽  
Homophilic Binding ◽  
Protein Tyrosine ◽  
Baculovirus Infection ◽  
Induced Aggregation ◽  
Cell Cell

The receptor-like protein tyrosine phosphatase, PTPmu, displays structural similarity to cell-cell adhesion molecules of the immunoglobulin superfamily. We have investigated the ability of human PTPmu to function in such a capacity. Expression of PTPmu, with or without the PTPase domains, by recombinant baculovirus infection of Sf9 cells induced their aggregation. However, neither a chimeric form of PTPmu, containing the extracellular and transmembrane segments of the EGF receptor and the intracellular segment of PTPmu, nor the intracellular segment of PTPmu expressed as a soluble protein induced aggregation. PTPmu mediates aggregation via a homophilic mechanism, as judged by lack of incorporation of uninfected Sf9 cells into aggregates of PTPmu-expressing cells. Homophilic binding has been demonstrated between PTPmu-coated fluorescent beads (Covaspheres) and endogenously expressed PTPmu on MvLu cells. Additionally the PTPmu-coated beads specifically bound to a bacterially expressed glutathione-S-transferase fusion protein containing the extracellular segment of PTPmu (GST/PTPmu) adsorbed to petri dishes. Covaspheres coated with the GST/PTPmu fusion protein aggregated in vitro and also bound to PTPmu expressed endogenously on MvLu cells. These results suggest that the ligand for this transmembrane PTPase is another PTPmu molecule on an adjacent cell. Thus homophilic binding interactions may be an important component of the function of PTPmu in vivo.

Receptor tyrosine phosphatase sigma (RPTPσ) regulates, p250GAP, a novel substrate that attenuates Rac signaling

2010 ◽  
Vol 22 (11) ◽  
pp. 1626-1633 ◽  
Author(s):  
Mélanie J. Chagnon ◽  
Chia-Lun Wu ◽  
Takanobu Nakazawa ◽  
Tadashi Yamamoto ◽  
Masaharu Noda ◽  
...  
Keyword(s):  
Tyrosine Phosphatase ◽  
Receptor Tyrosine Phosphatase
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