Receptor protein tyrosine phosphatase μ: measuring where to stick

2008 ◽  
Vol 36 (2) ◽  
pp. 167-172 ◽  
Author(s):  
A. Radu Aricescu ◽  
Christian Siebold ◽  
E. Yvonne Jones
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Cell Surface Receptor ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Phosphatase ◽  
Extracellular Region ◽  
Fibronectin Type Iii ◽  
Surface Receptor ◽  
And Function

We review here recent results on the structure and function of a receptor protein tyrosine phosphatase, RPTPμ. In addition to their intercellular catalytic domains which bear the phosphatase activity, the RPTPs are cell-surface-receptor-type molecules and in many cases have large extracellular regions. What role can these extracellular regions play in function? For RPTPμ, the extracellular region is known to mediate homophilic adhesion. Sequence analysis indicates that it comprises six domains: an N-terminal MAM (meprin/A5/μ), one immunoglobulin-like domain and four fibronectin type III (FN) repeats. We have determined the crystal structure of the entire extracellular region for RPTPμ in the form of a functional adhesion dimer. The physical characteristics and dimensions of the adhesion dimer suggest a mechanism by which the location of this phosphatase can be influenced by cell–cell spacings.

scholarly journals The Cell-Specific Phenotype of the Polymorphic vacA Midregion Is Independent of the Appearance of the Cell Surface Receptor Protein Tyrosine Phosphatase β

2006 ◽  
Vol 74 (1) ◽  
pp. 49-55 ◽  
Author(s):  
David A. G. Skibinski ◽  
Christophe Genisset ◽  
Silvia Barone ◽  
John L. Telford
Keyword(s):  
Cell Surface ◽  
Cell Lines ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Cell Surface Receptor ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Amino Acid Region ◽  
Receptor Protein Tyrosine Phosphatase ◽  
Surface Receptor

ABSTRACT There are two alleles, m1 and m2, of the midregion of the vacuolating cytotoxin gene (vacA) of Helicobacter pylori which code for toxins with different cell specificities. Here we describe the construction of five chimeric strains in which regions of vacA were exchanged between the two genotypes. By analyzing the toxicity of these strains for HeLa and RK13 cells we have confirmed that a 148-amino-acid region determines the phenotypic differences between the two forms of the protein and that this entire region is important for cytotoxicity. Furthermore, we have used our chimeric strains to investigate whether variations in the midregion of VacA have an effect on phorbol 12-myristate 13-acetate (PMA)-induced VacA sensitivity in HL-60 cells. The PMA-induced VacA sensitivity of HL-60 cells has been previously associated with the appearance of the cell surface receptor protein tyrosine phosphatase beta (RPTPβ). Our data indicate that both the m1 and m2 forms of VacA are able to utilize RPTPβ, and the cell-specific phenotype of the midregion is independent of the presence of RPTPβ. It appears that another as-yet-unidentified receptor exists in HL-60 cells that accounts for the m2 phenotype in this cell line. Also, by studying the effect of PMA on levels of RPTPβ in other cell lines and toxicity of VacA in these cell lines we have shown that RPTPβ does not play a major role in the vacuolation of HeLa cells.

scholarly journals Cloning and characterization of R-PTP-kappa, a new member of the receptor protein tyrosine phosphatase family with a proteolytically cleaved cellular adhesion molecule-like extracellular region.

1993 ◽  
Vol 13 (5) ◽  
pp. 2942-2951 ◽  
Author(s):  
Y P Jiang ◽  
H Wang ◽  
P D'Eustachio ◽  
J M Musacchio ◽  
J Schlessinger ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Precursor Protein ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Type Iii ◽  
Receptor Protein Tyrosine Phosphatase ◽  
Fibronectin Type Iii ◽  
Fibronectin Type

We describe a new member of the receptor protein tyrosine phosphatase family, R-PTP-kappa, cDNA cloning predicts that R-PTP-kappa is synthesized from a precursor protein of 1,457 amino acids. Its intracellular domain displays the classical tandemly repeated protein tyrosine phosphatase homology, separated from the transmembrane segment by an uncharacteristically large juxta-membrane region. The extracellular domain of the R-PTP-kappa precursor protein contains an immunoglobulin-like domain and four fibronectin type III-like repeats, preceded by a signal peptide and a region of about 150 amino acids with similarity to the Xenopus A5 antigen, a putative neuronal recognition molecule (S. Takagi, T. Hsrata, K. Agata, M. Mochii, G. Eguchi, and H. Fujisawa, Neuron 7:295-307, 1991). Antibodies directed against the intra- and extracellular domains reveal that the R-PTP-kappa precursor protein undergoes proteolytic processing, following which both cleavage products remain associated. By site-directed mutagenesis, the likely cleavage site was shown to be a consensus sequence for cleavage by the processing endopeptidase furin, located in the fourth fibronectin type III-like repeat. In situ hybridization analysis indicates that expression of R-PTP-kappa in the central nervous system is developmentally regulated, with highest expression seen in actively developing areas and, in the adult, in areas capable of developmental plasticity such as the hippocampal formation and cerebral cortex. The mouse R-PTP-kappa gene maps to chromosome 10, at approximately 21 centimorgans from the centromere.

Cloning and characterization of R-PTP-kappa, a new member of the receptor protein tyrosine phosphatase family with a proteolytically cleaved cellular adhesion molecule-like extracellular region

1993 ◽  
Vol 13 (5) ◽  
pp. 2942-2951
Author(s):  
Y P Jiang ◽  
H Wang ◽  
P D'Eustachio ◽  
J M Musacchio ◽  
J Schlessinger ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Precursor Protein ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Type Iii ◽  
Receptor Protein Tyrosine Phosphatase ◽  
Fibronectin Type Iii ◽  
Fibronectin Type

We describe a new member of the receptor protein tyrosine phosphatase family, R-PTP-kappa, cDNA cloning predicts that R-PTP-kappa is synthesized from a precursor protein of 1,457 amino acids. Its intracellular domain displays the classical tandemly repeated protein tyrosine phosphatase homology, separated from the transmembrane segment by an uncharacteristically large juxta-membrane region. The extracellular domain of the R-PTP-kappa precursor protein contains an immunoglobulin-like domain and four fibronectin type III-like repeats, preceded by a signal peptide and a region of about 150 amino acids with similarity to the Xenopus A5 antigen, a putative neuronal recognition molecule (S. Takagi, T. Hsrata, K. Agata, M. Mochii, G. Eguchi, and H. Fujisawa, Neuron 7:295-307, 1991). Antibodies directed against the intra- and extracellular domains reveal that the R-PTP-kappa precursor protein undergoes proteolytic processing, following which both cleavage products remain associated. By site-directed mutagenesis, the likely cleavage site was shown to be a consensus sequence for cleavage by the processing endopeptidase furin, located in the fourth fibronectin type III-like repeat. In situ hybridization analysis indicates that expression of R-PTP-kappa in the central nervous system is developmentally regulated, with highest expression seen in actively developing areas and, in the adult, in areas capable of developmental plasticity such as the hippocampal formation and cerebral cortex. The mouse R-PTP-kappa gene maps to chromosome 10, at approximately 21 centimorgans from the centromere.

scholarly journals Expression and Function of the Receptor Protein Tyrosine Phosphatase ζ and Its Ligand Pleiotrophin in Human Astrocytomas

2003 ◽  
Vol 62 (12) ◽  
pp. 1265-1275 ◽  
Author(s):  
Ulrike Ulbricht ◽  
Marc A. Brockmann ◽  
Achim Aigner ◽  
Carmen Eckerich ◽  
Sabine Müller ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Phosphatase ◽  
And Function ◽  
Human Astrocytomas

scholarly journals The receptor protein tyrosine phosphatase (RPTP)β/ζ is expressed in different subtypes of human breast cancer

2007 ◽  
Vol 362 (1) ◽  
pp. 5-10 ◽  
Author(s):  
Pablo Perez-Pinera ◽  
Olivia Garcia-Suarez ◽  
Primitiva Menendez-Rodriguez ◽  
J. Mortimer ◽  
Y. Chang ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Protein Tyrosine Phosphatase ◽  
Human Breast Cancer ◽  
Tyrosine Phosphatase ◽  
Receptor Protein ◽  
Human Breast ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Phosphatase

scholarly journals The receptor protein tyrosine phosphatase PTPRJ negatively modulates the CD98hc oncoprotein in lung cancer cells

Oncotarget ◽  
2018 ◽  
Vol 9 (34) ◽  
pp. 23334-23348 ◽  
Author(s):  
Sabrina D’Agostino ◽  
Delia Lanzillotta ◽  
Mariaconcetta Varano ◽  
Cirino Botta ◽  
Antonio Baldrini ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Cancer Cells ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Lung Cancer Cells ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Phosphatase
Sign in / Sign up

Export Citation Format

Share Document