Cloning, expression and chromosomal localization of a new putative receptor‐like protein tyrosine phosphatase

Gebbink, Martijn F.B.G.; Etten, Ingrid van; Hateboer, G.; Suijkerbuijk, Ron F.; Beijersbergen, Roderick L.; Kessell, Ad Geurts van; Moolenaar, Wouter H.

doi:10.1016/0014-5793(91)81241-y

Cited by 131 publications

(126 citation statements)

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“…Among them, type II RPTPs are characterized by the presence of varying numbers of immunoglobulin (Ig)-like and fibronectin type III repeat (FN-III)-like domains in the extracellular regions and include LAR [9,10], PTP6 [11,12], PTPx [13], PTP/t [14], PTPa (NE-3) [15,16] and Drosophila DPTP [10]. Since these structural motifs are also utilized by cell adhesion molecules such as the neural cell adhesion molecule (N-CAM), it has been postulated that type II RPTPs might be involved in cell adhesion.…”

Section: Introductionmentioning

confidence: 99%

Developmental regulation of gene expression for the MPTPδ isoforms in the central nervous system and the immune system

Mizuno¹,

Hasegawa²,

Ogimoto³

et al. 1994

FEBS Letters

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MPTP6 is a murine transmembrane protein tyrosine phosphatase which has three isoforms, types A-C, differing in the structure of the extracellular regions. In this study, we examined MPTP~ isoform expression in the brain and the immune system at discrete developmental or differentiation stages. RT-PCR analysis demonstrated that another isoform, type D, is transcribed from the MPTP~ gene. In\the brain, only type D was expressed until postnatal day 7 (P7), but after P14, all four isoforms were detected. In contrast, the spleen, thymus and all the hematopoietic cell lines examined express only types B and C isoforms. An in situ hybridization study showed that MPTP6 mRNA is diffusely expressed throughout the spleen, but its expression in the thymus is restricted to the medullary region.

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Section: Introductionmentioning

confidence: 99%

Developmental regulation of gene expression for the MPTPδ isoforms in the central nervous system and the immune system

Mizuno¹,

Hasegawa²,

Ogimoto³

et al. 1994

FEBS Letters

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“…The receptor protein-tyrosine phosphatase PTP is a member of the Ig superfamily of adhesion molecules. The extracellular segment of PTP contains a MAM ( (Meprin/A5/PTP ) domain, an Ig domain, and four fibronectin type III repeats (3). Expression of PTP induces aggregation of non-adherent cells (4,5) through a homophilic binding site that resides within the Ig domain (6).…”

mentioning

confidence: 99%

Expression of the Receptor Protein-tyrosine Phosphatase, PTPμ, Restores E-cadherin-dependent Adhesion in Human Prostate Carcinoma Cells

Hellberg¹,

Burden-Gulley

Pietz

et al. 2002

Journal of Biological Chemistry

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Normal prostate expresses the receptor protein-tyrosine phosphatase, PTP, whereas LNCaP prostate carcinoma cells do not. PTP has been shown previously to interact with the E-cadherin complex. LNCaP cells express normal levels of E-cadherin and catenins but do not mediate either PTP-or E-cadherin-dependent adhesion. Re-expression of PTP restored cell adhesion to PTP and to E-cadherin. A mutant form of PTP that is catalytically inactive was re-expressed, and it also restored adhesion to PTP and to E-cadherin. Expression of PTP-extra (which lacks most of the cytoplasmic domain) induced adhesion to PTP but not to E-cadherin, demonstrating a requirement for the presence of the intracellular domains of PTP to restore E-cadherinmediated adhesion. We previously observed a direct interaction between the intracellular domain of PTP and RACK1, a receptor for activated protein kinase C (PKC). We demonstrate that RACK1 binds to both the catalytically active and inactive mutant form of PTP. In addition, we determined that RACK1 binds to the PKC␦ isoform in LNCaP cells. We tested whether PKC could be playing a role in the ability of PTP to restore E-cadherin-dependent adhesion. Activation of PKC reversed the adhesion of PTPWT-expressing cells to E-cadherin, whereas treatment of parental LNCaP cells with a PKC␦-specific inhibitor induced adhesion to E-cadherin. Together, these studies suggest that PTP regulates the PKC pathway to restore E-cadherin-dependent adhesion via its interaction with RACK1.A diverse set of cellular behaviors including growth, differentiation, adhesion, and migration are regulated by protein tyrosine phosphorylation. Protein tyrosine kinases and proteintyrosine phosphatases (PTPs) 1 regulate intracellular phosphotyrosine levels. A subfamily of receptor-like PTPs (RPTPs) has extracellular segments containing adhesion molecule-like domains and intracellular segments that possess tyrosine phosphatase activity (1, 2). This structural arrangement suggests that RPTPs directly send signals in response to cell adhesion. The receptor protein-tyrosine phosphatase PTP is a member of the Ig superfamily of adhesion molecules. The extracellular segment of PTP contains a MAM ( (Meprin/A5/PTP ) domain, an Ig domain, and four fibronectin type III repeats (3). Expression of PTP induces aggregation of non-adherent cells (4, 5) through a homophilic binding site that resides within the Ig domain (6). The MAM domain plays a role in cell-cell aggregation by determining the specificity of the adhesive interaction (7). PTP contains a single membrane-spanning region with two cytoplasmic PTP domains. Only the membrane proximal PTP domain has catalytic activity (8). The role of the membrane distal PTP domain is not known, but this domain has been implicated in directing protein-protein interactions in other RPTPs (reviewed in Ref.2). The intracellular juxtamembrane domain of PTP contains a region that is homologous to the conserved intracellular domain of the cadherins (9

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“…Another subfamily that includes HPTPp (Gebbink et al, 1991), HPTPK (Jiang et al, 1993) and leukocyte common antigen-related (LAR; Streuli et al, 1988) bear Ig-like and FNIII elements in their extracellular domains which are characteristic of cell-adhesion molecules (CAM). Recent insights into the function of CAM motifs in these PTPases may indicate mechanisms by which they could impact upon developmental processes.…”

mentioning

confidence: 99%

Molecular Cloning and Tissue‐Specific RNA Processing of a Murine Receptor‐Type Protein Tyrosine Phosphatase

Wagner

Boerboom

Tremblay

1994

European Journal of Biochemistry

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The molecular cloning of a murine receptor-type protein tyrosine phosphatase, termed PTP NU-3, with an extracellular cell-adhesion-molecule-like domain is reported. NU-3 was isolated from 11.5-day total mouse embryonic RNA by reverse-transcriptase PCR using degenerate oligonucleotides flanking the conserved protein tyrosine phosphatase catalytic domain. This produced a 280-bp DNA probe which was subsequently employed to screen a mouse embryonic kidney library. Several overlapping cDNA clones were isolated, collectively forming a cDNA of 6.0 kb that encodes a putative 211 -kDa protein. Northern-blot analysis of total RNA from adult and embryonic mouse tissues indicates the existence of two major PTP NU-3 transcripts of approximately 6 kb and 7 kb. Both messages are expressed predominantly in brain tissues and neuronal-derived cell lines, although detectable levels of the 7-kb message were found in other non-neuronal tissues. We have identified a unique 132-bp exon segment that is present in the 7-kb message but is completely absent in the 6-kb transcript, suggesting tissue-specific levels of expression and RNA processing. Analysis of the amino acid sequence encoded by the 132-bp segment reveals that it completes a partial fibronectin type-I11 element resulting in a protein with a total of nine such elements. Bacterial expression of the two catalytic domains demonstrated that only the first domain possesses enzymic activity towards a tyrosine phosphorylated substrate.The location, extent and timing of protein phosphorylation at tyrosine residues have been shown to be key processes in events such as cell homeostasis, growth and proliferation. This is evidenced by the identification of multiple oncogenes encoding protein tyrosine kinases (PTKs) and the correlation of an oncogenic state with tyrosine phosphorylation of specific proteins. Therefore, much attention is now focussed on enzymes which perform the reverse reaction, namely protein tyrosine phosphatase (PTPases; for a recent review, see Mourey and Dixon, 1994). Cloning efforts by many groups have led to the identification of two major classes of PTPases. The first class is specific to phosphorylated tyrosine residues and a second class, known as the VH1-type PTPases, can dephosphorylate phosphorylated tyrosine as well as serine and threonine residues. The former can be further subdivided into two major groups; the intracellular and the receptor-like enzymes. Intracellular PTPases are generally small proteins containing one highly conserved catalytic domain, whereas the receptor-type enzymes usually

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Cloning, expression and chromosomal localization of a new putative receptor‐like protein tyrosine phosphatase

Cited by 131 publications

References 51 publications

Developmental regulation of gene expression for the MPTPδ isoforms in the central nervous system and the immune system

Developmental regulation of gene expression for the MPTPδ isoforms in the central nervous system and the immune system

Expression of the Receptor Protein-tyrosine Phosphatase, PTPμ, Restores E-cadherin-dependent Adhesion in Human Prostate Carcinoma Cells

Molecular Cloning and Tissue‐Specific RNA Processing of a Murine Receptor‐Type Protein Tyrosine Phosphatase

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