A novel receptor-type protein tyrosine phosphatase is expressed during neurogenesis in the olfactory neuroepithelium

Walton, Kenneth G.; Martell, Karen J.; Kwak, Seung; Dixon, Jack E.; Largent, Brian L.

doi:10.1016/0896-6273(93)90193-u

Cited by 75 publications

(49 citation statements)

References 74 publications

(47 reference statements)

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“…In particular, we have shown by chemical cross-linking that the ␣-latrotoxin/PTP complexes can form in brain membranes at a low physiologically relevant concentration of ␣-latrotoxin. Northern blotting data obtained by other groups indicate that the highest concentration of PTP is found in brain tissues (24,25,44), which is also compatible with its proposed role as a functional ␣-latrotoxin receptor.…”

Section: Figsupporting

confidence: 66%

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Protein-tyrosine Phosphatase-ς Is a Novel Member of the Functional Family of α-Latrotoxin Receptors

Krasnoperov

Bittner

et al. 2002

Journal of Biological Chemistry

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Receptor-like protein-tyrosine phosphatase sigma (PTP ) is essential for neuronal development and function. Here we report that PTP is a target of ␣-latrotoxin, a strong stimulator of neuronal exocytosis. ␣-Latrotoxin binds to the cell adhesion-like extracellular region of PTP . This binding results in the stimulation of exocytosis. The toxin-binding site is located in the C-terminal part of the PTP ectodomain and includes two fibronectin type III repeats. The intracellular catalytic domains of PTP are not required for the ␣-latrotoxin binding and secretory response triggered by the toxin in chromaffin cells. These features of PTP resemble two other previously described ␣-latrotoxin receptors, neurexin and CIRL. Thus, ␣-latrotoxin represents an unusual example of the neurotoxin that has three independent, equally potent, and yet structurally distinct targets. The known structural and functional characteristics of PTP , neurexin, and CIRL suggest that they define a functional family of neuronal membrane receptors with complementary or converging roles in presynaptic function via a mechanism that involves cellto-cell and cell-to-matrix interaction.

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Section: Figsupporting

confidence: 66%

“…This membrane phosphatase was discovered independently in several laboratories and is known as PTP (24), PTP NE-3 (25), PTP-P1 (26), and LAR-PTP2 (27). Genetic studies in mouse and Drosophila identified PTP as a protein essential for neuronal development and axonal pathfinding (28 -30).…”

mentioning

confidence: 99%

Protein-tyrosine Phosphatase-ς Is a Novel Member of the Functional Family of α-Latrotoxin Receptors

Krasnoperov

Bittner

et al. 2002

Journal of Biological Chemistry

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“…whole-mouse embryo RNA and has an 80% sequence identity to human LAR (Strueli et al, 1988) in the intracellular domain. During the course of our work, the rat homolog of PTP NU-3 was reported by several laboratories, including LAR-PTP2 , PTP NE-3 (Walton et al, 1993), CPTP-1/3 (Sahin and Hockfield, 1993), PTP-PUPS (Pan et al, 1993) and HPTP-a (Yan et al, 1993). A series of NU-3 cDNAs were cloned by screening an 18.5-day p.c.…”

Section: Gac M T Gac Ggt Ttc Atc Gtg Gtc Tac Ctg Cct Gat Ggc Cag Act mentioning

confidence: 99%

“…This manuscript reports the molecular cloning and the identification of a unique splice form of NU-3, the murine homolog of the rat CAM tyrosine phosphatase known as LAR-PTP2 , PTP NE-3, (Walton et al, 1993), CPTP-1/3 (Sahin and Hockfield, 1993), PTP-Pl/PS (Pan et al, 1993) and RPTP-a (Yan et al, 1993).…”

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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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“…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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A novel receptor-type protein tyrosine phosphatase is expressed during neurogenesis in the olfactory neuroepithelium

Cited by 75 publications

References 74 publications

Protein-tyrosine Phosphatase-ς Is a Novel Member of the Functional Family of α-Latrotoxin Receptors

Protein-tyrosine Phosphatase-ς Is a Novel Member of the Functional Family of α-Latrotoxin Receptors

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

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

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