The LAR/PTP delta/PTP sigma subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1.

Pulido, Rafael; Serra-Pagès, Carles; Tang, May; Streuli, Michel

doi:10.1073/pnas.92.25.11686

Cited by 189 publications

(169 citation statements)

References 36 publications

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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: 67%

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: 67%

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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“…The Slitrk1 and PTPs point mutants, described in Supplementary Table 3 were generated with a QuickChange site-directed mutagenesis kit (Stratagene) and verified by DNA sequencing. The PTPs and Slitrk1 residues are numbered with respect to the human PTPs (AAX50299.1) and Slitrk1 (NP_443142.1) sequence, respectively, which was previously described 5,12 .…”

Section: Methodsmentioning

confidence: 99%

“…In particular, multiple LAR-RPTP isoforms are generated by alternative splicing of four mini exons, termed MeA to MeD, that encode short peptides (Fig. 1a) 4,5 . The LARRPTPs have a single transmembrane domain followed by two intracellular phosphatase domains (a membrane-proximal catalytic domain called D1 and a membrane-distal non-catalytic domain called D2) where multiple intracellular adaptor proteins bind 6 .…”

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confidence: 99%

Structural basis for LAR-RPTP/Slitrk complex-mediated synaptic adhesion

et al. 2014

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Synaptic adhesion molecules orchestrate synaptogenesis. The presynaptic leukocyte common antigen-related receptor protein tyrosine phosphatases (LAR-RPTPs) regulate synapse development by interacting with postsynaptic Slit-and Trk-like family proteins (Slitrks), which harbour two extracellular leucine-rich repeats (LRR1 and LRR2). Here we identify the minimal regions of the LAR-RPTPs and Slitrks, LAR-RPTPs Ig1-3 and Slitrks LRR1, for their interaction and synaptogenic function. Subsequent crystallographic and structureguided functional analyses reveal that the splicing inserts in LAR-RPTPs are key molecular determinants for Slitrk binding and synapse formation. Moreover, structural comparison of the two Slitrk1 LRRs reveal that unique properties on the concave surface of Slitrk1 LRR1 render its specific binding to LAR-RPTPs. Finally, we demonstrate that lateral interactions between adjacent trans-synaptic LAR-RPTPs/Slitrks complexes observed in crystal lattices are critical for Slitrk1-induced lateral assembly and synaptogenic activity. Thus, we propose a model in which Slitrks mediate synaptogenic functions through direct binding to LAR-RPTPs and the subsequent lateral assembly of LAR-RPTPs/Slitrks complexes.

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“…The extracellular domains of LAR-like RPTPs contain Ig-like and fibronectin type III (FNIII) repeats. Alternative splicing of RPTP genes result in isoforms that differ in the extracellular domain and can exhibit tissue-specific expression and localization, suggesting the ectodomain confers functional specificity (O'Grady et al, 1994;Pulido et al, 1995;Honkaniemi et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

The Two Isoforms of theCaenorhabditis elegansLeukocyte-Common Antigen Related Receptor Tyrosine Phosphatase PTP-3 Function Independently in Axon Guidance and Synapse Formation

Ackley¹,

Harrington²,

Hudson³

et al. 2005

J. Neurosci.

107

146

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Leukocyte-common antigen related (LAR)-like phosphatase receptors are conserved cell adhesion molecules that function in multiple developmental processes. The Caenorhabditis elegans ptp-3 gene encodes two LAR family isoforms that differ in the extracellular domain. We show here that the long isoform, PTP-3A, localizes specifically at synapses and that the short isoform, PTP-3B, is extrasynaptic. Mutations in ptp-3 cause defects in axon guidance that can be rescued by PTP-3B but not by PTP-3A. Mutations that specifically affect ptp-3A do not affect axon guidance but instead cause alterations in synapse morphology. Genetic double-mutant analysis is consistent with ptp-3A acting with the extracellular matrix component nidogen, nid-1, and the intracellular adaptor ␣-liprin, syd-2. nid-1 and syd-2 are required for the recruitment and stability of PTP-3A at synapses, and mutations in ptp-3 or nid-1 result in aberrant localization of SYD-2. Overexpression of PTP-3A is able to bypass the requirement for nid-1 for the localization of SYD-2 and RIM. We propose that PTP-3A acts as a molecular link between the extracellular matrix and ␣-liprin during synaptogenesis.

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The LAR/PTP delta/PTP sigma subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1.

Abstract: The transmembrane protein-tyrosinephosphatases (PTPases) LAR

Cited by 189 publications

References 36 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

Structural basis for LAR-RPTP/Slitrk complex-mediated synaptic adhesion

The Two Isoforms of theCaenorhabditis elegansLeukocyte-Common Antigen Related Receptor Tyrosine Phosphatase PTP-3 Function Independently in Axon Guidance and Synapse Formation

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