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

Sap, Jan; Jiang, Ying-Ping; Friedlander, David R.; Grumet, Martin; Schlessinger, Joseph

doi:10.1128/mcb.14.1.1

Cited by 201 publications

(112 citation statements)

References 55 publications

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“…S2 insect cells overexpressing Ark formed multicellular aggregates that could be blocked by excess recombinant Ark ECD (6). Similar results could be achieved upon overexpression of D-Trk or protein phosphatase-and -in the same S2 cells (7)(8)(9). These data raise the possibility that receptor tyrosine kinases and transmembrane phosphatases may function both as adhesion molecules and as elements of the signaling cascade.…”

supporting

confidence: 68%

GAS6 Mediates Adhesion of Cells Expressing the Receptor Tyrosine Kinase Axl

McCloskey

Fridell²,

Attar³

et al. 1997

Journal of Biological Chemistry

126

103

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Axl is a receptor tyrosine kinase that contains both immunoglobulin and fibronectin III repeats in its extracellular domain reminiscent of cell adhesion molecules. Expression of the receptor tyrosine kinase Axl in the 32D myeloid cell line permits aggregation of cells in response to treatment with the native ligand GAS6; this aggregation was not observed in untreated 32D-Axl cells nor in treated parental cells. This aggregation can be blocked by the addition of excess Axl extracellular domain peptide and does not require intracellular Axl kinase activity. Cell surface binding activity of GAS6 was mapped to distinct plasma membrane interacting domains that are separate from the GAS6 motifs that engage the Axl receptor. This suggests that aggregation is mediated by a heterotypic intercellular mechanism whereby cell-bound GAS6 interacts with Axl receptor on an adjacent cell. This mechanism is supported by our observation that GAS6 binds to 32D parental cells which then permits their aggregation with untreated 32D-Axl cells. We have recently demonstrated that the GAS6-Axl interaction does not initiate mitogenesis in 32D cells. When considered with the adhesion results, these data suggest that an important biological function of the Axl-GAS6 interaction is to mediate cell-cell binding.

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supporting

confidence: 68%

GAS6 Mediates Adhesion of Cells Expressing the Receptor Tyrosine Kinase Axl

McCloskey

Fridell²,

Attar³

et al. 1997

Journal of Biological Chemistry

126

103

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“…more, interaction of PTP␤/ with its ligand, pleiotrophin, results in inactivation of its intrinsic catalytic activity and enhanced tyrosine phosphorylation of ␤-catenin (Meng et al, 2000). The RPTPs , ␥, and are closely related (Neel and Tonks, 1997) and all are able to mediate homophilic adhesions (Brady-Kalnay et al, 1993, Gebbink et al, 1993Sap et al, 1994;BradyKalnay and Tonks, 1994;Cheng et al, 1997). Thus it is interesting that there are two apparently different roles with respect to cadherin function within this structurally related group.…”

Section: Destabilizing Adhesions: Altering the Balance Between Phosphmentioning

confidence: 99%

Turn‐off, drop‐out: Functional state switching of cadherins

Lilien

Balsamo

Arregui

et al. 2002

Developmental Dynamics

147

116

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The classic cadherins are a group of calcium dependent, homophilic cell-cell adhesion molecules that drive morphogenetic rearrangements and maintain the integrity of cell groups through the formation of adherens junctions. The formation and maintenance of cadherin-mediated adhesions is a multistep process and mechanisms have evolved to regulate each step. This suggests that functional state switching plays an important role in development. Among the many challenges ahead is to determine the developmental role that functional state switching plays in tissue morphogenesis and to define the roles of each of the several regulatory interactions that participate in switching. One correlate of the loss of cadherinmediated adhesion, the "turn-off" of cadherin function, is the exit, or "drop-out" of cells from neural and epithelial layers and their conversion to a motile phenotype. We suggest that epithelial mesenchymal conversions may be initiated by signaling pathways that result in the loss of cadherin function. Tyrosine phosphorylation of ␤-catenin is one such mechanism. Enhanced phosphorylation of tyrosine residues on ␤-catenin is almost invariably associated with loss of the cadherin-actin connection concomitant with loss of adhesive function. There are several tyrosine kinases and phosphatases that have been shown to have the potential to alter the phosphorylation state of ␤-catenin and thus the function of cadherins. Our laboratory has focused on the role of the nonreceptor tyrosine phosphatase PTP1B in regulating the phosphorylation of ␤-catenin on tyrosine residues. Our data suggest that PTP1B is crucial for maintenance of N-cadherin-mediated adhesions in embryonic neural retina cells. By using an L-cell model system constitutively expressing N-cadherin, we have worked out many of the molecular interactions essential for this regulatory interaction. Extracellular cues that bias this critical regulatory interaction toward increased phosphorylation of ␤-catenin may be a critical component of many developmental events.

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“…For most rPTPs the ligands remain uncharacterized. Known ligands for rPTPs include the extracellular domains of PTPm and PTPk, that act as homophilic ligands (Brady-Kalnay et al, 1993;Gebbink et al, 1993;Sap et al, 1994), and contactin which interacts with PTPb/z and PTPa (Peles et al, 1995;Zeng et al, 1999), as well as the extracellular matrix proteins tenascin and the laminin-nidogen complex which binds PTPb/z and LAR, respectively (Barnea et al, 1994, O'Grady et al, 1998. The recent observation of pleiotrophin-mediated inactivation of PTPb/z provided the ®rst evidence for regulation of rPTPs by extracellular ligands (Meng et al, 2000).…”

mentioning

confidence: 99%

An extracellular ligand increases the specific activity of the receptor-like protein tyrosine phosphatase DEP-1

2001

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Cellular growth, di erentiation and migration is regulated by protein tyrosine phosphorylation. Receptor-like protein tyrosine phosphatases are thus likely to be key regulators of vital cellular processes. The regulation of these enzymes is in general poorly understood. Ligands have been identi®ed only for a small subset of the receptor-like protein tyrosine phosphatases and in no case has upregulation of the speci®c activity by extracellular ligands been demonstrated. Prompted by earlier ®ndings of ligands for receptor-like protein tyrosine phosphatases in extracellular matrix we investigated if Matrigel TM , a preparation of extracellular matrix proteins, contained modulators of the speci®c activity of the receptor-like protein tyrosine phosphatase DEP-1. Matrigel TM stimulation of cells increased the speci®c activity of immunoprecipitated DEP-1. Also, incubation of immunoprecipitated DEP-1 with Matrigel TM led to an increase in DEP-1 activity, which was blocked by soluble DEP-1 extracellular domain. Finally, immunoprecipitated DECD-DEP-1, a mutant form of DEP-1 lacking most of the extracellular domain, failed to respond to Matrigel TM stimulation. These experiments identify Matrigel TM as a source of DEP-1 agonist(s) and provide the ®rst evidence for upregulation of the speci®c activity of receptor-like protein tyrosine phosphatases by extracellular ligands. Oncogene (2001) 20, 5219 ± 5224.

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

Cited by 201 publications

References 55 publications

GAS6 Mediates Adhesion of Cells Expressing the Receptor Tyrosine Kinase Axl

GAS6 Mediates Adhesion of Cells Expressing the Receptor Tyrosine Kinase Axl

Turn‐off, drop‐out: Functional state switching of cadherins

An extracellular ligand increases the specific activity of the receptor-like protein tyrosine phosphatase DEP-1

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