Association between a transmembrane protein tyrosine phosphatase and the cadherin-catenin complex.

Kypta, Robert M.; Su, Hua; Reichardt, Louis F.

doi:10.1083/jcb.134.6.1519

Cited by 236 publications

(164 citation statements)

References 57 publications

(88 reference statements)

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“…This is even more intriguing since a molecular cross-talk between Wnt and EGF signalling is well known (Dierick and Bejsovec, 1999). Besides the kinases, several protein tyrosine phosphatases have been linked to b-catenin function (Hoschuetzky et al, 1994;Brady-Kalnay et al, 1995;Kypta et al, 1996). Future work will reveal which of the kinases or phosphatases is crucial for maintaining b-catenin in a dephosphorylated state in the case of sFRP-mediated signaling.…”

Section: Discussionmentioning

confidence: 99%

Secreted Frizzled-related proteins inhibit motility and promote growth of human malignant glioma cells

et al. 2000

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Cellular resistance to multiple proapoptotic stimuli and invasion of surrounding brain tissue by migrating tumor cells are main obstacles to an e ective therapy for human malignant glioma. Here, we report that the Wnt family of embryonic di erentiation genes modulate growth of malignant glioma cells in vitro and in vivo and inhibit cellular migration in vitro. sFRPs (soluble Frizzled-related proteins) are soluble proteins that bind to Wnt and interfere with Wnt signaling. We ®nd that sFRP-1 and sFRP-2 are produced by the majority of longterm and ex vivo malignant glioma cell lines. Glioma cells that ectopically express sFRPs exhibit increased clonogenicity and enhanced resistance to serum starvation. In contrast, sFRPs do not modulate glioma cell susceptibility to apoptosis induced by the cytotoxic cytokines, CD95 (Fas/APO-1) ligand (CD95L) or Apo2 ligand/tumor necrosis factor-related apoptosisinducing ligand (Apo2L/TRAIL), or various cytotoxic drugs. sFRP-2 strongly promotes the growth of intracranial glioma xenografts in nude mice. In contrast, enhanced expression of sFRPs inhibits the motility of glioma cells in vitro. sFRP-mediated e ects on glioma cells are accompanied by decreased expression and activity of matrix metalloproteinase-2 (MMP-2) and decreased tyrosine phosphorylation of b-catenin. Thus, sFRPs promote survival under non-supportive conditions and inhibit the migration of glioma cells. We suggest that the regulation of these cellular processes involves expression of MMP-2 and tyrosine phosphorylation of bcatenin. These data support a function for Wnt signaling and its modulation by sFRPs in the biology of human gliomas. Oncogene (2000) 19, 4210 ± 4220.

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Section: Discussionmentioning

confidence: 99%

Secreted Frizzled-related proteins inhibit motility and promote growth of human malignant glioma cells

et al. 2000

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“…The focal adhesion molecules β-catenin and p130cas are substrates for LAR (Kypta et al 1996). Dephosphorylation of p130cas by LAR reduces it stability and leads to p130cas degradation, an event that is associated with cell death (Weng et al 1999).…”

Section: Lar and R2a Subfamilymentioning

confidence: 99%

Receptor type protein tyrosine phosphatases (RPTPs) – roles in signal transduction and human disease

Fisher

2012

J. Cell Commun. Signal.

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Protein tyrosine phosphorylation is a fundamental regulatory mechanism controlling cell proliferation, differentiation, communication, and adhesion. Disruption of this key regulatory mechanism contributes to a variety of human diseases including cancer, diabetes, and auto-immune diseases. Net protein tyrosine phosphorylation is determined by the dynamic balance of the activity of protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs). Mammals express many distinct PTKs and PTPs. Both of these families can be sub-divided into non-receptor and receptor subtypes. Receptor protein tyrosine kinases (RPTKs) comprise a large family of cell surface proteins that initiate intracellular tyrosine phosphorylationdependent signal transduction in response to binding of extracellular ligands, such as growth factors and cytokines. Receptor-type protein tyrosine phosphatases (RPTPs) are enzymatic and functional counterparts of RPTKs. RPTPs are a family of integral cell surface proteins that possess intracellular PTP activity, and extracellular domains that have sequence homology to cell adhesion molecules. In comparison to extensively studied RPTKs, much less is known about RPTPs, especially regarding their substrate specificities, regulatory mechanisms, biological functions, and their roles in human diseases. Based on the structure of their extracellular domains, the RPTP family can be grouped into eight sub-families. This article will review one representative member from each RPTP sub-family.

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“…LAR-PTP (Kypta et al, 1996;Mü ller et al, 1999) has been shown to interact with and dephosphorylate ␤-catenin. Additionally, overexpression of LAR-PTP correlates with prevention of ␤-catenin phosphorylation and inhibition of epithelial cell migration (Mü ller et al, 1999).…”

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

149

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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Association between a transmembrane protein tyrosine phosphatase and the cadherin-catenin complex.

Cited by 236 publications

References 57 publications

Secreted Frizzled-related proteins inhibit motility and promote growth of human malignant glioma cells

Secreted Frizzled-related proteins inhibit motility and promote growth of human malignant glioma cells

Receptor type protein tyrosine phosphatases (RPTPs) – roles in signal transduction and human disease

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

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