CD148, a membrane protein tyrosine phosphatase, is able to induce tyrosine phosphorylation on human lymphocytes

Palou, Eduard; Fuente, Miguel A. de la; Nicolás, Josep M.; Vilardell, Carme; Vives, Jordi; Gayà, Antoni

doi:10.1016/s0165-2478(97)00069-2

Cited by 14 publications

(12 citation statements)

References 11 publications

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“…Our results showed that the crosslinking of CD148 is able to induce an increase in [Ca2+Ii as well as tyrosine phosphorylation of several substrates (20), including PLC-yl (6). It has also been shown that ligation of CD148 on T cells by immobilized, but not soluble, anti-CD148 mAb greatly augmented the in vitro pro-242 ANTON GAYA et al…”

Section: Functional Characterization Of Cd148mentioning

confidence: 61%

CD148, a New Membrane Tyrosine Phosphatase Involved in Leukocyte Function

Gayà¹,

Pirotto²,

Palou³

et al. 1999

Leukemia & Lymphoma

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Protein tyrosine phosphatases play an essential role in the control of leucocyte cell growth an differentiation. Recently a new receptor type membrane tyrosine phosphatase named CD148 has been identified. This molecule is present on the membrane of all the hematopoietic lineages as well as on several other cell types, mainly epithelial cells and its expression increases after cell activation. This molecule is able to act as a transducing molecule. Moreover, CD148 is able to modulate the signal transduction through the TCR/CD3 complex, in a manner similar to CD45. It has also been suggested that CD148 could be involved in mechanisms of differentiation and inhibition of cell growth. In addition, CD148 seems to be associated with a serine/threonine kinase in certain epithelial cell lines and leucocytes. Here, we review recent data on the expression and function of CD148 in both human, mouse and rat.

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Section: Functional Characterization Of Cd148mentioning

confidence: 61%

CD148, a New Membrane Tyrosine Phosphatase Involved in Leukocyte Function

Gayà¹,

Pirotto²,

Palou³

et al. 1999

Leukemia & Lymphoma

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“…Antibodies-DEP-1 monoclonal antibodies A3 and 143-41 used for immunoprecipitations were generous gifts from Dr. Gregorio Aversa and Dr. Antoni Gayá , respectively, and were described previously (9,10). The DEP-1 polyclonal antibody CS895A was generated against the DEP-1 extracellular domain peptide (CDASNTERSRAGSPTAP) corresponding to amino acids 292-307 coupled to KLH (Pierce, Rockford, IL).…”

Section: Methodsmentioning

confidence: 99%

“…DEP-1 comprises an extracellular segment of eight fibronectin type III repeats, a transmembrane domain, and a single cytoplasmic PTP domain. Also known as PTP- (6) and CD148 (9,10), DEP-1 is expressed in a variety of tissues and cell types. There is a growing body of evidence suggesting a role for DEP-1 in the inhibition of cell growth.…”

mentioning

confidence: 99%

Hepatocyte Growth Factor Receptor Tyrosine Kinase Met Is a Substrate of the Receptor Protein-tyrosine Phosphatase DEP-1

Palka

Park

Tonks

2003

Journal of Biological Chemistry

156

146

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The receptor protein-tyrosine phosphatase (PTP) DEP-1 (CD148/PTP-) has been implicated in the regulation of cell growth, differentiation, and transformation, and most recently has been identified as a potential tumor suppressor gene mutated in colon, lung, and breast cancers. We have generated constructs comprising the cytoplasmic segment of DEP-1 fused to the maltose-binding protein to identify potential substrates and thereby suggest a physiological function for DEP-1. We have shown that the substrate-trapping mutant form of DEP-1 interacted with a small subset of tyrosine-phosphorylated proteins from lysates of the human breast tumor cell lines MDA-MB-231, T-47D, and T-47D/Met and have identified the hepatocyte growth factor/scatter factor receptor Met, the adapter protein Gab1, and the junctional component p120 catenin as potential substrates. Following ligand stimulation, phosphorylation of specific tyrosyl residues in Met induces mitogenic, motogenic, and morphogenic responses. When co-expressed in 293 cells, the full-length substrate-trapping mutant form of DEP-1 formed a stable complex with the chimeric receptor colony stimulating factor 1 (CSF)-Met and wild type DEP-1 dephosphorylated CSF-Met. Furthermore, we observed that DEP-1 preferentially dephosphorylated a Gab1 binding site (Tyr 1349 ) and a COOH-terminal tyrosine implicated in morphogenesis (Tyr 1365 ), whereas tyrosine residues in the activation loop of Met (Tyr 1230 , Tyr 1234 , and Tyr 1235 ) were not preferred targets of the PTP. The ability of DEP-1 preferentially to dephosphorylate particular tyrosine residues that are required for Met-induced signaling suggests that DEP-1 may function in controlling the specificity of signals induced by this PTK, rather than as a simple "off-switch" to counteract PTK activity.A variety of ligands trigger the reversible phosphorylation of tyrosyl residues in cellular proteins, a process that underlies the control of such fundamental cellular functions as growth and proliferation, migration, and morphogenesis. Tyrosine phosphorylation is regulated by the coordinated action of protein-tyrosine kinases (PTKs) 1 and protein-tyrosine phosphatases (PTPs). Classically it was thought that the PTKs provided the "on-switch" to initiate a physiological response, whereas the PTPs functioned to counteract the PTKs and to return the system to its basal state. However, it was soon shown that PTPs may themselves function positively to promote signaling, for example, by promoting the dephosphorylation and activation of PTKs, thus coordinating with, rather than antagonizing PTK function (reviewed in Ref. 1). A further level of complexity has been introduced with the realization that whether a defined PTP functions positively or negatively may depend upon the signaling context. Thus, SHP-2 is an activator of signaling through the HGF/SF receptor Met (2) and the epidermal growth factor receptor (3), but is an inhibitor of signaling through the platelet-derived growth factor receptor (4). Following ligand binding, a receptor PT...

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“…DEP-1 is expressed at low levels in resting T cells, but is upregulated in activated T cells, and ligation with anti-DEP-1 antibodies induces proliferation of anti-CD3 activated T cells (Tangye et al, 1998a). Interestingly, transient transfection of DEP-1 has been reported to be a negative regulator of T cell activation, and also results in a reduction of TCR-mediated ERK-1 and ERK-2 activation, and reduced tyrosine phosphorylation (Palou et al, 1997;Hundt et al, 1997;Tangye et al, 1998a;Tangye et al, 1998b;Billard et al, 2000;del Pozo et al, 2000). DEP-1…”

Section: Introductionmentioning

confidence: 99%

The tyrosine phosphatase DEP-1 induces cytoskeletal rearrangements, aberrant cell-substratum interactions and a reduction in cell proliferation

Kellie

Craggs

Bird

et al. 2004

Journal of Cell Science

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The receptor protein tyrosine phosphatase density-enhanced phosphatase-1 (DEP-1) has been implicated in aberrant cancer cell growth and immune cell function, however, its function within cells has yet to be properly elucidated. To investigate the cellular function of DEP-1, stable cell lines inducibly expressing DEP-1 were generated. Induction of DEP-1 expression was found to decrease PDGF-stimulated tyrosine phosphorylation of a number of cellular proteins including the PDGF receptor, and to inhibit growth factor-stimulated phosphorylation of components of the MAPK pathway, indicating that DEP-1 antagonised PDGF receptor signalling. This was supported by data showing that DEP-1 expression resulted in a reduction in cell proliferation. DEP-1-expressing cells had fewer actin-containing microfilament bundles, reduced vinculin and paxillin-containing adhesion plaques, and were defective in interactions with fibronectin. Defective cell-substratum adhesion correlated with lack of activation of FAK in DEP-1-expressing cells. Time-lapse interference reflection microscopy of live cells revealed that although small focal contacts at the leading edge were generated in DEP-1-expressing cells, they failed to mature into stable focal adhesions, as found in control cells. Further motility analysis revealed that DEP-1-expressing cells retained limited random motility, but showed no chemotaxis towards a gradient of PDGF. In addition, cell-cell contacts were disrupted, with a change in the localisation of cadherin from discrete areas of cell-cell contact to large areas of membrane interaction, and there was a parallel redistribution of β-catenin. These results demonstrate that DEP-1 is a negative regulator of cell proliferation, cell-substratum contacts, motility and chemotaxis in fibroblasts.

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CD148, a membrane protein tyrosine phosphatase, is able to induce tyrosine phosphorylation on human lymphocytes

Cited by 14 publications

References 11 publications

CD148, a New Membrane Tyrosine Phosphatase Involved in Leukocyte Function

CD148, a New Membrane Tyrosine Phosphatase Involved in Leukocyte Function

Hepatocyte Growth Factor Receptor Tyrosine Kinase Met Is a Substrate of the Receptor Protein-tyrosine Phosphatase DEP-1

The tyrosine phosphatase DEP-1 induces cytoskeletal rearrangements, aberrant cell-substratum interactions and a reduction in cell proliferation

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