Tyrosine phosphorylation and cadherin/catenin function

BioEssays - Tập 19 Số 10 - Trang 883-891 - 1997
Juliet M. Daniel1, Albert B. Reynolds2
1Department of Cell Biology, Vanderbilt University School of Medicine, Nashville, TN 37232-2175, USA
2Dept of Cell Biology, MCN-C2310, Vanderbilt University School of Medicine, 1161 21st Ave. South, Nashville, TN 37232-2175, USA

Tóm tắt

AbstractCadherin‐mediated cell‐cell adhesion is perturbed in protein tyrosine kinase (PTK)‐transformed cells. While cadherins themselves appear to be poor PTK substrates, their cytoplasmic binding partners, the Arm catenins, are excellent PTK substrates and therefore good candidates for mediating PTK‐induced changes in cadherin behavior. These proteins, p120ctn, β‐catenin and plakoglobin, bind to the cytoplasmic region of classical cadherins and function to modulate adhesion and/or bridge cadherins to the actin cytoskeleton. In addition, as demonstrated recently for β‐catenin, these proteins also have crucial signaling roles that may or may not be related to their effects on cell‐cell adhesion. Tyrosine phosphorylation of cadherin complexes is well documented and widely believed to modulate cell adhesiveness. The data to date, however, is largely correlative and the mechanism of action remains unresolved. In this review, we discuss the current literature and suggest models whereby tyrosine phosphorylation of Arm catenins contribute to regulation or perturbation of cadherin function.

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Tài liệu tham khảo

Birchmeier W., 1993, Molecular mechanisms leading to cell junction (cadherin) deficiency in invasive carcinomas, Semin. Cancer Biol., 4, 231

10.1016/0955-0674(95)80104-9

10.1126/science.2006419

10.1016/S0962-8924(00)89015-7

Oyama T., 1994, A truncated β‐catenin disrupts the interaction between E‐cadherin and α‐catenin: a cause of loss of intercellular adhesiveness in human cancer cell lines, Cancer Res., 54, 6282

10.1128/MCB.15.3.1175

Morton R. A., 1993, Reduction of E‐cadherin levels and deletion of the β‐catenin gene in human prostate cancer cells, Cancer Res., 53, 3585

Shimoyama Y., 1992, Cadherin dysfunction in a human cancer cell line; possible involvement of loss of β‐catenin expression in reduced cell‐cell adhesiveness, Cancer Res., 52, 1

10.1126/science.8259518

10.1126/science.8259519

10.1038/359235a0

10.1016/0955-0674(95)80102-2

10.1083/jcb.127.6.2061

McCrea P. D., 1991, Purification of a 92‐kDa cytoplasmic protein tightly associated with the cell‐cell adhesion molecule E‐cadherin (Uvomorulin), J. Biol. Chem., 266, 4514, 10.1016/S0021-9258(20)64353-8

Nagafuchi A., 1989, Transmembrane control of cadherin‐mediated cell adhesion: a 94‐kD protein functionally associates with a specific region of the cytoplasmic domain of E‐cadherin, Cell Regul., 1, 37, 10.1091/mbc.1.1.37

10.1073/pnas.88.20.9156

10.1016/0092-8674(91)90392-C

10.1073/pnas.87.11.4246

10.1083/jcb.130.1.67

10.1128/MCB.14.12.8333

10.1083/jcb.128.5.949

10.1083/jcb.130.2.369

Reynolds A. B., 1992, p120, a novel substrate of protein tyrosine kinase receptors and of p60v‐src, is related to cadherin‐binding factors β‐catenin, plakoglobin and armadillo, Oncogene, 7, 2439

10.1128/MCB.15.9.4819

Reynolds A. B., 1997, Cytoskeletal‐Membrane Interactions and Signal Transduction

10.1006/geno.1997.4627

Hatzfeld M., 1996, Cloning and characterization of a new armadillo family member, p0071, associated with the junctional plaque: evidence for a subfamily of closely related proteins, J. Cell Sci., 109, 2767, 10.1242/jcs.109.11.2767

Hatzfeld M., Cytoskeletal‐Membrane Interactions and Signal Transduction

10.1016/0304-419X(96)00003-0

10.1083/jcb.113.4.867

10.1002/j.1460-2075.1993.tb05658.x

10.1128/MCB.9.2.629

10.1083/jcb.120.3.757

10.1083/jcb.118.3.703

10.3109/15419069409097261

Downing J. R., 1991, PDGF, CSF‐1, and EGF induce tyrosine phosphorylation of p120, a pp60src transformation‐associated substrate, Oncogene, 6, 607

10.1128/MCB.11.2.713

10.1083/jcb.127.5.1375

10.1006/excr.1996.0057

Shibata T., 1996, Dominant negative inhibition of the association between β‐catenin and c‐erbB‐2 by N‐terminally deleted β‐catenin suppresses the invasion and metastasis of cancer cells, Oncogene, 13, 883

10.1073/pnas.82.19.6576

Volberg T., 1992, The effect of tyrosine‐specific protein phosphorylation in the assembly of adherens‐type junctions, EMBO J., 11, 1733, 10.1002/j.1460-2075.1992.tb05225.x

10.1128/MCB.7.4.1326

10.1073/pnas.82.14.4625

McManus M. J., 1995, Tissue‐ and transformation‐specific phosphotyrosyl proteins in v‐erbB‐transformed cells, J. Virol., 69, 3631, 10.1128/jvi.69.6.3631-3638.1995

10.1128/MCB.15.2.704

10.1126/science.275.5307.1790

10.1126/science.275.5307.1752

10.1126/science.275.5307.1784

10.1126/science.275.5307.1787

Rosen N., 1986, Analysis of pp60c‐src protein kinase activity in human tumor cell lines and tissues, J. Biol. Chem., 26, 13754, 10.1016/S0021-9258(18)67084-X

10.1073/pnas.84.8.2251

10.1006/bbrc.1994.2631

10.1006/bbrc.1994.2213

10.1073/pnas.91.1.83

10.1002/j.1460-2075.1993.tb05735.x

10.1073/pnas.90.16.7696

10.1128/MCB.15.8.4553

10.1083/jcb.134.6.1519

10.1083/jcb.130.4.977

10.1074/jbc.271.28.16712

10.1083/jcb.134.3.801

10.1016/0955-0674(95)80106-5

10.1083/jcb.134.6.1513

10.1083/jcb.131.1.251

10.1073/pnas.87.9.3328

10.1128/MCB.11.10.5113

10.1073/pnas.89.11.5192

10.1128/MCB.13.12.7892

10.1038/376267a0

10.1074/jbc.272.2.1263

10.1083/jcb.130.2.461

10.1002/(SICI)1097-0215(19960927)68:1<14::AID-IJC3>3.0.CO;2-#

10.1073/pnas.92.19.8813

10.1016/0006-291X(92)91820-G

10.1016/S0955-0674(96)80059-7

10.1002/bies.950190208

10.1038/372786a0

Gopalakrishnan S., 1995, Modulation of E‐cadherin localization in cells expressing wild‐type E1A 12S or hypertransforming mutants, Cell Growth Diff., 6, 985

10.1083/jcb.129.5.1363

10.1083/jcb.127.1.235

10.1083/jcb.131.6.1839

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BioEssays

Tập 19 Số 10

883-891

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