DOI: 10.1242/jcs.110.17.2065. Cell confluence regulates tyrosine phosphorylation of adherens junction components in endothelial cells

Cell confluence regulates tyrosine phosphorylation of adherens junction components in endothelial cells

10.1242/jcs.110.17.2065

Crossref journal-article

The Company of Biologists

Journal of Cell Science (237)

Abstract

ABSTRACT In srcand ras-transformed cells, tyrosine phosphorylation of adherens junction (AJ) components is related to impairment of cell-cell adhesion. In this paper we report that in human endothelial cells (EC), tyrosine phosphorylation of AJ can be a physiological process regulated by cell density. Immunofluorescence analysis revealed that a phosphotyrosine (P-tyr) antibody could stain cell-cell junctions only in sparse or loosely confluent EC, while the staining was markedly reduced in tightly confluent cultures. This process was reversible, since on artificial wounding of EC monolayers, the cells at the migrating front reacquired P-tyr labelling at cell contacts. In EC, the major cadherin at intercellular AJ is the cell-type-specific VE-cadherin. We therefore analyzed whether this molecule was at least in part responsible for the changes in P-tyr content at cell junctions. Tyrosine phosphorylation of VE-cadherin, β-catenin and p120, occurred in looser AJ, i.e. in recently confluent cells, and was notably reduced in tightly confluent cultures. Changes in P-tyr content paralleled changes in the molecular organization of AJ. VE-cadherin was mostly associated with β-catenin and p120 in loose EC monolayers, while in long-confluent cells, these two catenins were largely replaced by plakoglobin. Inhibition of P-tyr phosphatases (PTPases) by PV markedly augmented the P-tyr content of VE-cadherin, which bound p120 and β-catenin more efficiently, but not plakoglobin. Transfection experiments in CHO cells showed that p120 could bind to a VE-cadherin cytoplasmic region different from that responsible for β-catenin binding, and PV stabilized this association. Overall these data indicate that endothelial AJ are dynamic structures that can be affected by the state of confluence of the cells. Tyrosine phosphorylation of VE-cadherin and its association to p120 and β-catenin characterizes early cell contacts, while the formation of mature and cytoskeleton-connected junctions is accompanied by dephosphorylation and plakoglobin association.

Bibliography

Lampugnani, M. G., Corada, M., Andriopoulou, P., Esser, S., Risau, W., & Dejana, E. (1997). Cell confluence regulates tyrosine phosphorylation of adherens junction components in endothelial cells. Journal of Cell Science, 110(17), 2065â2077.

Authors 6

Maria Grazia Lampugnani (first)
Monica Corada (additional)
Paraskevi Andriopoulou (additional)
Sybille Esser (additional)
Werner Risau (additional)
Elisabetta Dejana (additional)

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Dates

Type	When
Created	4 years, 4 months ago (April 25, 2021, 12:47 p.m.)
Deposited	1 year, 7 months ago (Jan. 6, 2024, 4:24 p.m.)
Indexed	4 months, 1 week ago (April 22, 2025, 3:32 a.m.)
Issued	28 years ago (Sept. 1, 1997)
Published	28 years ago (Sept. 1, 1997)
Published Online	28 years ago (Sept. 1, 1997)
Published Print	28 years ago (Sept. 1, 1997)

Funders 0

None

BibTeX

@article{Lampugnani_1997, title={Cell confluence regulates tyrosine phosphorylation of adherens junction components in endothelial cells}, volume={110}, ISSN={1477-9137}, url={http://dx.doi.org/10.1242/jcs.110.17.2065}, DOI={10.1242/jcs.110.17.2065}, number={17}, journal={Journal of Cell Science}, publisher={The Company of Biologists}, author={Lampugnani, Maria Grazia and Corada, Monica and Andriopoulou, Paraskevi and Esser, Sybille and Risau, Werner and Dejana, Elisabetta}, year={1997}, month=sep, pages={2065–2077} }

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