E-cadherin regulates the function of the EphA2 receptor tyrosine kinase

Nicole Dodge Zantek, Minoudokht Azimi, Mary Fedor-Chaiken, Bingcheng Wang, Robert Brackenbury, Michael S. Kinch

Research output: Contribution to journalArticlepeer-review

229 Scopus citations


EphA2 is a member of the Eph family of receptor tyrosine kinases, which are increasingly understood to play critical roles in disease and development. We report here the regulation of EphA2 by E-cadherin. In nonneoplastic epithelia, EphA2 was tyrosine-phosphorylated and localized to sites of cell-cell contact. These properties required the proper expression and functioning of E-cadherin. In breast cancer cells that lack E-cadherin, the phosphotyrosine content of EphA2 was decreased, and EphA2 was redistributed into membrane ruffles. Expression of E-cadherin in metastatic cells restored a more normal pattern of EphA2 phosphorylation and localization. Activation of EphA2, either by E-cadherin expression or antibody-mediated aggregation, decreased cell-extracellular matrix adhesion and cell growth. Altogether, this demonstrates that EphA2 function is dependent on E-cadherin and suggests that loss of E-cadherin function may alter neoplastic cell growth and adhesion via effects on EphA2.

Original languageEnglish
Pages (from-to)629-638
Number of pages10
JournalCell Growth and Differentiation
Issue number9
StatePublished - Sep 1999


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