The LIM protein ajuba is recruited to cadherin-dependent cell junctions through an association with α-catenin

Helene Marie, Stephen J. Pratt, Martha Betson, Holly Epple, Josef T. Kittler, Laura Meek, Stephen J. Moss, Sergey Troyanovsky, David Attwell, Gregory D. Longmore, Vania M.M. Braga

Research output: Contribution to journalArticlepeer-review

124 Scopus citations


Cell-cell adhesive events affect cell growth and fate decisions and provide spatial clues for cell polarity within tissues. The complete molecular determinants required for adhesive junction formation and their function are not completely understood. LIM domain-containing proteins have been shown to be present at cell-cell contact sites and are known to shuttle into the nucleus where they can affect cell fate and growth; however, their precise localization at cell-cell contacts, how they localize to these sites, and what their functions are at these sites is unknown. Here we show that, in primary keratinocytes, the LIM domain protein Ajuba is recruited to cadherin-dependent cell-cell adhesive complexes in a regulated manner. At cadherin adhesive complexes Ajuba interacts with α-catenin, and α-catenin is required for efficient recruitment of Ajuba to cell junctions. Ajuba also interacts directly with F-actin. Keratinocytes from Ajuba null mice exhibit abnormal cell-cell junction formation and/or stability and function. These data reveal Ajuba as a new component at cadherin-mediated cell-cell junctions and suggest that Ajuba may contribute to the bridging of the cadherin adhesive complexes to the actin cytoskeleton and as such contribute to the formation or strengthening of cadherin-mediated cell-cell adhesion.

Original languageEnglish
Pages (from-to)1220-1228
Number of pages9
JournalJournal of Biological Chemistry
Issue number2
StatePublished - Jan 10 2003


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