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A more recent version of this article appeared on March 1, 2004
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Submitted on July 25, 2003
Revised on October 29, 2003
Accepted on November 17, 2003
1 Molecular Tumor Biology Section, Basic Research Laboratory, National Cancer Institute, Bethesda, Maryland, 20892-4255
* Corresponding author. E-mail address: toru{at}helix.nih.gov.
Dynamic rearrangements of cell-cell adhesion underlie a diverse range of physiological processes, but their precise molecular mechanisms are still obscure. Thus identification of novel players that are involved in cell-cell adhesion would be important. We isolated a human kelch related protein, KLEIP, which contains the BTB/POZ motif and six-tandem kelch repeats. KLEIP interacted with F-actin, and was concentrated at cell-cell contact sites of MDCK cells, where it colocalized with F-actin. Interestingly, this localization took place transiently during the induction of cell-cell contact and was not seen at mature junctions. KLEIP recruitment and actin assembly were induced around E-cadherin-coated beads placed on cell surfaces. The actin depolymerizing agent, cytochalasin B inhibited this KLEIP recruitment around E-cadherin-coated beads. Moreover, constitutively active Rac1 enhanced the recruitment of KLEIP as well as F-actin to the adhesion sites. These observations strongly suggest that KLEIP is localized on actin filaments at the contact sites. We also found that N-terminal half of KLEIP, which lacks the actin-binding site and contains the sufficient sequence for the localization at the cell-cell contact sites, inhibited constitutively active Rac1-induced actin assembly at the contact sites. We propose that KLEIP is involved in Rac1-induced actin organization during cell-cell contact in MDCK cells.
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