QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

Vol. 15, Issue 3, 1172-1184, March 2004

This Article Full Text Full Text (PDF) Supplemental Figure All Versions of this Article: E03-07-0531v1 15/3/1172    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Hara, T. Articles by Miki, T. Search for Related Content PubMed PubMed Citation Articles by Hara, T. Articles by Miki, T.

Novel Kelch-like Protein, KLEIP, Is Involved in Actin Assembly at Cell-Cell Contact Sites of Madin-Darby Canine Kidney Cells

Molecular Tumor Biology Section, Basic Research Laboratory, National Cancer Institute, Bethesda, Maryland, 20892-4255

Submitted July 25, 2003; Revised October 29, 2003; Accepted November 17, 2003
Monitoring Editor: Martin A. Schwartz

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, Kelch-like ECT2 interacting protein (KLEIP), which contains the broad-complex, tramtrack, bric-a-brac (BTB)/poxvirus, zinc finger (POZ) motif and six-tandem kelch repeats. KLEIP interacted with F-actin and was concentrated at cell-cell contact sites of Madin-Darby canine kidney 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 Madin-Darby canine kidney cells.

Abbreviations used: CA, constitutively active; ECT2, epithelial cell transforming gene 2; GFP, green fluorescence protein; GST, glutathione S-transferase; KLEIP, Kelch-like ECT2 interacting protein; PBS, phosphate-buffered saline; TBS, Tris-buffered saline.

^* Corresponding author. E-mail address: toru{at}helix.nih.gov.

This article has been cited by other articles:

				Y. Yamaguchi, T. Passeron, T. Hoashi, H. Watabe, F. Rouzaud, K.-i. Yasumoto, T. Hara, C. Tohyama, I. Katayama, T. Miki, et al. Dickkopf 1 (DKK1) regulates skin pigmentation and thickness by affecting Wnt/{beta}-catenin signaling in keratinocytes FASEB J, April 1, 2008; 22(4): 1009 - 1020. [Abstract] [Full Text] [PDF]

				C. A. Balinsky, G. Delhon, C. L. Afonso, G. R. Risatti, M. V. Borca, R. A. French, E. R. Tulman, S. J. Geary, and D. L. Rock Sheeppox Virus Kelch-Like Gene SPPV-019 Affects Virus Virulence J. Virol., October 15, 2007; 81(20): 11392 - 11401. [Abstract] [Full Text] [PDF]

				T. G. Nacak, A. Alajati, K. Leptien, C. Fulda, H. Weber, T. Miki, F. S. Czepluch, J. Waltenberger, T. Wieland, H. G. Augustin, et al. The BTB-Kelch Protein KLEIP Controls Endothelial Migration and Sprouting Angiogenesis Circ. Res., April 27, 2007; 100(8): 1155 - 1163. [Abstract] [Full Text] [PDF]

				G. D. Salinas, L. A. C. Blair, L. A. Needleman, J. D. Gonzales, Y. Chen, M. Li, J. D. Singer, and J. Marshall Actinfilin Is a Cul3 Substrate Adaptor, Linking GluR6 Kainate Receptor Subunits to the Ubiquitin-Proteasome Pathway J. Biol. Chem., December 29, 2006; 281(52): 40164 - 40173. [Abstract] [Full Text] [PDF]

				J. A. Scott, A. M. Shewan, N. R. den Elzen, J. J. Loureiro, F. B. Gertler, and A. S. Yap Ena/VASP Proteins Can Regulate Distinct Modes of Actin Organization at Cadherin-adhesive Contacts Mol. Biol. Cell, March 1, 2006; 17(3): 1085 - 1095. [Abstract] [Full Text] [PDF]