RIFLE: a novel ring zinc finger-leucine-rich repeat containing protein, regulates select cell adhesion molecules in PC12 cells.

Cell adhesion molecules play a critical role in cell contacts, whether cell-cell or cell-matrix, and are regulated by multiple signaling pathways. In this report, we identify a novel ring zinc finger-leucine-rich repeat containing protein (RIFLE) and show that RIFLE, expressed in PC12 cells, enhances the Serine (Ser)21/9 phosphorylation of glycogen ...
synthase kinase-3alpha/beta (GSK-3alpha/beta) resulting in the inhibition of GSK-3 kinase activity and increase of beta-catenin levels. RIFLE expression also is associated with elevated E-cadherin protein levels but not N-cadherin. The regulation of these cell adhesion-associated molecules by RIFLE is accompanied by a significant increase in cell-cell and cell-matrix adhesion. Moreover, increase in cell-cell adhesion but not cell-matrix adhesion by RIFLE can be mimicked by selective inhibition of GSK-3. Our results suggest that RIFLE represents a novel signaling protein that mediates components of the Wnt/wingless signaling pathway and cell adhesion in PC12 cells.
Mesh Terms:
Amino Acid Sequence, Animals, Base Sequence, Cadherins, Calcium, Cell Adhesion Molecules, Collagen Type IV, Cytoskeletal Proteins, Fibronectins, Glycogen Synthase Kinase 3, Humans, Molecular Sequence Data, PC12 Cells, Phosphorylation, Proteins, Proto-Oncogene Proteins, Rats, Sequence Alignment, Signal Transduction, Tissue Distribution, Trans-Activators, Wnt Proteins, Zinc Fingers, beta Catenin
J. Cell. Biochem.
Date: Dec. 15, 2003
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