Delta-catenin/NPRAP: A new member of the glycogen synthase kinase-3beta signaling complex that promotes beta-catenin turnover in neurons.

Journal of Neuroscience Research
Sonja BareissQun Lu

Abstract

Through a multiprotein complex, glycogen synthase kinase-3beta (GSK-3beta) phosphorylates and destabilizes beta-catenin, an important signaling event for neuronal growth and proper synaptic function. delta-Catenin, or NPRAP (CTNND2), is a neural enriched member of the beta-catenin superfamily and is also known to modulate neurite outgrowth and synaptic activity. In this study, we investigated the possibility that delta-catenin expression is also affected by GSK-3beta signaling and participates in the molecular complex regulating beta-catenin turnover in neurons. Immunofluorescent light microscopy revealed colocalization of delta-catenin with members of the molecular destruction complex: GSK-3beta, beta-catenin, and adenomatous polyposis coli proteins in rat primary neurons. GSK-3beta formed a complex with delta-catenin, and its inhibition resulted in increased delta-catenin and beta-catenin expression levels. LY294002 and amyloid peptide, known activators of GSK-3beta signaling, reduced delta-catenin expression levels. Furthermore, delta-catenin immunoreactivity increased and protein turnover decreased when neurons were treated with proteasome inhibitors, suggesting that the stability of delta-catenin, like that of beta-catenin...Continue Reading

References

Mar 28, 1995·Proceedings of the National Academy of Sciences of the United States of America·S MunemitsuP Polakis
Jun 30, 1997·The Journal of Cell Biology·A L PollackK E Mostov
Jun 20, 1997·Neuroscience Letters·O MurayamaA Takashima
Jul 1, 1997·The EMBO Journal·H AberleR Kemler
Aug 1, 1997·Differentiation; Research in Biological Diversity·R Paffenholz, W W Franke
Feb 7, 1998·Genes & Development·K M Cadigan, R Nusse
Apr 18, 1998·Proceedings of the National Academy of Sciences of the United States of America·C SakanakaL T Williams
Aug 5, 1998·Proceedings of the National Academy of Sciences of the United States of America·A TakashimaB Wolozin
Mar 19, 1999·Biochemical and Biophysical Research Communications·N IdeY Takai
Aug 18, 1999·Journal of Chemical Neuroanatomy·K Leroy, J P Brion
Nov 1, 2000·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·N Barker, H Clevers
Oct 2, 2001·Science's STKE : Signal Transduction Knowledge Environment·J R Woodgett
Sep 6, 2002·Journal of Alzheimer's Disease : JAD·Juan Ramón Muñoz-MontañoJavier Díaz-Nido
Jul 2, 2003·The Journal of Cell Biology·Maria Cruz MartinezKenneth S Kosik
Oct 7, 2003·Nature Neuroscience·Xiang Yu, Robert C Malenka
Apr 13, 2004·Journal of Cell Science·Yoshitaka TatebayashiInge Grundke-Iqbal

❮ Previous
Next ❯

Citations

May 13, 2011·The Journal of Biological Chemistry·Dongmin GuPierre D McCrea
Nov 12, 2017·Neurology·Anne-Fleur van RootselaarArn M J M van den Maagdenberg
Jan 17, 2021·Molecular & Cellular Proteomics : MCP·Alba SimatsJoan Montaner

❮ Previous
Next ❯

Related Concepts

Related Feeds

Cadherins and Catenins

Cadherins (named for "calcium-dependent adhesion") are a type of cell adhesion molecule (CAM) that is important in the formation of adherens junctions to bind cells with each other. Catenins are a family of proteins found in complexes with cadherin cell adhesion molecules of animal cells: alpha-catenin can bind to β-catenin and can also bind actin. β-catenin binds the cytoplasmic domain of some cadherins. Discover the latest research on cadherins and catenins here.

Adherens Junctions

An adherens junction is defined as a cell junction whose cytoplasmic face is linked to the actin cytoskeleton. They can appear as bands encircling the cell (zonula adherens) or as spots of attachment to the extracellular matrix (adhesion plaques). Adherens junctions uniquely disassemble in uterine epithelial cells to allow the blastocyst to penetrate between epithelial cells. Discover the latest research on adherens junctions here.

Adenomatous Polyposis Coli

Adenomatous polyposis coli is a protein encoded by the APC gene and acts as a tumor suppressor. Discover the latest research on adenomatous polyposis coli here.

© 2021 Meta ULC. All rights reserved