Distinct functionality of dishevelled isoforms on Ca2+/calmodulin-dependent protein kinase 2 (CamKII) in Xenopus gastrulation.

Gentzel M, Schille C, Rauschenberger V, Schambony A (2015)

Publication Type: Journal article, Original article

Subtype: other

Publication year: 2015

Journal

Molecular Biology of the Cell American Society for Cell Biology

Book Volume: 26

Pages Range: 966-977

Journal Issue: 5

URI: http://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25568338&retmode=ref&cmd=prlinks

DOI: 10.1091/mbc.E14-06-1089

Abstract

Wnt ligands trigger the activation of a variety of β-catenin-dependent and β-catenin-independent intracellular signaling cascades. Despite the variations in intracellular signaling, Wnt pathways share the effector proteins frizzled, dishevelled, and β-arrestin. It is unclear how the specific activation of individual branches and the integration of multiple signals are achieved. We hypothesized that the composition of dishevelled-β-arrestin protein complexes contributes to signal specificity and identified CamKII as an interaction partner of the dishevelled-β-arrestin protein complex by quantitative functional proteomics. Specifically, we found that CamKII isoforms interact differentially with the three vertebrate dishevelled proteins. Dvl1 is required for the activation of CamKII and PKC in the Wnt/Ca(2+) pathway. However, CamKII interacts with Dvl2 but not with Dvl1, and Dvl2 is necessary to mediate CamKII function downstream of Dvl1 in convergent extension movements in Xenopus gastrulation. Our findings indicate that the different Dvl proteins and the composition of dishevelled-β-arrestin protein complexes contribute to the specific activation of individual branches of Wnt signaling.

Authors with CRIS profile

Carolin Schille Lehrstuhl für Entwicklungsbiologie Verena Rauschenberger Lehrstuhl für Entwicklungsbiologie Alexandra Schambony Lehrstuhl für Entwicklungsbiologie

Involved external institutions

Max-Planck-Institut für molekulare Zellbiologie und Genetik / Max Planck Institute of Molecular Cell Biology and Genetics (MPI-CBG) DE Germany (DE)

How to cite

APA:

Gentzel, M., Schille, C., Rauschenberger, V., & Schambony, A. (2015). Distinct functionality of dishevelled isoforms on Ca2+/calmodulin-dependent protein kinase 2 (CamKII) in Xenopus gastrulation. Molecular Biology of the Cell, 26(5), 966-977. https://dx.doi.org/10.1091/mbc.E14-06-1089

MLA:

Gentzel, Marc, et al. "Distinct functionality of dishevelled isoforms on Ca2+/calmodulin-dependent protein kinase 2 (CamKII) in Xenopus gastrulation." Molecular Biology of the Cell 26.5 (2015): 966-977.

BibTeX: Download