Nature Communications (Oct 2016)
Bimodal antagonism of PKA signalling by ARHGAP36
- Rebecca L. Eccles,
- Maciej T. Czajkowski,
- Carolin Barth,
- Paul Markus Müller,
- Erik McShane,
- Stephan Grunwald,
- Patrick Beaudette,
- Nora Mecklenburg,
- Rudolf Volkmer,
- Kerstin Zühlke,
- Gunnar Dittmar,
- Matthias Selbach,
- Annette Hammes,
- Oliver Daumke,
- Enno Klussmann,
- Sylvie Urbé,
- Oliver Rocks
Affiliations
- Rebecca L. Eccles
- Max-Delbrück-Center for Molecular Medicine
- Maciej T. Czajkowski
- Max-Delbrück-Center for Molecular Medicine
- Carolin Barth
- Max-Delbrück-Center for Molecular Medicine
- Paul Markus Müller
- Max-Delbrück-Center for Molecular Medicine
- Erik McShane
- Max-Delbrück-Center for Molecular Medicine
- Stephan Grunwald
- Max-Delbrück-Center for Molecular Medicine
- Patrick Beaudette
- Max-Delbrück-Center for Molecular Medicine
- Nora Mecklenburg
- Max-Delbrück-Center for Molecular Medicine
- Rudolf Volkmer
- Leibniz-Institut für Molekulare Pharmakologie
- Kerstin Zühlke
- Max-Delbrück-Center for Molecular Medicine
- Gunnar Dittmar
- Max-Delbrück-Center for Molecular Medicine
- Matthias Selbach
- Max-Delbrück-Center for Molecular Medicine
- Annette Hammes
- Max-Delbrück-Center for Molecular Medicine
- Oliver Daumke
- Max-Delbrück-Center for Molecular Medicine
- Enno Klussmann
- Max-Delbrück-Center for Molecular Medicine
- Sylvie Urbé
- Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool
- Oliver Rocks
- Max-Delbrück-Center for Molecular Medicine
- DOI
- https://doi.org/10.1038/ncomms12963
- Journal volume & issue
-
Vol. 7,
no. 1
pp. 1 – 16
Abstract
Protein kinase A (PKA) is a key mediator of cyclic AMP signalling. Here, Eccles et al. show that ARHGAP36 antagonizes PKA by acting as a kinase inhibitor and targeting the catalytic subunit for endolysosomal degradation, thus reducing sensitivity of cells to cAMP and promoting Hedgehog signalling.
