Skip to main content

GENERAL COMMENTARY article

Front. Pharmacol., 24 September 2015
Sec. Experimental Pharmacology and Drug Discovery
Volume 6 - 2015 | https://doi.org/10.3389/fphar.2015.00214
This article is part of the Research Topic Frontiers in the Pharmacological Manipulation of Intracellular cAMP Levels View all 18 articles

Corrigendum: Impact of kinase activating and inactivating patient mutations on binary PKA interactions

This article is a commentary on:

  1. Impact of kinase activating and inactivating patient mutations on binary PKA interactions

    1. Read original article
\r\nRuth RckRuth RöckJohanna E. MayrhoferJohanna E. MayrhoferVerena BachmannVerena BachmannEduard Stefan*Eduard Stefan*
  • Institute of Biochemistry and Center for Molecular Biosciences, University of Innsbruck, Innsbruck, Austria

A corrigendum on
Impact of kinase activating and inactivating patient mutations on binary PKA interactions

by Röck, R., Mayrhofer, J. E., Bachmann, V., and Stefan, E. (2015). Front. Pharmacol. 6:170. doi: 10.3389/fphar.2015.00170

Reason for Corrigendum:

There was a mistake in the figure legend for Figure 5 as published. The correct version of the figure legend (Figure 5B) appears below. The authors apologize for the mistake. This error does not change the scientific conclusions of the article in any way.

Figure 5. Impact of RIa mutations and cAMP elevation on PKA type I complexes. … (B) Following indicated modifications of RIa-F[1] sequences, combinations of wild type and mutant Rluc PCA tagged PKA subunits have been subjected to Rluc PCA measurements. The effect of isoproterenol (1 μM, 10 min; 48 h transient PCA reporter expression) on PKA complex formation has been determined (at least n = 3 independent experiments, ±SEM).

The original article was updated.

Conflict of Interest Statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Keywords: molecular interactions, patient mutations, cAMP-dependent protein kinase A, protein-fragment complementation assay, GPCR, Carney complex, Acrodysostosis

Citation: Röck R, Mayrhofer JE, Bachmann V and Stefan E (2015) Corrigendum: Impact of kinase activating and inactivating patient mutations on binary PKA interactions. Front. Pharmacol. 6:214. doi: 10.3389/fphar.2015.00214

Received: 09 September 2015; Accepted: 14 September 2015;
Published: 24 September 2015.

Edited and reviewed by: Apostolos Zarros, University of Glasgow, UK

Copyright © 2015 Röck, Mayrhofer, Bachmann and Stefan. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

*Correspondence: Eduard Stefan, eduard.stefan@uibk.ac.at

Disclaimer: All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.