Bosma, W.J.

Eisel, U.L.M.

Elzinga, C.R.S.

Halayko, A.J.

Menzen, M.

Meurs, H.

Nijholt, I.M.

Roscioni, S.S.

Schmidt, M.

English

Dissertations of the University of Groningen

   University of GroningenA Role of AKAP5 in PKA and Epac Mediated PKB/Akt Phosphorylation in the Lung.Bosma, W.J.; Menzen, M.; Roscioni, S.S.; Elzinga, C.R.S.; Nijholt, I.M.; Eisel, U.L.M.;Halayko, A.J.; Meurs, H.; Schmidt, M.Published in:American Journal of Respiratory and Critical Care MedicineIMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite fromit. Please check the document version below.Document VersionPublisher's PDF, also known as Version of recordPublication date:2009Link to publication in University of Groningen/UMCG research databaseCitation for published version (APA):Bosma, W. J., Menzen, M., Roscioni, S. S., Elzinga, C. R. S., Nijholt, I. M., Eisel, U. L. M., Halayko, A. J.,Meurs, H., & Schmidt, M. (2009). A Role of AKAP5 in PKA and Epac Mediated PKB/Akt Phosphorylation inthe Lung. American Journal of Respiratory and Critical Care Medicine, 179(1), A2055-A2055.CopyrightOther than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of theauthor(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons).The publication may also be distributed here under the terms of Article 25fa of the Dutch Copyright Act, indicated by the “Taverne” license.More information can be found on the University of Groningen website: https://www.rug.nl/library/open-access/self-archiving-pure/taverne-amendment.Take-down policyIf you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediatelyand investigate your claim.Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons thenumber of authors shown on this cover page is limited to 10 maximum.Download date: 04-06-2022A62 THE CYTOSKELETON AND CELL CONTRACTILITY / Thematic Poster / Sunday, May 17/8:15 AM−4:00 PM / Area A (SailsPavilion, Upper Level) San Diego Convention CenterA Role of AKAP5 in PKA and Epac Mediated PKB/Akt Phosphorylation in the Lung.W. J. Bosma1,2, M. Menzen1, S. S. Roscioni1, C. R.S. Elzinga1, I. M. Nijholt2, U. L.M. Eisel2, A. J. Halayko3, H. Meurs1 and M.Schmidt1.1Department of Molecular Pharmacology, University of Groningen, Netherlands; 2Department of Molecular Neurobiology,University of Groningen, Netherlands and 3Department of Physiology, University of Manitoba, Winnipeg, Canada.Protein kinase B (PKB)/Akt is a key mediator of cell proliferation, cell survival and metabolism. Disbalance in PKB/Akt signalingoccurs in inflammatory diseases including Alzheimer's dementia and chronic obstructive pulmonary disease.While the strong connection of cAMP−dependent signaling with downstream PKB/Akt is established, the precise nature of thisconnection remains unknown. We reported recently that cAMP−dependent protein kinase (PKA) activation reduced PKB/Aktphosphorylation, whereas activation of Rap−specific exchange proteins directly activated by cAMP (Epac1 and Epac2) enhancedPKB/Akt phosphorylation in murine neurons. We show that PKA, PKB/Akt and Epac2 complex with neuronal A−kinase anchoringprotein5 (AKAP5).After establishing the opposite effects of the two cAMP effectors Epac and PKA on PKB/Akt phosphorylation in murine neurons,we investigated the role of cAMP on PKB/Akt phosphorylation in both HEK293 cells, which are known to exhibit human neuronalsignaling capacities and in human airway smooth muscle (hTERT) cells.Indeed, activation of PKA reduced PKB/Akt phosphorylation, whereas activation of Epac proteins increased PKB/Aktphosphorylation. Again we show that PKA, PKB/Akt and Epac complex with AKAP5. In such multiprotein complexes, differencesin amounts of bound PKA and Epac proteins can modulate PKB/Akt phosphorylation, as shown in our studies with Epac1 andEpac2 specific siRNAs and cell treatment with peptides disrupting PKA anchoring to AKAPs.The involvement of Akt−related phosphatases is currently under investigation. We conclude that AKAP5 acts as a key regulatorbalancing the two cAMP pathways in PKB/Akt phosphorylation in neuronal and lung cells.This abstract is funded by: M. Schmidt is recipient of a Rosalind Franklin Fellowship.Am J Respir Crit Care Med 179;2009:A2055Internet address: www.atsjournals.org Online Abstracts Issue

A role of AKAP5 in PKA and Epac mediated PKB/Akt phosphorylation in the lung

https://pure.rug.nl/ws/files/2676390/2009AmJRespirCritCareMedBosma.pdf

A Role of AKAP5 in PKA and Epac Mediated PKB/Akt Phosphorylation in the Lung.

A Role of AKAP5 in PKA and Epac Mediated PKB/Akt Phosphorylation in the Lung.

Abstract

Similar works

Full text

Available Versions

Dissertations of the University of Groningen