Literature DB >> 11807172

AKAP mediated signal transduction.

Jennifer J Carlisle Michel1, John D Scott.   

Abstract

Compartmentalization of cyclic AMP-dependent protein kinase (PKA) is achieved through association with A-kinase anchoring proteins (AKAPs). AKAPs are a group of structurally diverse proteins with the common function of binding to the regulatory subunit of PKA and confining the holoenzyme to discrete locations within the cell. This mode of regulation ensures that PKA is exposed to isolated cAMP gradients, which allows for efficient catalytic activation and accurate substrate selection. Several AKAPs coordinate multiple members of signaling cascades, effectively assembling upstream activators and downstream effectors within the same macromolecular complex. Consequently, AKAPs may serve as points of integration for numerous signaling pathways. This review details the most recent advances in our understanding of the various biological functions dependent upon AKAP-anchored signaling complexes.

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Year:  2002        PMID: 11807172     DOI: 10.1146/annurev.pharmtox.42.083101.135801

Source DB:  PubMed          Journal:  Annu Rev Pharmacol Toxicol        ISSN: 0362-1642            Impact factor:   13.820


  92 in total

1.  Regulation of cardiac inward rectifier potassium current (I(K1)) by synapse-associated protein-97.

Authors:  Ravi Vaidyanathan; Steven M Taffet; Karen L Vikstrom; Justus M B Anumonwo
Journal:  J Biol Chem       Date:  2010-06-08       Impact factor: 5.157

Review 2.  Protein kinase CK2: structure, regulation and role in cellular decisions of life and death.

Authors:  David W Litchfield
Journal:  Biochem J       Date:  2003-01-01       Impact factor: 3.857

Review 3.  AKAPs (A-kinase anchoring proteins) and molecules that compose their G-protein-coupled receptor signalling complexes.

Authors:  Craig C Malbon; Jiangchuan Tao; Hsien-yu Wang
Journal:  Biochem J       Date:  2004-04-01       Impact factor: 3.857

Review 4.  Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm.

Authors:  Alexandra C Newton
Journal:  Biochem J       Date:  2003-03-01       Impact factor: 3.857

Review 5.  The evolving role of lipid rafts and caveolae in G protein-coupled receptor signaling: implications for molecular pharmacology.

Authors:  Rennolds S Ostrom; Paul A Insel
Journal:  Br J Pharmacol       Date:  2004-08-02       Impact factor: 8.739

6.  Sperm-specific protein kinase A catalytic subunit Calpha2 orchestrates cAMP signaling for male fertility.

Authors:  Michael A Nolan; Donner F Babcock; Gunther Wennemuth; William Brown; Kimberly A Burton; G Stanley McKnight
Journal:  Proc Natl Acad Sci U S A       Date:  2004-08-31       Impact factor: 11.205

7.  The two regulatory subunits of aplysia cAMP-dependent protein kinase mediate distinct functions in producing synaptic plasticity.

Authors:  Jinming Liu; Jiang-Yuan Hu; Samuel Schacher; James H Schwartz
Journal:  J Neurosci       Date:  2004-03-10       Impact factor: 6.167

8.  Optic atrophy 1 is an A-kinase anchoring protein on lipid droplets that mediates adrenergic control of lipolysis.

Authors:  Guillaume Pidoux; Oliwia Witczak; Elisabeth Jarnæss; Linda Myrvold; Henning Urlaub; Anne Jorunn Stokka; Thomas Küntziger; Kjetil Taskén
Journal:  EMBO J       Date:  2011-10-07       Impact factor: 11.598

9.  Targeted disruption of PDE3B, but not PDE3A, protects murine heart from ischemia/reperfusion injury.

Authors:  Youn Wook Chung; Claudia Lagranha; Yong Chen; Junhui Sun; Guang Tong; Steven C Hockman; Faiyaz Ahmad; Shervin G Esfahani; Dahae H Bae; Nazari Polidovitch; Jian Wu; Dong Keun Rhee; Beom Seob Lee; Marjan Gucek; Mathew P Daniels; Christine A Brantner; Peter H Backx; Elizabeth Murphy; Vincent C Manganiello
Journal:  Proc Natl Acad Sci U S A       Date:  2015-04-15       Impact factor: 11.205

10.  Mechanism for targeting the A-kinase anchoring protein AKAP18δ to the membrane.

Authors:  Andreas Horner; Frank Goetz; Robert Tampé; Enno Klussmann; Peter Pohl
Journal:  J Biol Chem       Date:  2012-10-24       Impact factor: 5.157

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