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Components of the mitochondrial cAMP signalosome.
Monterisi, Stefania; Zaccolo, Manuela.
Affiliation
  • Monterisi S; Department of Physiology, Anatomy and Genetics, University of Oxford, Oxford, U.K. stefania.monterisi@dpag.ox.ac.uk.
  • Zaccolo M; Department of Physiology, Anatomy and Genetics, University of Oxford, Oxford, U.K. stefania.monterisi@dpag.ox.ac.uk.
Biochem Soc Trans ; 45(1): 269-274, 2017 02 08.
Article in En | MEDLINE | ID: mdl-28202681
ABSTRACT
3'-5'-Cyclic adenosine monophosphate/protein kinase A (cAMP/PKA) signalling is activated by different extracellular stimuli and mediates many diverse processes within the same cell. It is now well established that in order to translate into the appropriate cellular function multiple extracellular inputs, which may act simultaneously on the same cell, the cAMP/PKA signalling pathway is compartmentalised. Multimolecular complexes are organised at specific subcellular sites to generate spatially confined signalosomes, which include effectors, modulators and targets of the pathway. In recent years, it has become evident that mitochondria represent sites of compartmentalised cAMP signalling. However, the exact location and the molecular composition of distinct mitochondria signalosomes and their function remain largely unknown. In this review, we focus on individual components of the cAMP/PKA signalling pathway at distinct mitochondria subdomains represented by the outer and inner mitochondrial membranes, the intermembrane space and the matrix, highlighting some of the questions that remain unanswered.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Signal Transduction / Cyclic AMP-Dependent Protein Kinases / Cyclic AMP / Mitochondria Limits: Animals / Humans Language: En Journal: Biochem Soc Trans Year: 2017 Document type: Article Affiliation country: United kingdom

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Signal Transduction / Cyclic AMP-Dependent Protein Kinases / Cyclic AMP / Mitochondria Limits: Animals / Humans Language: En Journal: Biochem Soc Trans Year: 2017 Document type: Article Affiliation country: United kingdom