rdf:type |
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lifeskim:mentions |
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pubmed:issue |
35
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pubmed:dateCreated |
2011-8-29
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pubmed:abstractText |
Mitochondria are central organelles in cellular energy metabolism, apoptosis, and aging processes. A signaling network regulating these functions was recently shown to include soluble adenylyl cyclase as a local source of the second messenger cAMP in the mitochondrial matrix. However, a mitochondrial cAMP-degrading phosphodiesterase (PDE) necessary for switching off this cAMP signal has not yet been identified. Here, we describe the identification and characterization of a PDE2A isoform in mitochondria from rodent liver and brain. We find that mitochondrial PDE2A is located in the matrix and that the unique N terminus of PDE2A isoform 2 specifically leads to mitochondrial localization of this isoform. Functional assays show that mitochondrial PDE2A forms a local signaling system with soluble adenylyl cyclase in the matrix, which regulates the activity of the respiratory chain. Our findings complete a cAMP signaling cascade in mitochondria and have implications for understanding the regulation of mitochondrial processes and for their pharmacological modulation.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3',5'-Cyclic-AMP Phosphodiesterases,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic GMP,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic Nucleotide...,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidase K,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PDE2A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Pde2a protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1083-351X
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pubmed:author |
pubmed-author:Acin-PerezRebecaR,
pubmed-author:BuckJochenJ,
pubmed-author:GünnewigKathrinK,
pubmed-author:GertzMelanieM,
pubmed-author:LevinLonny RLR,
pubmed-author:ManfrediGiovanniG,
pubmed-author:RamosLavoisierL,
pubmed-author:RassowJoachimJ,
pubmed-author:RusswurmMichaelM,
pubmed-author:SteegbornClemensC,
pubmed-author:ZoidlGeorgG
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pubmed:issnType |
Electronic
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pubmed:day |
2
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pubmed:volume |
286
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
30423-32
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pubmed:meshHeading |
pubmed-meshheading:21724846-3',5'-Cyclic-AMP Phosphodiesterases,
pubmed-meshheading:21724846-Animals,
pubmed-meshheading:21724846-Brain,
pubmed-meshheading:21724846-Cell Respiration,
pubmed-meshheading:21724846-Cyclic GMP,
pubmed-meshheading:21724846-Cyclic Nucleotide Phosphodiesterases, Type 2,
pubmed-meshheading:21724846-Endopeptidase K,
pubmed-meshheading:21724846-Green Fluorescent Proteins,
pubmed-meshheading:21724846-Humans,
pubmed-meshheading:21724846-Liver,
pubmed-meshheading:21724846-Microscopy, Confocal,
pubmed-meshheading:21724846-Mitochondria,
pubmed-meshheading:21724846-Protein Isoforms,
pubmed-meshheading:21724846-Protein Structure, Tertiary,
pubmed-meshheading:21724846-Rats,
pubmed-meshheading:21724846-Signal Transduction
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pubmed:year |
2011
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pubmed:articleTitle |
A phosphodiesterase 2A isoform localized to mitochondria regulates respiration.
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pubmed:affiliation |
Department of Neurology and Neuroscience, Weill Medical College of Cornell University, New York, New York 10065, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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