Group:MUZIC:Calcineurin
From Proteopedia
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[[Image:Calcineurin1.jpg]] | [[Image:Calcineurin1.jpg]] | ||
== Calcineurin(CnA) == | == Calcineurin(CnA) == | ||
- | This calcium/calmodulin-dependent | + | This calcium/calmodulin-dependent protein serine/threonine phosphate is localized in the nucleus and in the Z-disc of muscle fibers. Its activity is controled by calcium signals that lead to remodeling of skeletal and cardiac muscle in response to physiological and pathological stimuli. In addition to several cytoplasmic substrates, calcineurin dephosphorylates members of the nuclear factor of activated T-cell (NFAT) family of transcription factors, resulting in their nuclear translocation and activation of target genes.<ref>PMID: 11114196</ref> |
- | + | ||
+ | == Structure == | ||
+ | <Structure load='1aui' size='300' frame='true' align='right' caption='Insert caption here' scene='User:Ariadna_Rodriguez-Chamorro/Workbench/Calcineurin/Calcium_dependent_calciuneurin/7'/> | ||
+ | The calcium/calmodulin-dependent phosphatase calcineurin is composed by two chains: chain A which is the catalytic subunit and the B chain confers calcium sensitivity. | ||
Revision as of 08:51, 24 June 2011
Calcineurin(CnA)
This calcium/calmodulin-dependent protein serine/threonine phosphate is localized in the nucleus and in the Z-disc of muscle fibers. Its activity is controled by calcium signals that lead to remodeling of skeletal and cardiac muscle in response to physiological and pathological stimuli. In addition to several cytoplasmic substrates, calcineurin dephosphorylates members of the nuclear factor of activated T-cell (NFAT) family of transcription factors, resulting in their nuclear translocation and activation of target genes.[1]
Structure
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The calcium/calmodulin-dependent phosphatase calcineurin is composed by two chains: chain A which is the catalytic subunit and the B chain confers calcium sensitivity.
References
- ↑ Frey N, Richardson JA, Olson EN. Calsarcins, a novel family of sarcomeric calcineurin-binding proteins. Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14632-7. PMID:11114196 doi:10.1073/pnas.260501097