Regulation of Smad activity

Article Abstract:

Regulation of activity of Smads, which have turned out to be a family of transcriptional comodulators that interact with a wide range of DNA-binding proteins to regulate their activity in response to transforming growth factor beta family signaling, is discussed. Topics include the BMP pathway, generation of specific Smad transcriptional responses, regulation of Smad levels and subcellular distribution. How much Smad is in the nucleus is critical and is closely regulated before and after activation by the receptor kinase. Discorveries about how Smad proteins are turned over and how they are moved around in the cell are being made.

Canada, Bones, Genetic aspects, Proteins, Genetic regulation, Genetic transcription, Transcription (Genetics), Cell receptors, Microtubules

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PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts

Article Abstract:

Regulation by protein kinase A (PKA) of phosphorylation binding of FKBP12.6 to the calcium release channel (ryanodine receptor) is discussed relative to defective regulation in human hearts in decline. RyR2 is PKA hyperphosphorylated and that brings defective channel function caused by increased sensitivity to Ca(super.2+)-induced activation.

United States, Calcium channels, Molecular genetics, Heart muscle, Sarcoplasmic reticulum, Myocardium

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SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor

Article Abstract:

The function of the intracellular signaling mediator (Smad) Smad2/Smad3 interacting protein possessing a double zinc finger, or FYVE domain, called Smad anchor for receptor activation (SARA) was investigated. SARA inducted Smad2 into distinct subcellular locations and interacted with the transforming growth factor beta (TGFbeta) receptors. It was discovered that SARA determined a component of the TGFbeta signaling which acted to recruit Smad2 to the receptor mediating the subcellular localization of Smad.

Membrane proteins, Cellular signal transduction

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