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Biological sciences

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The immunophilin FKBP12 functions as a common inhibitor of the TGFbeta family type I receptors

Article Abstract:

Previous research has failed to explain the physiological roles played by the immunophilin FKBP12, an evolutionarily conserved abundant protein. Experiments are performed to determine the protein's physiological roles. Results indicate that FKBP12 inhibits the signaling pathways mediated by the transforming growth factor (TGF) beta receptor. Furthermore, in the presence of ligand, FKBP12 is released when the TGB beta type II receptor phosphorylates the type I receptor, indicating that the protein is essential for the activation of type I receptors.

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The MAD-related protein Smad7 associates with the TGFbeta receptor and functions as an antagonist of TGFbeta signaling

Article Abstract:

The expression of Smad7 in TGFbeta-responsive cells' role in ligand-dependent signaling was analyzed to determine its effectiveness in blocking the access and phosphorylation and interaction with TGFbeta. Results show that the MAD-related protein Smad7 associates with the TGFbeta receptor and works as an antagonist of TGFbeta signaling. Furthermore, Smad7 mutations hinder receptor binding which consequently disrupts inhibitory activity.

Proteins, Cellular signal transduction

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X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex

Article Abstract:

The X-ray structure of the ternary complex of a calcineurin A, calcineurin B, FKBP12, and the FK506 has been determined and observed that immunophilin-immunosuppressant FKBP12-FK506 complex inhibit the dephosphorylation of the phosphatase active site on calcineurin A. The ternary complex represents the 3D structure of a Ser/Thr protein phosphatase.

Analysis, Phosphatases, Inhibition, Inhibition (Psychology), FK 506

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