Inactivation of the sarcoplasmic reticulum calcium channel by protein kinase

Article Abstract:

The calcium ion channel which allows calcium to move from the sarcoplasmic reticulum (SR) lumen into the cytoplasm during muscle activation can be blocked by calcium itself, suggesting that the calcium release process is controlled by a negative feedback mechanism. Protein phosphorylation can occur under the same conditions that permit inactivation of the ryanodine/calcium channel of skeletal muscle SR. An endogenous protein kinase may regulate channel gating and be closely associated with the ryanodine receptor protein.

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The G-protein-gated atrial K+ channel I(KACh) is a heteromultimer of two inwardly rectifying K(+)-channel proteins

Article Abstract:

The structure of the native I(KACh), an inward rectifier of the potassium ion channel family, is found to be made up of two homologus subunits with GIRK1 and CIR gene products. The structure of the I(KACh) is determined by the use of antibodies specific to the encoding regions of the rectifier. The I(KACh) structure will enable the study at the process of regulation of the G proteins.

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Tyrosine-kinase-dependent recruitment of RGS12 to the N-type calcium channel

Article Abstract:

Research into the G-protein RGS12 shows that it is multi-functional and able to directly interact with the tyrosine-phosphorylated calcium channel via its PTB domain.

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