The eight research groups have established a wide spectrum of modern of skeletal muscle. Action potentials spreading along the transverse techniques such as i) biochemical identification and purification of proteins, ii) cloning, sequencing, site directed mutagenesis, and tubular membrane into the cell interior cause a conformational change of expression of genes, iii) immunocytochemical identification of proteins, the voltage-sensitive dihydropyridine receptors (DHPR) embedded in this iv) ultrastructural localisation of proteins, v) functional membrane. It is by a complex and not yet understood process that activated characterisation of proteins in pharmacological binding assays, vi) DHPR triggers the release of Ca2+ from internal Ca2+ stores, the characterisation of heterologously expressed or reconstituted channel sarcoplasmic reticulum (SR). Ca2+ is conducted by the ryanodine receptor (RyR) situated in the SR membrane into the cytoplasma where it activates proteins by patch and bilayer clamping.
the contractile apparatus. More than 10 proteins associated with DHPR and RyR, such as triadin, FKBP12, calsequestrin and several not yet identified proteins are required for functional EC coupling.
Here, eight experienced research groups will employ an integrated and multi-disciplinary approach to characterise known and novel proteins of the DHPR/RyR complex and their relationships. The major objective comprises the expression of normal and recombinant known proteins, the identification, isolation and expression of novel proteins, and the analysis of their interactions at structural and functional levels. This project will significantly advance our understanding of the role of the proteins involved in EC coupling.
Funding Schemeundefined - undefined