(PhD - Technical University, Berlin)
120 Mason Farm Road, CB# 7260
3047 Genetic Medicine Building
Chapel Hill, NC 27599-7260
HONORS & AWARDS
- NIH MERIT Award: 2010
- Fellow of the Biophysical Society: 1999
- NIH MERIT Award: 1990
- Established Investigator of American Heart Association: 1972
The laboratory’s research focuses on defining the molecular basis of Ca2+ release channel/ryanodine receptor (RyR1) function in skeletal muscle. RyR1s are 2,200 kDa ion channels that release Ca2+ ions in response to an action potential from the sarcoplasmic reticulum, an intracellular Ca2+-storing compartment in skeletal muscle. In our studies, we use mutagenesis, Ca2+ imaging and single channel measurements to determine the molecular mechanisms underlying RyR1 function. As our studies progress we expect to gain new insights in the complex mechanisms of RyR1 channel ion conductance and selectivity, and gating by its multiple ligands, and how these processes are altered by mutations in RyR1 linked to muscle diseases such as central core disease and malignant hyperthermia.
- Mei Y, Xu L, Mowrey DD, Mendez Giraldez R, Wang Y, Pasek DA, Dokholyan NV, Meissner G. Channel gating dependence on pore lining helix glycine residues in skeletal muscle ryanodine receptor. J Biol Chem (2015) 290, 17535-17545.
- Xu L, Wang Y, Yamaguchi N, Pasek DA, Meissner G. Single channel properties of heterotetrameric mutant RyR1 ion channels linked to core myopathies. J Biol Chem (2008) 283:6321-6329.
- Xu L, Wang Y, Gillespie D, Meissner G. Two rings of negative charges in the cytosolic vestibule of type-1 ryanodine receptor modulate ion fluxes. Biophys J (2006) 90:443-453.
- Eu JP, Sun J, Xu L, Stamler JS, Meissner G: The skeletal muscle calcium release channel: coupled O2 sensor and NO signaling functions. Cell (2000) 102:499-509.
- Lai FA, Erickson HP, Rousseau E, Liu QY, Meissner G: Purification and reconstitution of the calcium release channel from skeletal muscle. Nature (1988) 331:315-319.