Friday, May 1, 2015, 11:00 am — John Dunn Seminar Room, Bldg. 463
Ca2+ is a ubiquitous intracellular messenger that regulates cellular activities in plants, animals and humans. Cytosolic Ca2+ is kept at a low level, but subcellular organelles such as the endoplasmic reticulum (ER) maintain Ca2+ stores. Under resting conditions, Ca2+ homeostasis is dynamically regulated to equilibrate between active calcium uptake and passive calcium leak. Ca2+ homeostasis is cytoprotective. An overloaded ER Ca2+ content promotes cell death. We determined crystal structures of a Ca2+ leak channel and characterized its biochemical functions. The structure has a novel seven-transmembrane-helix fold consisting of a centralized C-terminal helix wrapped by two triple-helix sandwiches. Lateral displacement of transmembrane helix TM2 by change of pH leaves a transmembrane pore, allowing a leak of Ca2+ across membranes. The leak is regulated by a di-aspartyl pH sensor consisting of two conserved aspartate residues. The leak is intrinsic to all kinds of cells and is cytoprotective for life.
Hosted by: Huilin Li
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