Biochemistry

E-mail: shaw@biochem.utah.edu
Address: 14 N. Medical Drive, Rm 4100
Phone: 585-6205

Mitochondrial Fusion

The Fzo1p GTPase is embedded in the outer mitochondrial membrane and mediates mitochondrial fusion.  Work from our lab and others indicates that Fzo1p forms a complex with itself and two additional proteins, Mgm1p and Ugo1p.  Interest in mitochondrial fusion has been stimulated by the finding that mutations in the human homologs of Mgm1p and Fzo1p cause neurological diseases including dominant optic atrophy and Charcot-Marie-Tooth Syndrome.  We collaborate with researchers in Human Genetics at the University of Utah to better understand why defects in mitochondrial fusion cause these disorders in humans. We also use yeast as a simple model system to study how these mutations affect mitofusin function.

Potential Project: Although Mgm1p is required for mitochondrial fusion, like Dnm1p, it is a dynamin-related GTPase. How a dynamin related protein participates in fusion is not understood. We recently obtained a bacterially expressed form of yeast Mgm1p that is soluble. This protein can now be purified allowing its GTPase, assembly and membrane interaction properties to be examined in vitro.

1/2008