Associate Professor, Human Genetics
Rangos 5117, 4401 Penn Ave, Pittsburgh, PA 15224
Primary Phone: 967-147-2407
Web site: http://www.chp.edu/research/areas/genetics/projects/goetzman
2002 University of Alabama-Birmingham, PhD
The Goetzman Lab studies the role of post-translational modifications as regulators of mitochondrial energy metabolism. Lysine is a positively charged amino acid known to play a role in protein:DNA interactions, protein:protein interactions, and protein:lipid interactions. Lysine residues are also important for proper intracellular localization of many proteins. In recent years it has become apparent that lysine residues are subject to a myriad of post-translational modifications such as acetylation, succinylation, malonylation, glutarylation, and sumoylation, to name a few, and these modifications can alter the function of proteins. For example, we have recently shown that an important mitochondrial fatty acid oxidation enzyme known as VLCAD becomes acetylated and succinylated on three lysines that are necessary for mediating binding of VLCAD to cardiolipin on the inner mitochondrial membrane. Acylation at these sites disrupts cardiolipin binding, thereby causing mislocalization of the enzyme to the mitochondrial matrix. Acylation of VLCAD and many other metabolic enzymes can be reversed by lysine deacylases known as sirtuins. Of the seven sirtuin family members, three reside in the mitochondria: SIRT3, SIRT4, and SIRT5. The Goetzman Lab is actively studying the role of these sirtuins in governing mitochondrial function and communication between mitochondria and other organelles.
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