JUPITER, FL, August 23, 2011 In a joint research effort with researchers at St. Jude Children's Research Hospital, and with help from scientists at The University of Pennsylvania, The University of Minnesota, and the National Institutes of Health, investigators from the Florida campus of The Scripps Research Institute have defined a specific protein complex that allows cells to rid themselves of damaged mitochondria, which are the energy producing machines of the cell.
"This protein complex is already being targeted in cancer therapeutics," said John Cleveland, chair of the Department of Cancer Biology at Scripps Florida, "but now we understand why some of the therapies that target this complex work and this new knowledge will have tremendous impact on both current and potential cancer therapies."
In particular, the study, which appears in the current issue of the journal Molecular Cell, focuses on how the cell uses a process known as autophagythe major recycling center of the cellto remove damaged mitochondria. The autophagy pathway is exploited by many tumors to survive stressful conditions and to remove damaged components.
The Cell under Stress
On a molecular level, the new study focuses on the role of the molecular complex known as "Hsp90-Cdc37 chaperone complex," which orchestrates various aspects of the cellular stress response. Although scientists had known that both the Hsp90-Cdc37 complex and autophagy help maintain the integrity of mitochondria, the exact relationship between Hsp90-Cdc37 and autophagy has not been well understood until the new study.
Hsp90, is a heat-shock protein, one of the cell's most abundant proteins, and assists in everything from protein folding and tumor repression to cell signaling. Cdc37, also a protein, is a co-chaperone to Hsp90 and is involved in cell signal transduction and connecting Hsp90 to the right kinases (kinases add a phosphate group to various molec
|Contact: Eric Sauter|
Scripps Research Institute