| Mitochondria are essential cellular organelles that produce most of the cell's energy. In addition, studies have found that mitochondria are key organelles controlling cellular redox state, Ca2+ homeostasis, and apoptosis. Mitochondria are dynamic organelles undergoing frequent fission, fusion and translocation. Proper control of this dynamic process is essential as perturbation of normal mitochondrial morphology leads to the loss of mitochondrial function and subsequent cell death. Accumulation of dysfunctional mitochondria in human tissues is one of the leading causes of human diseases including myopathy, cardiomyopathy, neurodegeneration, blindness, deafness, diabetes, and aging.
My laboratory currently focuses on how cells control mitochondrial shape and number. We have been studying proteins involved in mitochondrial fission and fusion. We identified two mammalian proteins hFis1 and the dynamin-like protein DLP1 that mediate membrane scission during mitochondrial division. Our studies indicate that hFis1 functions as a receptor molecule on the mitochondrial surface to recruit the cytosolic protein DLP1. Because normal mitochondrial morphology is maintained by balance between fission and fusion, these processes are believed to be regulated temporally and spatially. Our hypothesis is that signals from inside and/or outside of mitochondria regulate DLP1 and hFis1 to control the fission reaction. We are testing whether Ca2+-, ATP-, and growth factor-mediated signals control mitochondrial morphology. All these studies utilize cell and molecular biological approaches including digital imaging, immunological methods, DNA manipulations, and standard biochemical techniques.
Extensive research that led to the discovery of metabolic pathways that generate cellular energy some 50 years ago culminated in the award of a Nobel Prize. Now, mitochondrial research pinnacles one more time through their implication in cell death, many human diseases, and aging. Studying mitochondrial morphology is certainly an exciting field because of its ability to dictate mitochondrial function. |
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Brookes, P.S., Y. Yoon, J.L. Robotham, M.W. Anders, and S-.S. Sheu. 2004. Calcium, ATP, and ROS: a mitochondrial love-hate triangle. Am. J. Physiol.-Cell Physiol. 287: C817-C833.
Yoon, Y. 2004. Sharpening the scissors: mitochondrial fission with aid. Cell Biochem. Biophys. 41: 193-205.
Pitts, K.R., M.A. McNiven, and Y. Yoon. 2004. Mitochondria-specific function of the dynamin family protein DLP1 is mediated by its C-terminal domains. J. Biol. Chem. 279: 50286-50294.
Yoon, Y. 2005. Regulation of mitochondrial dynamics: Another process modulated by Ca2+ signal? Sci. STKE 2005, pe18.
Kong, D., L. Xu, Y. Yu, W. Zhu, D.W. Andrews, Y. Yoon, and T. Kuo. 2005. Regulation of Ca2+-induced permeability transition by Bcl-2 is antagonized by Drp1 and hFis1. Mol. Cell. Biochem. 272: 187-199.
Yu, T., R.J. Fox, L.S. Burwell, and Y. Yoon. 2005. Regulation of mitochondrial fission and apoptosis by the mitochondrial outer membrane protein hFis1. J. Cell Sci. 118: 4141-4151.
Koch, A., Y. Yoon, N.A. Bonekamp, M.A. McNiven, and M. Schrader. 2005. A role for Fis1 in both mitochondrial and peroxisomal fission in mammalian cells. Mol. Biol. Cell. 16: 5077-5086.
Yu, T., J.L. Robotham, and Y. Yoon. 2006. Increased production of reactive oxygen species in hyperglycemic conditions requires dynamic changes of mitochondrial morphology. Proc. Natl. Acad. Sci. USA. 103: 2653-2658.
Hom, J.R., J.S. Gewandter, L. Michael, S-.S. Sheu, Y. Yoon. 2007. Thapsigargin induces biphasic fragmentation of mitochondria through calcium-mediated mitochondrial fission and apoptosis. J. Cell. Physiol. 212: 498-508.
Huang, P., T. Yu, Y. Yoon. 2007. Mitochondrial clustering induced by overexpression of the mitochondrial fusion protein Mfn2 causes mitochondrial dysfunction and cell death. Eur. J. Cell Biol. 86: 289-302.
Schrader, M. and Y. Yoon. 2007. Mitochondria and peroxisomes: are the ‘Big Brother’ and the ‘Little Sister’ closer than assumed? BioEssays. 29: 1105-1114.
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