David Pagliarini, PhD
Associate Professor, Department of Biochemistry
441B Biochemistry Addition
- Lab Website
- Pagliarini Lab
Mitochondria are complex organelles whose dysfunction underlies a broad spectrum of human diseases. Mitochondria house a wide range of metabolic pathways, and are central to apoptosis, ion homeostasis and reactive oxygen species production. Thus, to maintain cellular homeostasis cells must exert careful control over their mitochondrial composition and function.
How do cells custom-build mitochondria to suit their metabolic needs? What mechanisms do cells leverage to efficiently control mitochondrial processes? Which mitochondrial processes are disrupted in diseases and how might these be targeted therapeutically?
Our lab takes a multi-disciplinary approach to investigating these questions. By integrating classic biochemistry, molecular biology and genetics with large-scale proteomics and systems approaches, we aim to elucidate how cells regulate mitochondrial metabolism and establish a customized mitochondrial infrastructure across tissues and in response to a changing cellular environment. Below are current focuses of our lab.
Honors & Awards
- 2012 Shaw Scientist Award, The Greater Milwaukee Foundation
- 2011 Glenn Award, Glenn Foundation for Medical Research
- 2011 Searle Scholar Award, Kinship Foundation
- 2011 EllisonMedical Foundation New Scholar Award in Aging (declined)
- 2011–Hilldale Undergraduate/Faculty Research Fellowship Awards (4)
- Tagliabracci VS*, Wiley SE*, Guo X, Kinch LN, Durrant E, Wen J, Xiao J, Cui J, Engel JL, Coon JJ, Grishin N, Pinna LA, Pagliarini DJ and Dixon JE, A single kinase generates the majority of the secreted phosphoproteome, Cell, 2015, 18;161(7):16-19-32.
- Overmyer KA, Evans CR, Qi NR, Minogue CV, Chermside-Scaboo CJ, Kock LG, Britton SL, Pagliarini DJ, Coon JJ and Burant CF, Maximal exercise oxidative capacity in male and female rats is driven by skeletal muscle mitochondrial fuel selection and protein acetylation, Cell Metabolism, 2015, 3;21(3):468-78.
- Stefely JA*, Reidenbach AG*, Ulbrich A, Oruganty K, Floyd BJ, Jochem A, Saunders JM, Johnson IE, Minogue CE, Wrobel RL, Barber GE, Lee D, Li S, Kannan N, Coon JJ, Bingman CA and Pagliarini DJ, Mitochondrial ADCK3 employs an atypical protein kinase-like fold to enable ubiquinone biosynthesis, Molecular Cell, 2015, 57: 83-94.
- Lohman DC*, Forouhar F*, Beebe ET, Stefely MS, Minogue CE, Ulbrich A, Stefely JA, Sukumar S, Luna-Sanchez M, Lew S, Seetharaman J, Xiao R, Wang H, Wrobel RL, Everett JK, Mitchell JC, Lopez LC, Coon JJ, Tong L† and Pagliarini DJ†, Mitochondrial COQ9 is a lipid binding protein that associates with COQ7 to enable coenzyme Q biosynthesis, Proceedings of the National Academy of Sciences, 2014, 111(44):E4697-705 (Direct submission)
- Khadria AS, Mueller BK, Stefely JA, Tan CH, Pagliarini DJ† and Senes A†, A Gly-zipper motif mediates homo-dimerization of the transmembrane domain of the mitochondrial kinase ADCK3, Journal of the American Chemical Society, 2014, 136, 14068-77