How is mitochondrial architecture controlled in healthy and dying cells?We are an interdisciplinary team seeking to understand how membrane architecture is achieved and regulated by proteins. We approach this question by using the mitochondria as a model system and study proteins that regulate mitochondrial membrane architecture in healthy and dying cells. Currently we are focused on proteins involved in mitochondrial fission and fusion as well as proteins that interact with mitochondria during apoptosis. Our work contributes to understanding the basic biology, chemistry, and physics of protein-protein and protein-membrane interactions that underlie these signalling pathways and are important in human disease. We strive for an understanding that will identify new therapeutic routes and will also allow synthetic biology applications such as the the rational control of membrane architecture in the design of novel nanodevices. To accomplish these goals, we use a wide range of tools to address these questions including cell biological, biochemical, and biophysical assays including NMR spectroscopy and x-ray crystallography for protein structure determination. Please visit our lab website for more information: https://sites.google.com/site/hillbiologylab/SELECTED PUBLICATIONSPicton LK, Casares S, Monahan AC, Majumdar A, Hill RB. Evidence for conformational heterogeneity of fission protein Fis1 from Saccharomyces cerevisiae. Biochemistry. 2009 Jul 21;48(28):6598-609. PubMed PMID: 19522466. F.J. Tan, J.E. Zuckerman, A.Z. Fire, and R.B. Hill. 2007. Regulation of apoptosis by C. elegans CED-9 in the absence of the C-terminal transmembrane domain. Cell Death Differ . 14:1925-35. R.C. Wells, L.K. Picton, S.C.P. Williams, F.J. Tan, and R.B. Hill. 2007. Direct binding of the dynamin-like GTPase, Dnm1, to mitochondrial dynamics protein Fis1 is negatively regulated by the Fis1 N-terminal arm. J Mol Biol. 359(4):1045-58. EpubApr 6. G.R. Thuduppathy, O. Terrones, J. W. Craig, G. Basañez, and R.B. Hill. 2006. The N-terminal domain of Bcl-xL reversibly binds membranes in a pH-dependent manner. J Biochemistry. 45:14533-42. Thuduppathy GR, Craig JW, Kholodenko V, Schon A, Hill RB. 2006. Evidence that membrane insertion of the cytosolic domain of Bcl-xL is governed by an electrostatic mechanism. J Mol Biol. 359(4):1045-58. EpubApr 6. Team Protein (aka Lab Members) Graduate Students: Undergraduate Students:
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