Scott D. Emr
Professor of Molecular Biology & Genetics
Director, Weill Institute for Cell and Molecular Biology &
Department of Molecular Biology and Genetics

Phone

607-255-0816

Address

Department of Molecular Biology & Genetics
441 Weill Hall
Cornell University
Ithaca, NY 14853-7202

Email

Web Sites

Background

Scott D. Emr is the Frank H.T. Rhodes Professor of Molecular Biology and Genetics at Cornell University. He also is Director of the Weill Institute for Cell and Molecular Biology. He received his Ph.D. degree in Molecular Genetics from Harvard University in 1981.

Prior to joining the faculty at Cornell University, Dr. Emr has held positions at the California Institute of Technology (Assistant and Associate Professor; 1983-1991) and the University of California, San Diego School of Medicine (Distinguished Professor and Investigator in the Howard Hughes Medical Institute; 1991-2007).

Dr. Emr counts among his early honors a Searle Scholars Award and an NSF Presidential Young Investigator Award. He has been elected a member of the National Academy of Sciences, the American Academy of Arts and Sciences and the American Academy of Microbiology. In 2003, he was awarded the Hansen Foundation Gold Medal Prize for “elucidating intracellular sorting and transport pathways”. In 2007, he was awarded the Avanti Prize for his “key contributions in understanding lipid signaling pathways”. Dr. Emr presently serves as a member of the Council for the American Society for Cell Biology and he also serves as a member of the Advisory Board for the Pew Scholars Program in Biomedical Sciences.

Research Description

Dr. Emr’s research focuses on 1) the regulation of cell signaling pathways by phosphoinositide lipids, 2) vesicle-mediated transport reactions required for the secretion of hormones and sorting of lysosomal enzymes and 3) the endocytosis and down-regulation of activated cell surface receptors. The Emr group was the first to demonstrate an essential role for phosphoinositide lipid kinases and phosphatases in the regulation of membrane trafficking pathways. These essential enzymes regulate cell growth, cell shape and cell size. They function to ensure the temporal and spatial specificity of vesicle-mediated transport reactions throughout the cell. Dr. Emr’s lab recently identified the first components (the ESCRT complexes) of a molecular machine required for receptor down-regulation and the budding and release of the HIV virus. more

Publications

Chu, T., J. Sun, S. Saksena and S.D. Emr. 2006. ew component of ESCRT-I regulates endosomal sorting complex assembly. J. Cell BioI., 175: 815-823.

Tabuchi, M., A Audhya, AB. Parsons, C. Boone and S.D. Emr. 2006. The P14,5P2 effectors Sim 1 and SIm2 link calcineurin and sphingolipid signaling pathway. Mol. Cell BioI., 26: 5861-5875.

Kostelansky,M.S., J. Sun, S. Lee, J. Kim, R. Ghirlando, A Hierro, S.D. Emr, and J.H. Hurley. 2006. Structural and functional organization of the ESCRT-I trafficking complex. Cell, 125: 113-126.

Teo, H.• O.J. Gill. J. Sun. O. Perisic. O.B. Veprintsev. Y. Vallis. S.D. Emr and R.L Williams. 2006. Structures of the ESCRT-I core and the ESCRT-II GLUE domain: central role for GLUE domain in direct linking to ESCRT-l, phosphoinositides and ubiquitin. Cell, 125: 99-111.

Obita, T., S. Saksena, S. Ghazi-Tabatabai, D.J. Gill, O. Perisic, S.D. Emr and R.L. Williams. 2007. Structural basis for selective recognition of ESCRT-1I1 by the AAA ATPase Vps4. Nature, 449: 735-739.

Saksena, S., J. Sun, T. Chu and S.D. Emr. 2007. ESCRTing proteins in the endocytic pathway. Trends Biochem. Sci., 32:561-573.

Rue, S.M., S. Mattei, S. Saksena and S.D. Emr. 2008. Novellst-1-Did2 Complex functions at a late step in MVB sorting. Mol. Bioi. Cell, 19: 475-484.

Saksena, S. and S.D. Emr. 2008. Ordered assembly of the ESCRT-III complex on endosomes is required to sequester cargo during MVB formation. Dev. Cell, In Press.

Lin, C.H., JA MacGurn, T. Chu, U. Stefan and S.D. Em'. 2008 Arrestln-related ubiquitin-ligase adaptors regulate endocytosis and turnover of proteins at the cell surface. Cell, In Press.

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