PHS 398 (Rev. 9/04), Biographical Sketch Format Page

advertisement
BIOGRAPHICAL SKETCH
Provide the following information for the key personnel and other significant contributors in the order listed on Form Page 2.
Follow this format for each person. DO NOT EXCEED FOUR PAGES.
NAME
Hughson, Frederick M.
POSITION TITLE
Associate Professor of Molecular Biology
eRA COMMONS USER NAME
fhughson
EDUCATION/TRAINING (Begin with baccalaureate or other initial professional education, such as nursing, and include postdoctoral training.)
DEGREE
(if applicable)
YEAR(s)
Yale University, New Haven, CT
B.S.
1984
Stanford University, Stanford, CA
Ph.D.
1990
Postdoctoral
Fellow
1990-1994
INSTITUTION AND LOCATION
Harvard University, Cambridge, MA
FIELD OF STUDY
Molecular Biophysics &
Biochemistry
Biochemistry
Biochemistry
A. Positions and Honors.
Positions and Employment
1984-1990
Graduate Fellow, Stanford Department of Biochemistry
Robert L. Baldwin, advisor. Research: protein folding.
1990-1994
Postdoctoral Fellow, Harvard Dept. of Biochemistry & Molecular Biology
Don C. Wiley, advisor. Research: X-ray crystal structure of low-pH hemagglutinin.
1994-2002
Assistant Professor of Molecular Biology, Princeton University
2002Associate Professor of Molecular Biology, Princeton University
2006Director, HHMI Undergraduate Science Education Program at Princeton
Honors
1983
1984
1984-1987
1990-1994
1991-1994
1995-1998
1995-1997
20012003-
Sigma Xi
Summa cum laude, Yale University
NSF Predoctoral Fellowship
Helen Hay Whitney Postdoctoral Fellowship
Harvard Board of Tutors
Searle Scholar
Beckman Young Investigator
Member, Faculty of 1000
Editorial Board, PLoS Biology
B. Selected peer-reviewed publications (in chronological order).
1.
2.
3.
4.
5.
6.
Hughson, F.M. and Baldwin, R.L. (1989) Use of site-directed mutagenesis to destabilize native
apomyoglobin relative to folding intermediates. Biochemistry 28, 4415-4422.
Hughson, F.M., Wright, P.E. and Baldwin, R.L. (1990) Structural characterization of a partly folded
apomyoglobin intermediate. Science 249, 1544-1548.
Hughson, F.M., Barrick, D. and Baldwin, R.L. (1991) Probing the stability of a partly folded apomyoglobin
intermediate by site-directed mutagenesis. Biochemistry 30, 4413-4418.
Barrick, D., Hughson, F.M., and Baldwin, R.L. (1994) Molecular mechanisms of acid denaturation: the
role of histidine residues in the partial unfolding of apomyoglobin. J. Mol. Biol. 237, 588-601.
Bullough, P.A., Hughson, F.M., Treharne, A.C., Ruigrok, R.W.H., Skehel, J.J., and Wiley, D.C. (1994)
Crystals of a fragment of influenza haemagglutinin in the low pH induced conformation. J. Mol. Biol. 236,
1262-1265.
Bullough, P.A.*, Hughson, F.M.*, Skehel, J.J., and Wiley, D.C. (1994) The structure of influenza
haemagglutinin at the pH of membrane fusion. Nature 371, 37-43. *Authors contributed equally.
7.
8.
9.
10.
11.
12.
13.
14.
15.
16.
17.
18.
19.
20.
21.
22.
23.
24.
25.
26.
27.
28.
29.
30.
Hughson, F.M. (1995) Structural characterization of viral fusion proteins [review]. Curr. Biol. 5, 265-274.
Hughson, F.M. (1995) Molecular mechanisms of protein-mediated membrane fusion [review]. Curr. Opin.
Struct. Biol. 5, 507-513.
Chen, J., Wharton, S.A., Weissenhorn, W., Calder, L.J., Hughson, F.M., Skehel, J.J., and Wiley, D.C.
(1995) A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds
in Escherichia coli into the low-pH-induced conformation. Proc. Natl. Acad. Sci. USA 92, 12205-12209.
Hughson, F.M. (1997) Enveloped viruses: a common mode of membrane fusion? [review]. Curr. Biol. 7,
R565-R569.
Nicholson, K.L., Munson, M., Miller, R.B., Filip, T.J., Fairman, R., and Hughson, F.M. (1998) Regulation
of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p. Nature Struct. Biol. 5,
793-802.
Hughson, F.M. (1999) Membrane fusion: structure snared at last [review]. Curr. Biol. 9, R49-R52.
Carr, C.M., Grote, E., Munson, M., Hughson, F.M., and Novick, P.J. (1999) Sec1p binds to SNARE
complexes and concentrates at sites of secretion. J. Cell Biol. 146, 333-344.
Lerman, J.C., Robblee, J., Fairman, R., and Hughson, F.M. (2000) Structural analysis of the neuronal
SNARE protein syntaxin-1A. Biochemistry 39, 8470-8479.
Waters, M.G. and Hughson, F.M. (2000) Membrane tethering and fusion in the secretory and endocytic
pathways [review]. Traffic 1, 588-597.
Munson, M., Chen, X., Cocina, A.E., Schultz, S.M., and Hughson, F.M. (2000) Interactions within the
yeast t-SNARE Sso1p that control SNARE complex assembly. Nature Struct. Biol. 7, 894-902.
Chen, X., Schauder, S., Potier, N., Van Dorsselaer, A., Pelczer, I., Bassler, B.L., and Hughson, F.M.
(2002) Structural identification of a bacterial quorum sensing signal containing boron. Nature 415, 545549.
Barrick, D. and Hughson, F.M. (2002) Irreversible assembly of membrane fusion machines [News &
Views]. Nature Struct. Biol. 9, 78-80.
Munson, M. and Hughson, F.M. (2002) Conformational regulation of SNARE assembly and disassembly
in vivo. J. Biol. Chem. 277, 9375-9381.
Ungar, D. and Hughson, F.M. (2003) SNARE protein structure and function [review]. Ann. Rev. Cell
Devel. Biol. 19, 493-517.
Zweifel, M.E., Leahy, D.J., Hughson, F.M., and Barrick, D. (2003) Structure and stability of the ankyrin
domain of the Drosophila Notch receptor. Protein Science 12, 2622-2632.
Oka, T., Ungar, D., Hughson, F.M., and Krieger, M. (2004) The COG and COPI complexes interact to
control the abundance of GEARs, a subset of Golgi integral membrane proteins. Mol. Biol. Cell 15, 24232435.
Miller, S.T., Xavier, K.B., Campagna, S.R., Taga, M.E., Semmelhack, M.F., Bassler, B.L., and Hughson,
F.M. (2004) Salmonella typhimurium recognizes a chemically distinct form of the bacterial quorum
sensing signal AI-2. Mol. Cell 15, 677-687.
Neiditch, M.B., Federle, M.J., Miller, S.T., Bassler, B.L., and Hughson, F.M. (2005) Regulation of LuxPQ
receptor activity by the quorum-sensing signal autoinducer-2. Mol. Cell 18, 507-518.
Ungar, D., Oka, T., Vasile, E., Krieger, M., and Hughson, F.M. (2005) Subunit architecture of the
conserved oligomeric Golgi complex. J. Biol. Chem. 280, 32729-32735.
Oka, T., Vasile, E., Penman, M., Novina, C.D., Dykxhoorn, D.M., Ungar, D., Hughson, F.M., Krieger, M.
(2005) Genetic analysis of the subunit organization and function of the COG complex: Studies of Cog5
and Cog7 deficient mammalian cells. J. Biol. Chem. 280, 32736-32745.
Ungar, D., Oka, T., Krieger, M., and Hughson, F.M. (2006) Retrograde transport on the COG railway
[review]. Trends Cell Biol., 16, 113-120.
Neiditch, M.B., Federle, M.J., Pompeani, A.J., Kelly, R.C., Swem, D.L., Jeffrey, P.D., Bassler, B.L., and
Hughson, F.M. (2006) Ligand-induced asymmetry in histidine sensor kinase complex regulates quorum
sensing. Cell 126, 1095-1108.
Togneri, J., Cheng, Y.S., Munson, M., Hughson, F.M., and Carr, C.M. (2006) SNARE complex binding
mode of the Sec1/Munc-18 protein, Sec1p. Proc. Natl. Acad. Sci. USA 103, 17730-17735.
Cavanaugh, L.F., Chen, X., Richardson, B.C., Ungar, D., Pelczer, I., Rizo, J., Hughson, F.M. (2007)
Structural analysis of conserved oligomeric golgi complex subunit 2. J. Biol. Chem. 282, 23418-23426.
31.
32.
Neiditch, M.B., Hughson, F.M. (2007) The regulation of histidine sensor kinase complexes by quorum
sensing signal molecules. Methods Enzymol. 423, 250-263.
Hughson, F.M. (2008) Both layers of the COPII coat come into view [review]. Cell 134, 384-385.
C. Research Support
Ongoing Research Support
R01 AI054442
Hughson (PI)
3/1/2003 - 2/29/2013
NIH - NIAID
Structure-Function Analysis of AI-2 Quorum Sensing
This project is focused on studies of bacterial signaling via AI-2 and CAI-1. Goals are mechanistic studies of
LuxPQ as a model for two-component signaling; discovery and mechanistic studies of LuxPQ antagonists and
agonists; determination of the mechanism of CAI-1 synthesis; and studies of the recognition and transduction
of the CAI-1 signal. Co-investigators are Bonnie Bassler and Martin Semmelhack, both at Princeton
University.
R01 GM071574 Hughson (PI)
3/1/2005 - 2/28/2009
NIH - NIGMS
Structural Analysis of Golgi Trafficking Proteins
This project is focused on elucidating the overall architecture of the conserved oligomeric Golgi (COG)
complex, identifying COG-interacting proteins, determining the structure of the yeast Cog2 subunit, and
determining the structures of other COG subunits as well as larger subassemblies.
Completed Research Support
AHA 0355657T Hughson (PI)
7/1/2003 – 6/30/2006
American Heart Association Heritage Affiliate Grant-In-Aid
Structure of Yeast Cog2p
The main goal of this grant was to use NMR spectroscopy to initiate characterization of yeast Cog2 protein.
Download