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Dr. Yu-Ling Shih
Associate Research Fellow
Room 702, Institute of Biological Chemistry, Academia Sinica
128, Academia Road Sec. 2, Nankang, Taipei 115, Taiwan
TEL: +886-2-2785-5696 ext. 7020
FAX: +886-2-2788-9759

Our laboratory studies cell division and the cytoskeleton of bacteria. We are particularly interested in the protein-membrane interactions underlying the cell division process. The current projects are described below.

(1) The Min system and membrane localization of proteins
        The Min system regulates the cell division site placement in Escherichia coli. The Min system consists of three proteins, MinC, MinD, and MinE, that associate with the membrane and oscillate between two cell poles over the cell cycle. The oscillation establishes a concentration gradient of the division inhibition at both poles, thus facilitating division from the middle of the cell. MinD and MinE can self-assemble on the membrane and further organize into dynamic mesoscale patterns in the presence of ATP. Our laboratory has investigated the biochemical basis of protein self-assembly on the membrane and protein-membrane interaction that drives the process.
        In addition to the division site placement, we recently discovered that the Min system could affect membrane localization of proteins. We hypothesize that Min oscillation may be involved in maintaining homeostasis of the inner membrane proteins. We expect to gain further insights in the near future.

(2) Studying protein-membrane interaction using the membrane-mimetic system
        We have used the membrane-mimetic system to study the MinE-membrane interaction in our previous works. The approach allowed for characterization of the fine structures down to nanoscale resolution and provided spatial and temporal information about the protein-membrane interaction under a defined biochemical environment. We established a collaboration to develop a membrane-mimetic platform for separation and detection of membrane proteins with different membrane-anchoring motifs, aimed at studying the behavior of membrane proteins under their native environment.

(3) Bacterial physiology and antibiotic resistance
        Bacterial physiology is the basis for understanding antibiotic resistance, which leads the way for developing new antibiotics and alternative therapy. Based on the knowledge that the integrity of the cell envelope and maintaining metabolic balance could affect sensitivity to antibiotic treatment, we hope to find approaches that could alter cell physiology to re-sensitize the resistant strains.

1996,10 - 1999,05 Ph.D., Department of Biochemistry, University of Cambridge, UK
1992,08 - 1994,06 M.Sc., Department of Plant Pathology and Entomology, National Taiwan University
1988,08 - 1992,06 B.Sc., Department of Plant Pathology and Entomology, National Taiwan University

2014,03 - present Associate Research Fellow, Institute of Biological Chemistry, Academia Sinica
2009 - 2013 Career Development Award, Academia Sinica
2006,06 - 2014,03 Assistant Research Fellow, Institute of Biological Chemistry, Academia Sinica
2004,01 - 2006,05 Instructor, Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, USA
1999,02 - 2003,12 Postdoctoral Fellow, Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, USA

    Publications List
Quantitative proteomics analysis reveals the Min system of Escherichia coli modulates reversible protein association with the inner membrane.
Lee HL, Chiang IC, Liang SY, Lee DY, Chang GD, KY Wang, Lin SY, Shih YL MOLECULAR & CELLULAR PROTEOMICS (2016)
Self-Assembly of MinE on the Membrane Underlies Formation of the MinE-Ring to Sustain Function of the E. coli Min System.
Zheng M, Chiang YL, Lee HL, Kong LR, Hsu ST, Hwang IS, Rothfield LI and Shih YL J Biol Chem (2014)
Spatial control of the cell division site by the Min system in E. coli.
Shih YL and Zheng M Environmental Microbiology (2013)
The N-terminal amphipathic helix of the topological specificity factor MinE is associated with shaping membrane curvature.
Shih YL, Huang KF, Lai HM, Liao JH, Lee CS, Chang CM, Mak HM, Hsieh CW & Lin CC PLoS One (2011)
Direct MinE-membrane interaction contributes to the proper localization of MinDE in E. coli.
Hsieh CW, Lai HM, Lin CC, Lin TY, Hsieh TS, Shih YL Molecular Microbiology (2010)
The bacterial cytoskeleton.
Y-L Shih, LI Rothfield Microbiology and Molecular Biology Reviews (2006)
The MreB and Min cytoskeletal-like systems play independent roles in prokaryotic polar differentiation.
Y-L Shih, I Kawagishi and LI Rothfield Mol Microbiol (2005)
Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles.
Shih YL, Le T, Rothfield L Proc Natl Acad Sci USA (2003)
Division site placement in E.coli: mutations that prevent formation of the MinE ring lead to loss of the normal midcell arrest of growth of polar MinD membrane domains.
Y-L Shih, X Fu, GF King , T Le and LI Rothfield EMBO J (2002)

Updated 2018.08.01

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