Skip to Content

Dr. Fu-Cheng Liang

Phone
Fax
N/A
Email
Title
Associate Professor
Department
Chemistry
Location
N/A
Room
307G

Bio

The research focus of my laboratory is in protein biochemistry, specifically focusing on protein targeting and translocation in bacteria and chloroplast. I have extensively studied how membrane protein chaperones use spatiotemporal regulation to prevent its substrate from aggregation during the membrane protein biogenesis. More recently I have been expanding my research to protein aggregation-prone disease, such as Alzheimer's and Parkinson's disease. 

Institution Degree Graduation Date
Texas A&M Health Science Center PhD 2011
National Taiwan University MS 2002
National Chung Cheng University BS 2000
Employer Position Start Date End Date
California Institute of Technology Post-doctoral Scholar 07/01/2011 06/01/2017
Academia Sinica Research Assistant 07/01/2002 06/01/2004

Publication: 

  1. Alex Siegel, Camille Z. McAvoy, Vinh Lam, Fu-Cheng Liang, Gerard Kroon, Emily Miaou, Patrick Griffin, Peter E. Wright, Shu-ou Shan (2020) Journal of Molecular Biology, 432, 166708, “A disorder-to-order transition activates an ATP-Independent Membrane Protein Chaperone.”
  2. Peng Wang, Fu-Cheng Liang, Daniel Wittmann, Alex Siegel, Shu-ou Shan, Bernhard Grimm (2018) Proceedings of the National Academy of Sciences of the United States of America115(15), E3588-E3596 “Chloroplast SRP43 acts as chaperone for glutamyl-tRNA reductase, the rate-limiting enzyme in tetrapyrrole biosynthesis.”
  3. Fu-Cheng Liang, Gerard J. Kroon, Camille McAvoy, Chris Chi, Peter Wright and Shu-ou Shan (2016) Proceedings of the National Academy of Sciences of the United States of America, 113(12), E1615-E1624 “Conformational Dynamics of a Membrane Protein Chaperone Enables Spatially-regulated Substrate Capture and Release.”
  4. Peera Jaru-Ampornpan, Fu-Cheng Liang, Alex Nisthal, Thang X. Nguyen, Steven Mayo, and Shu-ou Shan (2013) The Journal of Biological Chemistry, 288, 13431-13445 “Mechanism of an ATP-independent Protein Disaggregase. II. Distinct Molecular Interactions Drive Multiple Steps during Aggregate Disassembly.”
  5. Fu-Cheng Liang, Umesh K. Bageshwar and Siegfried M. Musser (2012) The Journal of Biological Chemistry, 287, 12703-12714 “Position-dependent Effects of Polylysine on Sec Protein Transport.”
  6. Fu-Cheng Liang, Umesh K. Bageshwar and Siegfried M. Musser (2009) Molecular Biology of the Cell, 20, 4256-4266 “Bacterial Sec Protein Transport is Rate-Limited by Precursor Length: A Single Turnover Study.”
  7. Umesh K. Bageshwar, Neal Whitaker, Fu-Cheng Liang and Siegfried M. Musser (2009) Molecular Microbiology, 74(1), 209-226 “Interconvertibility of Lipid- and Translocon- Bound Forms of the Bacterial Tat Precursor pre-Sufl.”
  8. Marianne M. Lee, Clara E. Isaza, James D. White, Rita P.-Y. Chen, George F.-C. Liang, Hannah T.-F. He, Sunney I. Chan, Michael K. Chan (2009) Proteins: Structure, Function, and Bioinformatics, 77(3), 647-657 “Insight into the substrate length restriction of M32 carboxypeptidases: Characterization of two distinct subfamilies.”
  9. Rita P.-Y. Chen, Fu-Cheng Liang, Chung-Tien Lee, Rosa Zerella and Sunney I. Chan (2008) Journal of the Chinese Chemical Society 55(4), 772-781Contributions of a Surface Hydrophobic Cluster to the Folding and Structural Stability of Ubiquitin.”
  10. Clara E. Isaza, Xuejun Zhong, Lucia E. Rosas, James D. White, Rita P.-Y. Chen, George F.-C. Liang, Sunney I. Chan, Abhay R. Satoskar and Michael K. Chan (2008) Biochem Biophys Res Commun. 373(1), 25-29 “A Proposed role for Leishmania major Carboxypeptidase in Peptide Catabolism.”
  11. Fu-Cheng Liang, Rita P.-Y. Chen, Chun-Cheng Lin, Kuo-Ting Huang and Sunney I. Chan (2006) Biochem Biophys Res Commun. 342(2), 482-488 “Tuning the Conformation Properties of a Peptide by Glycosylation and Phosphorylation.”

Research interested:

  • Protein targeting and transport across cell membrane
  • Protein folding and misfolding or amyloid formation
  • Membrane protein biogenesis
  • Protein structural and functional studies by NMR and fluorescence spectroscopy