Dr. Lee, Fang-Jen's Laboratory

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Ph.D. Lee, Fang-Jen

Institute of Molecular Medicine, School of Medicine, National Taiwan University, 7 Chung Shan South Rd., Taipei, Taiwan, R.O.C.

Tel: 886-2-23123456 ext. 65730 (office)
Fax: 886-2-23957801

Email: fangjen@ntu.edu.tw

Last Update: 2012/12


Research Interest

  • 台大雙月刊專欄「細胞生命的重要基礎:囊泡運輸研究」(請點選連結開啟中文介紹)
  • Roles of ARL small GTPases in vesicular trafficking and cytoskeletal modulation
    My laboratory is primarily focused on basic studies of the regulation of vesicular trafficking by small GTPases. An emphasis is on members of the family of 21 kDa ADP-ribosylation factor (ARF) proteins, which are involved in vesicular and membrane transport, maintenance of organelle integrity, and cytoskeletal organization. The ARF family comprises at least six ARFs and more than twenty ARF-like proteins (ARLs), however, the biological functions of ARLs are still unknown. We have identified several ARL encoding proteins that are structurally related to ARF/ARL. Biochemical analyses of purified recombinant ARLs revealed properties similar to ARF/ARL proteins, including the ability to bind and hydrolyze GTP. The biological significance of studying these small GTPases is reflected in the discoveries that several genetic disorders might be caused by aberrant intracellular vesicular trafficking. A memory-associated ARF-related protein, Cp20, was identified from Alzheimer disease study. ARF6 is required in Breast cancer cell invasion and migration. Insulin can also active and trans-locate ARF in rat adipocytes. The roles of ARFs and ARLs in vesicular traffic, intracellular organelle regulation, and cytoskeletal modulation are studied using combined genetic, biochemical, and molecular and cell biological techniques. 
  • Functional studies of the Rbp1p-associated complex in mRNA metabolism
    RNA-binding proteins play key roles in the posttranscriptional regulation of mRNA metabolism. The biological significance of these interactions is reflected in the discoveries that several genetic disorders are caused by aberrant expression of RNA-binding proteins. For example, the FMRP, involved in mRNA localization and translation, is the target of mutations that cause fragile X syndrome, the most common form of hereditary mental retardation. The main objective of this study is to use yeast to investigate the structure and function of an RNA-binding protein, Rbp1p, and its associated complex. Our studies indicate that Rbp1p can selectively binds a subset of mRNAs, forms messenger ribonucleoprotein (mRNP) complexes, and regulate protein expression. We propose that Rbp1p with its associated proteins form a complex for mRNA to achieve secondary structure, thereby regulate their turnover, translation, and/or targeting. We will employ genetics, biochemistry, molecular biology, and cell biology to test this hypothesis.




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