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蔣輯武 Chi-Wu Chiang


Chi-Wu Chiang, Ph.D.

E-mail:chiangcw@mail.ncku.edu.tw  /   pp2acwc@hotmail.com

TEL:06-2353535 ext 3637(off.) ext 3591(lab.)


Cancer and Apoptotic Signaling Lab


Educations / Professional Experience


Educations 1993-1998 Ph.D. Graduate student Department of Biology and Division of Geographic Medicine University of Alabama at Birmingham,Birmingham, Alabama, U.S.A.
  1988-1990 M.S., Graduate Institute of Microbiology and Immunology National Yang-Ming University, Taipei, Taiwan, R.O.C.
  1984-1988 B.S., Biology, National Cheng-Kung University, Tainan, Taiwan, R.O.C.


Current Position 2010-present Associate Professor, Institute of Molecular Medicine, National Cheng Kung University Medical College

Professional Experience

2003~2010 Assistant Professor, Institute of Molecular Medicine, National Cheng Kung University Medical College, Tainan, Taiwan


1998-2003 Postdoctoral Research Fellow, Department of Pediatrics and Vanderbilt-Ingram Cancer center, Vanderbilt University, Nashville, TN, U.S.A.


1993-1998 Graduate assistant, Department of Biology and Division of Geographic Medicine University of Alabama at Birmingham Birmingham, Alabama, U.S.A.


1992-1993 Research assistant, Dr. Chen-Kung Chou’s lab Endocrinology Laboratory, Taipei Veterans General Hospital, Taiwan. Studies on the regulation of Hepatitis B Virus gene expression by retinoids


Expertise /Research Interests


protein phosphatase, signal transduction, tumor biology




Reversible phosphorylation is a crucial modification regulating signal transduction in many cellular processes in eukaryotic cells. The state of protein phosphorylation is a consequence of integrated actions of both protein kinases and protein phosphatases.

Protein phosphatase 2A (PP2A) is one of the major serine/ threonine phosphatases in eukaryotic cells involved in regulating multiple cellular processes including DNA replication and repair, protein synthesis, cell cycle progression, and apoptosis. PP2A is a heterotrimeric enzyme which consists of a scaffold subunit A, a catalytic subunit C, and a variable regulatory subunit B. PP2A is known to be regulated by post-translational modifications and by association with regulatory molecules.

Our research is focused on investigating the mechanisms underlying how PP2A participates in a variety of cellular functionsthrough association with regulatory subunits, such as the regulatory B subunits, alpha4, the PP2A phosphatase activator (PTPA), midline-1 (Mid1), and type 2A-interacting protein (TIP) and the mechanisms underlying how PP2A acts as a tumor suppressor. Three main topics are currently pursued in my laboratory. First, we are investigating the role of the B regulatory subunits in regulating the subcellular localization of PP2A, especially focusing on how the B56γ3 subunit controls PP2A nuclear localization. Second, we are investigating the role of PP2A interacting proteins, PTPA and TIP, in regulating PP2A activation and biogenesis, and theirs role in cellular functions. Third, we are investigating how the B56γ3-containing PP2A complex (PP2A-B56γ3) regulates tumorigenesis. We have applied technology of biochemistry, recombinant DNA, fluorescence imaging, and proteomics to address the PP2A-regulated cellular functions.


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