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Wong, Won-Jing

  • Assistant Professor
  • Education:PhD. Institute of Molecular Medicine, National Taiwan University;Postdoc. Cell Biology Program, Memorial Sloan Kettering Cancer Center
  • Office: R606, 6F, Tradition Medicine Building
  • Phone: 886-2-2826-7117
  • Email:
  • Research

    The centriole is an evolutional conserved organelle and can be found in most of the cells in our body. Centrioles are microtubule-based structures that have two major roles in animal cells. In cycling cells, centrioles serve as the core structure of the centrosomes that function as microtubule-organization centers (MTOC). Centrioles also function as basal bodies that seed the assembly of the primary cilia. Abnormalities in the number of centrosomes are commonly found in cancers, and basal body dysfunction has been implicated in many human diseases (collectively called ciliopathy) related to cilia function. Essentially, both the number and structural integrity of centrioles need to be maintained properly during cell division and development.

    Through a SILAC-based proteomic screen, we have acquired a centriole proteome that allows us to study the role of centrioles in detail. With this centriole proteome, I’ve found a novel centriole-distal-end component that functions as the axoneme-recognition protein to promote the assembly of ciliary transition zone. The long-term goal of my research is to understand the biogenesis and function of centrioles and cilia, both in the normal cellular context and disease. Specifically, I will continue to shed light on molecular mechanisms underlying the following processes:
    (a) The centriole number control during cell cycle.
    (b) The role of centriole proteins in the regulation of cilia assembly and activity.


    • Wang WJ, Tay HG, Soni RK, Perumal GS, Goll MG, Macaluso FP, Asara JM, Amack JD, Tsou MF. 2013. CEP162 is an axoneme-recognition protein promoting transition zone assembly at the cilia base. Nature Cell Biol. 15(6): 591-601.


    • Tanos BE, Yang HJ, Soni RK, Wang WJ, Macaluso FP, Asara JM, Tsou MF. 2013. Centriole-distal appendages promote membrane docking, leading to cilia initiation. Genes& Dev. 27(2): 163-8.


    • Wang WJ, Soni RK, Uryu K, Tsou MF. 2011. The conversion of centrioles to centrosome: essential coupling of duplication with segregation. J Cell Biol. 193(4): 727-39.


    • Tsou MF, Wang WJ, George KA, Uryu K, Stearns T, Jallepalli PV. 2009. Polo kinase and separase regulate the mitotic licensing of centriole duplication in human cells. Dev. Cell. 17(3): 344-354 (co-first author)


    • Lin YM, Chen YR, Lin JR, Wang WJ, Inoko A, Inagaki M, Wu YC, and Chen RH. 2008. eIF3k regulates apoptosis in epithelial cells by releasing caspase 3 from keratin-containing inclusion. J Cell Sci. 121(Pt 14): 2382-93.


    • Wang WJ, Kuo JC, Ku W, Lee YR, Lin FC, Chang YL, Lin YM, Chen CH, Huang YP, Chiang MJ, Yeh SW, Wu PR, Shen CH, Wu CT, and Chen RH. 2007. The tumor suppressor DAPK is reciprocally regulated by tyrosine kinase Src and phosphatase LAR. Mol. Cell. 27(5): 701-16. (selected as “The Editors’ choice in Sci. STKE,” 2007. Reciprocal regulation of DAPK. Issue 403, p.331)


    • Kuo JC, Wang WJ, Yao CC, Wu PR, and Chen RH. 2006. The tumor suppressor DAPK inhibits cell motility by blocking integrin-mediated polarity pathway. J Cell Biol. 172(4): 619-31.


    • Chen RH, Wang WJ, and Kuo JC. 2006. The tumor suppressor DAP-kinase links cell adhesion and cytoskeleton reorganization to cell death regulation. J Biomed Sci. 13(2): 193-199.


    • Chen CH, Wang WJ, Kuo JC, Tsai HC, Lin JR, Chang ZF, Chen RH. 2005. Bidirectional signals transduced by DAPK-ERK interaction promote the apoptotic effect of DAPK. EMBO J. 24(2): 294-304.


    • Wang WJ, Kuo JC, Yao CC, Chen RH. 2002. DAP-kinase induces apoptosis by suppressing integrin activity and disrupting matrix survival signals. J Cell Biol. 159(1): 169-79.


    • Lin KH, Wang WJ, Wu YH, Cheng SY. 2002. Activation of antimetastatic Nm23-H1 gene expression by estrogen and its alpha-receptor. Endocrinology. 143(2): 467-75.
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