• YANG,Chih-Chi
  • Ext.:4773
  • Office:科四217室
  • Email:ctyu@ncnu.edu.tw
  • Webpage: My Website
Education & Experience
Associate Professor, Department of Applied Chemistry, National Chi Nan University 2015-
Assistant Professor, Department of Applied Chemistry, National Chi Nan University 2011-2015
Assistant Professor, Graduate Institute of Biomedicine and Biomedical Technology, National Chi Nan University 2006-2015
Postdoc Fellow, National Health Research Institutes, Taichung Veterans General Hospital and Yang Ming University 1999-2006
Maser and Ph.D in Genetics, National Yang-Ming University 1991-1999
B.S. in Biology, Tunghai University 1987-1991
Research Interests
Cancers arise with multiple mechanisms, leading to the difficulty for anticancer therapy. To understand how cancers develop, we firstly focused our study on identifying novel genes with altered expression in cancer tissues. Several genes upregulated or downregulated in lung cancer tissues have been identified and the mechanisms by which they induced cancer formation are partly resolved. Intriguingly, we found that many of those cancer related genes are functionally linked to organelle. For example, the potential oncoprotein HURP regulates the expression of many Golgi assembly factors. Additionally, when HURP is phosphorylated by the oncogenic kinase Aurora-A, the pHURP assembles Golgi ribbon by attracting and stabilizing some cis-Golgi assembly factors, and positions Golgi complex by interacting with nuclear membrane protein Synes.
Golgi complex has been pointed out participating in cancer development recently. Firstly, abnormal fragmentation of Golgi complex releases and activates certain oncogenic factors. Secondly, Golgi complex repositions to the cell leading end during cell migration, directionaly provding essential factors for cell movement. We found that HURP, after being methylated by the methyltransferase PRMT5, impaired cell migration via rigidifying Golgi complex; on the contrary, the unmethylated HURP stimulated cell migration by promoting Golgi repositioning via Cdc42-dependent pathway. Thirdly, Golgi complex is fragmented during aggresome formation. Aggresome is a relatively new organelle engaged in quarantining and clearing the misfolded proteins when proteasome fails to remove those protein garbage. We found that aggresome is only generated when Golgi complex is disassembled, thereby releasing some essential factors to the former. Some of those factors enter and enlarge centrosome, and finally aggresome is constructed on the enlarged centrosome. Hence, we are working on how Golgi complex, centrosome and aggresome coordinate each other to ensure the construction of aggresome during protein misfolding pressure, which is highly toxic to cells. Tremendous amounts of misfolded proteins are found in cancer cells, where aggresome is built up to clear those toxic proteins. Inactivation of aggresome is reported providing a alternative way to kill cancer cells. We are on the process testing the cancer cell killing effect of various inhibitors for the aggresome constructing factors released from Golgi complex.