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Chuan Li

Chuan Li

(Professor; Ph. D)


Tel:886-4-2473-0022 ext 12321


Interests in Research

My laboratory has been studying stable protein methylation since 1997 for mostly arginine methylation in lymphoblastoid cells and HeLa cells. We successfully utilized bioinformatic as well as proteomic tools to globally study protein arginine methylation both for the protein arginine methyltransferases (PRMT) and the methylaccepting proteins. Besides, we have been involved in studies of human genetic diseases such as fragile X mental retardation, spinocerebellar ataxia, dentatorubral and pallidoluysian atrophy and Hirschsprung disease.

We also use zebrafish as a model system to study protein arginine methylation We have successfully established the zebrafish culture system and analyzed the expression patterns of the zebrafish PRMT genes and knock-downed the expression of PRMT1 gene by antisense morpholino oligonucleotide (AMO). We have characterized the phenotypes of the morphants and are analyzing the arginine-methylated proteins in embryogenesis.

In our previous proteomic studies, we have identified a few RNA binding proteins that are candidate protein arginine methylated protein. We have obtained evidences of the modification and would like to further pursue the physiological roles of the modification. We thus would like to use cultured human cells as well as zebrafish as the model systems to characterize protein arginine methylation of specific RNA binding proteins and to investigate the involvement of the posttranslational modification in cellular function and embryogenesis.

Publications (at most 7 publications in recent 5 years)

  1. Lin, YL, Tsai, YJ, Liu, YF, Cheng, YC, Hung, CM, Lee, Y, Pan,H and Li, C (2013) The critical role of protein arginine methyltransferase prmt8 in zebrafish early embryonic and neural development is non-redundant with its paralogue prmt1. PLOS One 8, issue 3, e55221. (IF:4.092, 12/85, 75)
  2. Chang, HH, Hu, HH, Lee YJ, Wei, HM, Fan-June, MC, Hsu, T-C, Tsay, GJ and Li, C (2013) Proteomic analyses and identification of arginine methylated proteins differentially recognized by autosera from anti-Sm positive SLE patients. J BioMed Sci 20:27 (IF: 1.980, 63/112, 60)
  3. Lee, YJ, Wei, HM, Chen, LY and Li, C. (2013) Localization of SERBP1 in stress granules and nucleoli. FEBS J. 281, 352-364 (IF: 3.790, 89/290, 60)
  4. Wei, HM, Hu, HH, Chang, GY, Lee, YJ, Li, YJ, Chang, HH and Li, C (2014) Arginine methylation of the cellular nucleic acid binding protein does not affect its subcellular localization but impedes RNA binding. FEBS LETT 588, 1542-8.
  5. Wang, YC, Wang, JD, Chen, CH, Chen, YW, and Li, C (2015) A novel BLAST-based relative distance (BBRD) method can effectively group members of protein arginine methyltransferases and suggest their evolutionary relationship. Molecular Phylogenetics and Evolution 84: 101–111
  6. Chuang, CY, Chang, CP, Lee, YJ, Lin, WL, Chang, WW, Wu, JS, Cheng, YW, Lee, H and Li, C (2017) PRMT1 expression is elevated in head and neck cancer and inhibition of protein arginine methylation by adenosine dialdehyde or PRMT1 knockdown affect proliferation and migration of oral cancer cells. Oncology Reports, 38:1115-1123
  7. Wang, YC, Wang CW, LC, Lee, Lin WC, Tsai YJ, Chang, CP, Lee YJ, Lin MJ and Li, C (2017) Identification, chromosomal arrangements and expression analyses of the evolutionarily conserved prmt1 gene in chicken in comparison with its vertebrate paralogue prmt8. PLOS One. 12(9):e0185042