Education and Training
- Ph.D., Peking University, Beijing, P. R. China, 2005
- M.S., Huazhong Agriculture University, Wuhan, P. R. China, 1999
- B.S., Wuhan University, Wuhan, P. R. China, 1996
Zhong Y and Fang S. Live cell imaging of protein dislocation from the endoplasmic reticulum. J. Biol. Chem. 287(33), 28057-28066, 2012. PMCID: PMC3431711
Liu L, Liu C, Zhong Y, Apostolou A, Fang S. ER stress response during the differentiation of H9 cells induced by retinoic acid. Biochem. Biophys. Res. Commun. 417(2): 738-743, 2012.
Zhong Y, Wang Y, Yang H, Ballar P, Lee J, Ye Y, Monteiro MJ, Fang S. Importin β interacts with the ER-associated degradation machinery and promotes ubiquitination and proteasomal degradation of mutant α1-antitrypsin. J Biol Chem. 286(39): 33921-33930, 2011.
Wang Y, Ballar P, Zhong Y, Zhang X, Liu C, Zhang Y, Monteiro MJ, Li J, and Fang S. SVIP induces localization of p97/VCP to the plasma and lysosomal membranes and regulates autophagy. PLoS One. 6(8): e24478, 2011. PMCID: PMC3190800
Jiang H, Jans R, Xu W, Rorke E, Lin C, Chen Y, Fang S, Zhong Y, Richard L Eckert. Type I transglutaminase accumulation in the endoplasmic reticulum may be an underlying cause of autosomal recessive congenital ichthyosis. J Biol Chem. 285(41): 31634-31646, 2010. PMCID: PMC2951236
Additional Publication Citations
Yang H, Liu C, Zhong Y, Luo S, Monteiro M, and Fang S. Huntingtin interacts with the Cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP. PLoS One. 5(1): e8905, 2010. PMCID: PMC2811200
Du S, Li H, Bian Y, and Zhong Y. Heat-shock protein 90α1 is required for organized myofibril assembly in skeletal muscles of zebrafish embryos. Proc. Natl. Acad. Sci. USA 105(2): 554-559, 2008. PMCID: PMC2206574
Ballar P, Zhong Y, Nagahama M, Tagaya M, Shen Y, Fang S. Identification of SVIP as an endogenous inhibitor of endoplasmic reticulum-associated degradation. J Biol Chem. 282(47): 33908-14, 2007.
Liu H, Wei C, Zhong Y, Li Y. Rice black-streaked dwarf virus minor core protein P8 is a nuclear dimeric protein and represses transcription in tobacco protoplasts. FEBS Lett. 581(13): 2534-40, 2007.
Liu H, Wei C, Zhong Y, Li Y. Rice black-streaked dwarf virus outer capsid protein P10 has self-interactions and forms oligomeric complexes in solution. Virus Res. 127(1): 34-42, 2007.
Zhong Y, Guo A, Li C, Zhuang B, Lai M, Wei C, Luo J, and Li Y. Identification of a naturally occurring recombinant isolate of Sugarcane mosaic virus causing maize dwarf mosaic disease. Virus Genes 30(1), 75-83, 2005.
Li Y, Bao Y, Wei C, Kang Z, Zhong Y, Mao P, Wu G, Chen Z, Schiemann J, and Nelson R. Rice dwarf phytoreovirus segment S6 encoded-nonstructural protein has a cell-to-cell movement function. J. Virol. 78, 5382-5389, 2004. PMCID: PMC400330
Li C, Gao F, Zhong Y, Wei C, and Li Y. Cloning and Functional Analysis of Tobacco Pectin Methylesterase. Prog. Biochem. Biophys. 31(7), 643-649, 2004.
Zhong Y, Zhou J, Zhuang B, Wei C, and Li Y. cDNA Cloning and expression in Escherichia coli of Rice black-streaked dwarf virus segment 7. Acta Microbiol. Sin. 43, 442-447, 2003.
Li C, Zhong Y, Zhang X, Wei C, and Li Y. Cloning and expression of S9-1 gene of Rice black-streaked dwarf virus in Escherichia coli. Acta Microbiol. Sin. 43, 330-335, 2003.
Li H, Zhong Y, Zhao C, and Liao Y. Cloning and expression analysis of a wheat chitinase gene Wch2. J. Plant Physiol. Mol. Biol. 29, 347-352, 2003.
My current research is focusing on endoplasmic reticulum-associated degradation (ERAD). ERAD is a mean for protein quality control of the secretory pathway and for regulating certain normal protein levels. It involves coordinated events of protein dislocation from the ER, ubiquitination and degradation by the proteasome. My major work is to understand how the substrate proteins are transported from the ER to the cytosol. In my previous research, I have identified a protein that was well known as a nuclear import factor, importin β, as a protein involved in ERAD. It may co-work with a previously reported protein complex, VCP complex, and help the aberrant folded proteins to pass through the membrane. And we recently established a dislocation-dependent reconstitute GFP (drGFP) assay that can be used to measure the protein dislocation in the cell.