Likunwang
Institute of Biophysics
Chinese Academy of Sciences
China
Biography
2001-2005 Beijing Normal University, B.S. 2005-2010 Institute of Biophysics, Chinese Academy of Sciences, Ph.D. 2010- 2014 University of California, San Francisco, Postdoctoral Employee 2014-2016 University of California, San Francisco, Associate Specialist 2016- Institute of Biophysics, Chinese Academy of Sciences, Principle Investigator 2001-2005 Beijing Normal University, B.S. 2005-2010 Institute of Biophysics, Chinese Academy of Sciences, Ph.D. 2010- 2014 University of California, San Francisco, Postdoctoral Employee 2014-2016 University of California, San Francisco, Associate Specialist 2016- Institute of Biophysics, Chinese Academy of Sciences, Principle Investigator
Research Interest
In eukaryotes, about one third of the newly synthesized peptides are destined to enter the endoplasmic reticulum (ER) lumen. The ER contains many chaperones and enzymes, providing a unique environment for protein folding, post-translational modification and quality control of secretory proteins. Intrinsic and extrinsic stimulations such as genetic mutation, aging and environmental stresses may lead to unfolded proteins accumulation in the ER and ER dysfunction, a condition called ER stress. This triggers the Unfolded Protein Response (UPR), which can further induce various cellular responses, including ER homeostasis maintenance, cell differentiation, apoptosis, etc. Aberrance of the UPR can cause diseases such as neurodegenerative disease, diabetes, and cancer.We aim to understand the function of the ER and the mechanism of the UPR, and how it relates to ER stress-related diseases.
Publications
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Likun Wang, Lei Wang, Stefano Vavassori, Shengjian Li, HuiminKe, TizianaAnelli, Massimo Degano, Riccardo Ronzoni, Roberto Sitia, Fei Sun, Chihâ€chen Wang.(2008) Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tail. EMBO Rep. 9(7): 642-647.