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Wei LI, Ph. D.

Mechanisms of protein modification and their roles in reproduction and aging


Co-workers: Chao Liu, Hui Gao, Long Yan, Fuping Wen, Hongna Wang, Zhiliang Xu, Zhenhua Song, Chao Liu, Yuanting Wang, Haiyan Yu, Chaoming Tang, Yongliang Shang, Yang Hu

• LI Group website

 

  "To be or not to be" is the eternal theme for all creatures. Thus reproduction and aging are the most fundamental issues of biology. I have been interested in these topics since I joined the Institute of Cell Biology in Lanzhou University as a Ph.D candidate in 1998. According to my research experience, our long term goal is to study the general mechanisms of protein modification and their roles in reproduction and aging.

  In the immediate future, we would like to address the following questions:
   1. Posttranslational modification regulation of gametogenesis, especially for meiosis.
   2. The functional role of histone modifications on meiosis, stem cell reprogramming, self renew and differentiation.
   3. Posttranslational regulation basis of reproductive and aging related diseases.

 

 

 

 

 

Plain English:
  The genetic information is coded in DNA, which is then transcribed and translated to proteins to exert biological functions. Besides this central dogma, protein posttranslational modification plays important roles to modulate numerous aspects of protein functions in various biological processes. Ubiquitination, SUMOylation and autophagy are important posttranslational modifications. These modifications regulate stability, activity, cellular localization of proteins as well as protein-protein interactions to affect cell cycle, DNA recombination and repair as well as reproduction and development. Our group focuses on studying the role of protein posttranslational modifications in reproduction and aging processes as well as related diseases.

 

Selected publications:

  1. Liu C, Liu W, Ye Y, Li W*. Ufd2p synthesizes branched ubiquitin chains to promote the degradation of proteins modified with atypical ubiquitin chains. Nat Commun. 2017 Feb 6;8:14274. doi: 10.1038/ncomms14274.
  2. Yang Y, Zhou C, Wang Y, Liu W, Liu C, Wang L, Liu Y, Shang Y, Li M, Zhou S, Wang Y, Zeng W, Zhou J, Huo R*, Li W*. The E3 ubiquitin ligase RNF114 and TAB1 degradation are required for maternal-to-zygotic transition. EMBO Rep. 2017 Feb;18(2):205-216. 
  3. Xu Z, Song Z, Li G, Tu H, Liu W, Liu Y, Wang P, Wang Y, Cui X, Liu C, Shang Y, de Rooij DG, Gao F, Li W*. H2B ubiquitination regulates meiotic recombination by promoting chromatin relaxation. Nucleic Acids Res.  2016 Nov 16;44(20):9681-9697.
  4. Shang YL, Wang HN, Jia PF, Zhao HC, Liu C, Liu WX, Song ZH, Xu ZL,Yang L, Wang YF, Li W*. Autophagy regulates spermatid differentiation via degradation of PDLIM1. Autophagy. 2016 Sep;12(9):1575-92. doi: 10.1080/15548627.2016.1192750.
  5. Wen FP, Guo YS, Hu Y, Wang YT, Wang Q, Yu HY, Tang CM, Yang J, Zhou T, Sha JH, Guo XJ*, Li W*. Distinct temporal requirements for autophagy and proteasome in yeast meiosis. Autophagy. 2016 Apr 2;12(4):671-88.
  6. Liu C,Wang HN, Shang YL, Liu WX, Song ZH, Zhao HC, Wang LN, Jia PF, Gao FY,  Xu ZL, Yang L, Gao F, Li W*. Autophagy is required for ectoplasmic specialization assembly in Sertoli cells. Autophagy. 2016 May 3;12(5):814-32.
  7. Wang HN, Wan HF, Li XX, Liu WX, Chen Q, Wang YQ, Yang L, Duan EK, Tang HM, Zhang XJ, Zhao XY, Gao F*, Li W*. Atg7 is required for acrosome biogenesis during spermatogenesis in mice. Cell Res. 2014 Jul;24(7):852-69.
  8. Liu WX, Shang YL, Zeng Y, Liu C, Li YC, Zhai LH, Wang P, Lou JZ, Xu P, Ye Y*, Li W*. Dimeric Ube2g2 simultaneously engages donor and acceptor ubiquitins to form Lys48-linked ubiquitin chains. EMBO J. 2014 Jan 1;33(1):46-61.
  9.  Li W*, Tu D*, Li LY, Wollert T, Ghirlando R, Brunger AT, Ye Y. Mechanism of ubiquitin chain assembly on the active site cysteine of the ubiquitin conjugating enzyme Ube2g2. Proc Natl Acad Sci U S A. 2009 Mar 10; 106(10):3722-7.
  10. Li W, Tu D, Brunger A, Ye Y. (2007) An ubiquitin ligase transfers preformed polyqubiquitin chains from a conjugating enzyme to substrate. Nature 446(7133):333-7.