清华大学医学院沈晓骅教授
清华大学医学院沈晓骅教授
Xiaohua Shen received her Ph.D in 2003 at the University of Michigan. She did the postdoctoral training with Dr. Stuart Orkin, a world-renowned stem cellbiologist, at the Dana-Farber Cancer Institute and Harvard Medical School. She was an Instructor at Harvard Medical School before her professorship appointmentat Tsinghua University. Her major research interest is to understand how chromatin structure influences gene expression and cell fate determination. Particularly, she has focused on the role of Polycomb group proteins in theepigenetic regulation of stem cell pluripotency. In Dr. Orkin’s lab, she made two important discoveries including the identification of EZH1 as an alternative histone H3K27 methyltransferase (Mol Cell, 2008) and JUMONJI as a novelmodulator of EZH2 (Cell, 2009). Her work has demonstrated greater complexity in the composition of the Polycomb repressive complex 2 (PRC2), which may renderepigenetic specificity during cell-fate transitions. In addition, fine-tuned, dynamic regulation of the H3K27me3 mark by PcG and associated protein controlsthe balance between self-renewal and differentiation of embryonic stem cells and is thus critical for execution of pluripotency.
Publications
Original Articles
1. Chen Y and Shen X. 1998. Rapid detection of Helicobacter pylori in gastric biopsy material by polymerase chain reaction. Chinese Journal of Birth Health & Heredity 1998; 6(4): 10 – 13.
2. Norris SR, Shen X, and DellaPenna D. Complementation of the Arabidopsis pds1 mutation with the gene encoding p-Hydroxyphenylpyruvate Dioxygenase. Plant Physiol. 1998; 117(4): 1317 –1323.
3. Shen X, Ellis RE, Lee K, Liu C, Yang K, Solomon A, Yoshida H, Morimoto R, Kurnit DM, Mori K, and Kaufman RJ. Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development. Cell 2001; 107: 893-903.
4. Lee K, Tirasophon W, Shen X, Michalak M, Prywes R, Okada T, Yoshida H, Mori K, and Kaufman RJ. IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response. Genes Dev. 2002; 16: 452-466.
5. Shen X, Ellis RE, Sakaki K and Kaufman RJ. 2005. Genetic interactions due to constitutive and inducible gene regulation mediated by the unfolded protein response in C. elegans. PLoS Genetics. 2005; 1(3):e37.
6. Zhang K, Shen X, Wu J, Sakaki K, Saunders T, Rutkowski DT, Back SH, Kaufman RJ. Stress in the endoplasmic reticulum activates s1p- and s2p-mediated cleavage of CREBh, a novel liver-specific transcription factor required to induce the acute phase response. Cell 2006; 124(3): 587-99.
7. Wang J, Rao S, Chu J, Shen X, Levasseur DN, Theunissen TW, Orkin SH. A protein interaction network for pluripotency of embryonic stem cells. Nature 2006; 444(7117):364-8.
8. Kim J, Chu J, Shen X, Wang J, Orkin SH. An extended transcriptional network for pluripotency of embryonic stem cells. Cell 2008; 132(6): 1049-61.
9. Shen X, Liu Y, Hsu Y, Fujiwara Y, Kim J, Mao X, Yuan G, and Orkin SH. EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in maintaining stem cell identity and executing pluripotency. Mol Cell 2008; 32(4):491-502.
10. Shen X, Kim W, Fujiwara Y, Simon MD, Liu Y, Mysliwiec MR, Yuan G, Lee Y, Orkin SH. Jumonji modulates Polycomb activity and self-renewal versus differentiation of stem cells. Cell 2009; 139(7): 1303-1314.
Reviews
11. Kaufman RJ, Scheuner D, Schroder M, Shen X, Lee K, Liu C and Arnold SM. A role for the unfolded protein response in nutrient sensing and differentiation. Nat Rev Mol Cell Biol. 2002; 3(6):411-21.
12. Shen X, Zhang K, and Kaufman RJ. The unfolded protein response - a stress signaling pathway of the endoplasmic reticulum. J Chem Neuroanat.2004; 28(1-2):79-92.
13. Orkin SH, Wang J, Kim J, Chu J, Rao S, Theunissen TW, Shen X, Levasseur DN. The transcriptional network controlling pluripotency in ES cells. Cold Spring Harb Symp Quant Biol. 2008.
14. Shen X, Orkin SH. Glimpses of the epigenetic landscape. Cell Stem Cell. 2009; 4(1): 1-2.
Ph.D. Thesis
Shen, X. Unfolding the unfolded protein response: Turn to the worm!
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