廈門大學(xué)生物學(xué)系導(dǎo)師：韓愛(ài)東 正文

　　姓名：韓愛(ài)東　　
　　性別：男　　
　　職稱：教授　
　　學(xué)院：生命科學(xué)學(xué)院
　　研究方向：通過(guò)結(jié)構(gòu)生物學(xué)實(shí)驗(yàn)手段研究在細(xì)胞編程和重編程過(guò)程中，轉(zhuǎn)錄因子與其輔因子的結(jié)構(gòu)與功能，通過(guò)結(jié)構(gòu)生物學(xué)實(shí)驗(yàn)手段，揭示其表觀遺傳和轉(zhuǎn)錄調(diào)控分子機(jī)制
　　E-mail: ahan@xmu.edu.cn
　　
　　個(gè)人簡(jiǎn)介：
　　1999年獲中國(guó)科學(xué)學(xué)院微生物所微生物學(xué)博士學(xué)位；1999-2006年科羅拉多州大學(xué)生化系博士后；2006-2007年南加州大學(xué)分子與計(jì)算生物系博士后。
　　1999, Ph.D., Institute of Microbiology, Chinese Academy of Sciences; 1999-2006, Postdoctoral follow, University of Colorado at Boulder; 2006-2007, Senior research associate, University of Southern

　　主要研究領(lǐng)域（Research Area）
　　轉(zhuǎn)錄是基因表達(dá)的關(guān)鍵步驟，而轉(zhuǎn)錄因子與特異的增強(qiáng)子結(jié)合并進(jìn)一步形成調(diào)節(jié)復(fù)合體。這些轉(zhuǎn)錄因子之間及與DNA間的相互作用能夠有效地編程和重編程細(xì)胞, 如用Oct4, Sox2, Nanog和Klf4可以將體細(xì)胞轉(zhuǎn)換為多潛能干細(xì)胞技術(shù)（iPS）。我們主要通過(guò)結(jié)構(gòu)生物學(xué)實(shí)驗(yàn)手段研究在細(xì)胞編程和重編程過(guò)程中，轉(zhuǎn)錄因子與其輔因子的結(jié)構(gòu)與功能，通過(guò)結(jié)構(gòu)生物學(xué)實(shí)驗(yàn)手段，揭示其表觀遺傳和轉(zhuǎn)錄調(diào)控分子機(jī)制。我們的研究與退行性疾病、組織再生和修復(fù)有著緊密的聯(lián)系。
　　Transcription is a key step for gene expression regulation, which in turn globally programs or reprograms the cells. Transcription factors as well as cofactors are centered on the specific enhancer regions of genes to form high-order regulatory assemblies. The most, if not all, of these cofactors are histone modification enzymes that convey a variety of upstream signals to epigenetic marks. This process is best illustrated in the stem cell production induced by a set of ectopically expressed transcription factors, including Oct4, Sox2, Nanog and Klf4 that can convert somatic cells into induced pluropotent stem cells (iPS). Their activities are always associated with epigenetic modifications, for example histones acetylation by p300, CBP and PCAF. Our lab is taking a structural and functional approach to understand molecular mechanisms of the epigenetics and transcriptional regulation.

　　代表性論文（Selected Publications）
　　He, Ju; Ye, Jun; Cai, Yongfei; Riquelme, Cecilia; Liu, Jun O.; Liu, Xuedong; Han, Aidong; Chen, L. Structure of p300 bound to MEF2 on DNA reveals a mechanism of enhanceosome assembly (accepted)
　　Wu Y, Dey R, Han A, Jayathilaka N, Philips M, Ye J, Chen L. Structure of the MADS-box/MEF2 domain of MEF2 bound to DNA and its implication for myocardin recruitment. Journal of Molecular Biology, Mar 26;397(2):520-33, 2010
　　Guo L, Han A, Bates DL. Cao J, Chen L. Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains. Proceedings of the National Academy of Sciences USA, 13;104: 4297-4302, 2007.
　　Wu Y, Borde M, Heissmeyer V, Feuerer M, Lapan AD, Stroud JC, Bates DL, Guo L, Han A, Ziegler SF, Mathis D, Benoist C, Chen L& Rao A. FOXP3 controls regulatory T cell function through cooperation with NFAT. Cell, 126: 375-387, 2006.
　　Stroud JC, Wu Y, Bates DL, Han A, Nowick K, Paabo S, Tong H, Chen L. Structure of the forkhead domain of FOXP2 bound to DNA. Structure, Jan;4(1):159-166, 2006.
　　Han A, He J, Wu Y, Liu JO, Chen L. Mechanism of recuitment of class II histone deacetylases by Myocyte enhancer factor-2. Journal of Molecular Biology, 7;345(1):91-102, 2005.
　　Han A, Pan F, Stroud JC, Youn HD, Liu JO, Chen L. Sequence-specific recruitment of transcriptional co-repressor Cabin1 by Myocyte Enhancer Factor-2. Nature, 422(6933): 730-734, 2003.
　　
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