Chao Xu, Ph. D

Professor, School of Life Sciences, University of Science and Technology of China

443 Huangshan Street, Hefei City, Anhui 230027, P.R.China

Tel: (+86) 551-63600061, E-mail: xuchaor@ustc.edu.cn

EDUCATION AND RESEARCH EXPERIENCE

2016 – Present: Professor, School of Life Sciences, University of Science & Technology of China,

2009 – 2015: Postdoc, Structural Genomics Consortium (SGC), University of Toronto, Canada,

2006 – 2008: Postdoc, Mayo Clinic College of Medicine, USA

2000 – 2005: Ph.D. Biochemistry and molecular biology, School of Life Sciences, University of Sciences and Technology of China, China

1996 – 2000: B.Sc. Biology, School of Life Sciences, University of Sciences and Technology of China, China

RESEARCH INTERESTS

Our research aims to uncover the molecular mechanisms underlying the complicated roles of chemical modifications in mediating the functions of biomacromolecules. Chemical biology, combined with structural biology, molecular biology and cell biology, is utilized for the development of potent chemical tools to interfere with chemical modifications and to examine how aberrant chemical modifications are associated with severe human diseases, such as cancer and neurodegenerative diseases. Overall, by having an impact on our understanding of human biology mechanistically, our research will provide clue to the identification of important therapeutic target and to the treatment of human diseases. 

SELECTED PUBLICATIONS (#: corresponding author; *: Co-first author)

After 2016 (inclusive):

1. #Chen X, #Raiff A, Li S, Guo Q, Zhang J, Zhou H, Timms RT, Yao X, Elledge SJ, *Koren I, *Zhang K, *Xu C. Mechanism of Ψ-Pro/C-degron recognition by the CRL2^FEM1B ubiquitin ligase. Nat. Commun. 15: 3558. (2024). 

2. #Zhao S, #Olmayev-Yaakobov D, Ru W, Li S, Chen X, Zhang J, Yao X, *Koren I, *Zhang K, *Xu C. Molecular basis for C-degron recognition by CRL2^APPBP2 ubiquitin ligase. Proc Natl Acad Sci U S A. 120: e2308870120. (2023).
   

3. #Chen Z, #Lundy T, Zhu Z, Hoskins V, Zhang J, Yao Z, *Strahl B, *Xu C. Molecular basis for Eaf3-mediated assembly of Rpd3S and NuA4. Cell.  Discov. 9: 51. (2023).

4. #Wang X, #Xie H, Guo Q, Cao D, Ru W, Zhao S, Zhu Z, Zhang J, Pan W, Yao X, *Xu, C. Molecular basis for METTL9-mediated N1-histidinemethylation. Cell.  Discov. 9: 38. (2023).

5. Guo Q, Chen X, *Xu, C. TRIM-away via Gln/C-degrons. Nat. Chem. Biol. 18, 1168–1169. (2022).

6. #Guo Q, #Zhao S, #Francisco-Velilla R, Zhang J, Embarc-Buh A, Abellan S, Lv M, Tang P, Gong Q, Shen H, Sun L, Yao X, Min J, Shi Y, *Martínez-Salas E, *Zhang K, *Xu C. Structural basis for Gemin5 decamer-mediated mRNA binding. Nat. Commun. 13: 5166. (2022).

7. #Wang X., #Zeng C., #Liao S., Zhu Z., Zhang J., Tu X., Yao X., *Feng X., *Guang S., *Xu C. Molecular basis for PICS-mediated piRNA biogenesis and cell division. Nat. Commun. 12: 5595. (2021).

8. #Chen X., #Liao S., #Makaros Y., Guo Q., Zhu Z., Krizelman R., Dahan K., Tu X., Yao X., *Koren I., *Xu C. Molecular basis for arginine C-terminal degron recognition by Cul2^FEM1 E3 ligase. Nat. Chem. Biol. 17, 254-262. (2021).

9. #Liao S., #Rajendraprasad G., #Wang N., Eibes S., Gao J., Yu H., Wu G., Tu X., *Huang H., *Barisic M., *Xu C. Molecular basis of vasohibins-mediated detyrosination and its impact on spindle function and mitosis. Cell Res. 29, 533-547. (2019).

10. #Guo Q., #Liao S.,#Kwiatkowski S., Tomaka W., Yu H., Wu G., Tu X., Min J., *Drozak J., *Xu C. Structural insights into SETD3-mediated histidine methylation on β-actin. eLife 8: e43676. (2019).

Before 2016：

1. *#Xu C., #Wang X., #Liu K., Roundtree I., Tempel W., Li Y., Lu Z., *He C., *Min J. Structural basis for selective binding of m6A RNA by the YTHDC1 YTH domain. Nat. Chem. Biol. 10, 927-929. (2014). (Recommended by Faculty of 1000). 

2. #Ni Z., #Xu C., Guo X., Hunter G., Kuznetsova O., Tempel W., Marcon E., Zhong G., Guo H., Kuo W., Li J., Young P., Olsen J., Wan C., Loppnau P., Bakkouri M., Senisterra, G., He H., Huang H., Sidhu S., Emili A., Murphy S., Mosley A., Arrowsmith C., *Min J., *Greenblatt J. RPRD1A and RPRD1B Serve as RNA Polymerase II Carboxyl-Terminal Domain Scaffolds to Recruit RPAP2 for Serine 5 Dephosphorylation. Nat. Struct. Mol. Biol. 21, 686-695. (2014).

3. #Xu Y., #Xu C., #Kato A., Tempel W., Abreu J.C., Bian C., Hu Y., Hu D., Zhao B., Cerovina T., Diao J., Wu F., He H.H., Cui Q., Clark E., Ma C., Barbara A., Veenstra G.J.C., Xu G., Kaiser U.B., Liu X.S., Sugrue S.P., He X., *Min J., *Kato Y., *Shi Y.G. Tet3 CXXC Domain and Dioxygenase Activity Cooperatively Regulate Key Genes for XenopusEye and Neural Development. Cell 151, 1200-1213. (2012).

4. #Xu C., #Jin J., Bian C., Lam R., Tian R., Weist R., You L., Nie J., Bochkarev A., Tempel W., Tan C., Wasney G., Vedadi M., Gish G., Arrowsmith C., Pawson T., Yang X., *Min J. Sequence-specific Recognition of a PxLPxI/L Motif by the Ankyrin-repeat Tumbler Lock. Sci. Signal. 5, ra39. (2012). (cover article).

5. #Bian, C., #Xu C., #Ruan J., #Lee K., #Burke T., Tempel W., Barsyte D., Li J., Wu M., Zhou B., Fleharty B.E., Paulson A., Allali-Hassani A., Zhou J., Mer G., Grant P., *Workman J.L., *Zang J., *Min J. Structural Basis of Sgf29 Tandem Tudor Domains Selectively Binding Methylated Histone H3K4 to Regulate Enzymatic Activity of the SAGA Complex. EMBO J. 30, 2849-2842. (2011).

6. #Xu C., #Bian C., Lam R., Dong A. *Min J. Structural Basis of Selective Binding of Nonmethylated CpG islands by the CXXC Domain of CFP1. Nat. Commun. 2: 227. (2011).

7. #Xu C., #Bian C., #Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones A., MacKenzie F., Pan P., *Li S., *Wang H., *Min J. Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Proc. Natl. Acad. Sci. 107, 19266-19271. (2010).