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Cell and Molecular Biology - Faculty

Xiang-Lei Yang, Ph.D.

Associate Professor
Department of Chemical Physiology
California Campus
Laboratory Website
xlyang@scripps.edu
(858) 784-8976

Scripps Research Joint Appointments

Department of Cell and Molecular Biology
Faculty, Kellogg School of Science and Technology

Research Focus

Our research is focused on elucidating the mechanism of the functional diversity of human aminoacyl-tRNA synthetases and understanding how different functions are activated and regulated. Known as an essential component of the translational apparatus, aminoacyl-tRNA synthetase family catalyzes the first step reaction in protein synthesis, that is, to specifically attach each amino acid onto its cognate tRNA. While preserving this essential role, tRNA synthetases develop other roles during evolution. Human tRNA synthetases, in particular, have diverse functions in various pathways involving angiogenesis, inflammation and apoptosis. The functional diversity is further illustrated in the association with various diseases through genetic mutations on tRNA synthetases that do not affect aminoacylation or protein synthesis. A cross-disciplinary approach combining biochemical, biophysical, molecular genetics, cell biology and evolutionary analysis is used in our research.

Education

B.S., Biomedical Engineering, Capital Institute of Medical Sciences, Beijing, China, 1993
Ph.D., Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, 2000

Selected References

Xu, X., Shi, Y., Zhang, H.-M., Swindell, E.C., Marshall, A.G., Guo, M., Kishi, S. & Yang, X.-L. (2012) Unique domain appended to vertebrate tRNA synthetase is essential for vascular development. Nat. Commun. 3:681 doi: 10.1038/ncomms1686 

Fu, G., Xu, T., Shi, Y. Wei, N. & Yang, X.-L. (2012) tRNA controlled nuclear import of a human tRNA synthetase. J. Biol. Chem. 287, 9330-9334 (Chose as “Paper of the week” and considered as top 1% of papers published by the journal in terms of significance and overall importance)

He. W., Zhang, H.-M., Chong, Y. E., Guo, M., Marshall, A.G. & Yang, X.-L. (2011) Dispersed disease-causing neomorphic mutations on a single protein promote the same localized conformational opening. Proc. Natl. Acad. Sci. U S A 108, 12307-12312 

Zhou, Q., Kapoor, M., Guo, M., Belani, R., Xu, X., Kiosses, W.B., Hanan M., ParK, C., Armour, E., Do, M.-H., Nangle, L. A., Schimmel, P. and Yang, X.-L. (2010) Orthogonal use of a human tRNA synthetase active site to achieve multi-functionality. Nat. Struc. Mol. Biol. 17, 57-61

Links

Collaboration Unlocks Evolutionary Secret of Blood Vessels

Team Solves Mystery of Nerve Disease Genes

Scientists Crack Mystery of Protein's Dual Function

Analysis of Protein-Building Enzyme Sheds Light on Protein Evolution