Scholars@Duke

• Background
• 

  Education, Training, & Certifications

  • Ph.D., Oklahoma State University, Stillwater 2003
  • M.D., Beijing Medical University (China) 1993
• 

  Previous Appointments & Affiliations

  • Assistant Professor of Medicine, Medicine, Cardiology, Medicine 2008 - 2015
  • Instructor, Temporary in the Department of Medicine, Medicine, Cardiology, Medicine 2008
• Research
• 

  Selected Grants

  • Mitochondrial Protein Acetylation and Energy Metabolism in Muscle awarded by National Institutes of Health 2015 - 2018
  • Regulation of Cardiac Adrenergic Function by S-nitrosylation awarded by National Institutes of Health 2009
• Publications & Artistic Works
• 

  Selected Publications

  • Academic Articles

    • Fonseca, Fabio V., Thomas M. Raffay, Kunhong Xiao, Precious J. McLaughlin, Zhaoxia Qian, Zachary W. Grimmett, Naoko Adachi, et al. “S-nitrosylation is required for β2AR desensitization and experimental asthma.” Mol Cell 82, no. 16 (August 18, 2022): 3089-3102.e7. https://doi.org/10.1016/j.molcel.2022.06.033.
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    • He, Qing-Tao, Peng Xiao, Shen-Ming Huang, Ying-Li Jia, Zhong-Liang Zhu, Jing-Yu Lin, Fan Yang, et al. “Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2.” Nat Commun 12, no. 1 (April 22, 2021): 2396. https://doi.org/10.1038/s41467-021-22731-x.
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    • Liu, Qi, Qing-Tao He, Xiaoxuan Lyu, Fan Yang, Zhong-Liang Zhu, Peng Xiao, Zhao Yang, et al. “DeSiphering receptor core-induced and ligand-dependent conformational changes in arrestin via genetic encoded trimethylsilyl 1H-NMR probe.” Nat Commun 11, no. 1 (September 25, 2020): 4857. https://doi.org/10.1038/s41467-020-18433-5.
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    • Nieto, Ainhoa, Makoto R. Hara, Victor Quereda, Wayne Grant, Vanessa Saunders, Kunhong Xiao, Patricia H. McDonald, and Derek R. Duckett. “βarrestin-1 regulates DNA repair by acting as an E3-ubiquitin ligase adaptor for 53BP1.” Cell Death Differ 27, no. 4 (April 2020): 1200–1213. https://doi.org/10.1038/s41418-019-0406-6.
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    • Zhang, Qiangmin, Kunhong Xiao, Hongda Liu, Lei Song, Jennifer C. McGarvey, W Bruce Sneddon, Alessandro Bisello, and Peter A. Friedman. “Site-specific polyubiquitination differentially regulates parathyroid hormone receptor-initiated MAPK signaling and cell proliferation.” J Biol Chem 293, no. 15 (April 13, 2018): 5556–71. https://doi.org/10.1074/jbc.RA118.001737.
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    • Xiao, Kunhong, and Jinpeng Sun. “Elucidating structural and molecular mechanisms of β-arrestin-biased agonism at GPCRs via MS-based proteomics.” Cell Signal 41 (January 2018): 56–64. https://doi.org/10.1016/j.cellsig.2017.09.013.
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    • Liu, Chun-Hua, Zheng Gong, Zong-Lai Liang, Zhi-Xin Liu, Fan Yang, Yu-Jing Sun, Ming-Liang Ma, et al. “Arrestin-biased AT1R agonism induces acute catecholamine secretion through TRPC3 coupling.” Nat Commun 8 (February 9, 2017): 14335. https://doi.org/10.1038/ncomms14335.
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    • Watson, Lewis J., Kevin M. Alexander, Maradumane L. Mohan, Amber L. Bowman, Supachoke Mangmool, Kunhong Xiao, Sathyamangla V. Naga Prasad, and Howard A. Rockman. “Phosphorylation of Src by phosphoinositide 3-kinase regulates beta-adrenergic receptor-mediated EGFR transactivation.” Cell Signal 28, no. 10 (October 2016): 1580–92. https://doi.org/10.1016/j.cellsig.2016.05.006.
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    • Li, Ang, Duxiao Yang, Mengyuan Zhu, Keng-chang Tsai, Kun-hong Xiao, Xiao Yu, Jinpeng Sun, and Lupei Du. “Discovery of novel FFA4 (GPR120) receptor agonists with β-arrestin2-biased characteristics.” Future Med Chem 7, no. 18 (2015): 2429–37. https://doi.org/10.4155/fmc.15.160.
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    • Wang, Hong-Mei, Yun-Fei Xu, Shang-Lei Ning, Du-Xiao Yang, Yi Li, Yu-Jie Du, Fan Yang, et al. “The catalytic region and PEST domain of PTPN18 distinctly regulate the HER2 phosphorylation and ubiquitination barcodes.” Cell Res 24, no. 9 (September 2014): 1067–90. https://doi.org/10.1038/cr.2014.99.
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    • Shukla, Arun K., Gerwin H. Westfield, Kunhong Xiao, Rosana I. Reis, Li-Yin Huang, Prachi Tripathi-Shukla, Jiang Qian, et al. “Visualization of arrestin recruitment by a G-protein-coupled receptor.” Nature 512, no. 7513 (August 14, 2014): 218–22. https://doi.org/10.1038/nature13430.
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    • Brady, Donita C., Matthew S. Crowe, Michelle L. Turski, G Aaron Hobbs, Xiaojie Yao, Apirat Chaikuad, Stefan Knapp, et al. “Copper is required for oncogenic BRAF signalling and tumorigenesis.” Nature 509, no. 7501 (May 22, 2014): 492–96. https://doi.org/10.1038/nature13180.
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    • Wisler, James W., Kunhong Xiao, Alex R. B. Thomsen, and Robert J. Lefkowitz. “Recent developments in biased agonism.” Curr Opin Cell Biol 27 (April 2014): 18–24. https://doi.org/10.1016/j.ceb.2013.10.008.
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    • Kahsai, Alem W., Sudarshan Rajagopal, Jinpeng Sun, and Kunhong Xiao. “Monitoring protein conformational changes and dynamics using stable-isotope labeling and mass spectrometry.” Nat Protoc 9, no. 6 (2014): 1301–19. https://doi.org/10.1038/nprot.2014.075.
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    • Li, Rong, Di-Dong Xie, Jun-Hong Dong, Hui Li, Kang-Shuai Li, Jing Su, Lai-Zhong Chen, et al. “Molecular mechanism of ERK dephosphorylation by striatal-enriched protein tyrosine phosphatase.” J Neurochem 128, no. 2 (January 2014): 315–29. https://doi.org/10.1111/jnc.12463.
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    • Files, D Clark, Kunhong Xiao, Tan Zhang, Chun Liu, Jiang Qian, Weiling Zhao, Peter E. Morris, Osvaldo Delbono, and Xin Feng. “The posterior cricoarytenoid muscle is spared from MuRF1-mediated muscle atrophy in mice with acute lung injury.” Plos One 9, no. 1 (2014): e87587. https://doi.org/10.1371/journal.pone.0087587.
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    • Shukla, Arun K., Aashish Manglik, Andrew C. Kruse, Kunhong Xiao, Rosana I. Reis, Wei-Chou Tseng, Dean P. Staus, et al. “Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide.” Nature 497, no. 7447 (May 2, 2013): 137–41. https://doi.org/10.1038/nature12120.
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    • Li, R., D. -. D. Xie, J. -. H. Dong, H. Li, K. -. S. Li, J. Su, L. -. Z. Chen, et al. “Molecular mechanism of ERK dephosphorylation by striatal-enriched protein tyrosine phosphatase.” Journal of Neurochemistry, 2013.
    • Pan, Chang, Hong-Da Liu, Zheng Gong, Xiao Yu, Xu-Ben Hou, Di-Dong Xie, Xi-Bin Zhu, et al. “Cadmium is a potent inhibitor of PPM phosphatases and targets the M1 binding site.” Sci Rep 3 (2013): 2333. https://doi.org/10.1038/srep02333.
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    • Shukla, A. K., A. Manglik, A. C. Kruse, K. Xiao, R. I. Reis, W. C. Tseng, D. P. Staus, et al. “Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide.” Nature 497, no. 7447 (2013): 137–41. https://doi.org/10.1038/nature12120.
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    • Tang, Hao, Kunhong Xiao, Lan Mao, Howard A. Rockman, and Douglas A. Marchuk. “Overexpression of TNNI3K, a cardiac-specific MAPKKK, promotes cardiac dysfunction.” J Mol Cell Cardiol 54 (January 2013): 101–11. https://doi.org/10.1016/j.yjmcc.2012.10.004.
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    • Han, Sang-oh, Kunhong Xiao, Jihee Kim, Jiao-Hui Wu, James W. Wisler, Nobuhiro Nakamura, Neil J. Freedman, and Sudha K. Shenoy. “MARCH2 promotes endocytosis and lysosomal sorting of carvedilol-bound β(2)-adrenergic receptors.” J Cell Biol 199, no. 5 (November 26, 2012): 817–30. https://doi.org/10.1083/jcb.201208192.
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    • Xiao, K., J. Sun, J. Kim, S. Rajagopal, B. Zhai, J. Villén, W. Haas, et al. “Erratum: Global phosphorylation analysis of ß-arrestin-mediated signaling downstream of a seven transmembrane receptor (7TMR) (Proceedings of the National Academy of Sciences of the United States of America (2010) 107, 34 (15299-15304) doi:10.1073/pnas.1008461107).” Proceedings of the National Academy of Sciences of the United States of America 109, no. 33 (August 14, 2012): 13464. https://doi.org/10.1073/pnas.1211889109.
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    • Sarker, Subhodeep, Kunhong Xiao, and Sudha K. Shenoy. “A tale of two sites: How ubiquitination of a G protein-coupled receptor is coupled to its lysosomal trafficking from distinct receptor domains.” Commun Integr Biol 4, no. 5 (September 2011): 528–31. https://doi.org/10.4161/cib.4.5.16458.
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    • Shukla, Arun K., Kunhong Xiao, and Robert J. Lefkowitz. “Emerging paradigms of β-arrestin-dependent seven transmembrane receptor signaling.” Trends Biochem Sci 36, no. 9 (September 2011): 457–69. https://doi.org/10.1016/j.tibs.2011.06.003.
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    • Kahsai, Alem W., Kunhong Xiao, Sudarshan Rajagopal, Seungkirl Ahn, Arun K. Shukla, Jinpeng Sun, Terrence G. Oas, and Robert J. Lefkowitz. “Multiple ligand-specific conformations of the β2-adrenergic receptor.” Nat Chem Biol 7, no. 10 (August 21, 2011): 692–700. https://doi.org/10.1038/nchembio.634.
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    • Hara, Makoto R., Jeffrey J. Kovacs, Erin J. Whalen, Sudarshan Rajagopal, Ryan T. Strachan, Wayne Grant, Aaron J. Towers, et al. “A stress response pathway regulates DNA damage through β2-adrenoreceptors and β-arrestin-1.” Nature 477, no. 7364 (August 21, 2011): 349–53. https://doi.org/10.1038/nature10368.
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    • Nobles, Kelly N., Kunhong Xiao, Seungkirl Ahn, Arun K. Shukla, Christopher M. Lam, Sudarshan Rajagopal, Ryan T. Strachan, et al. “Distinct phosphorylation sites on the β(2)-adrenergic receptor establish a barcode that encodes differential functions of β-arrestin.” Sci Signal 4, no. 185 (August 9, 2011): ra51. https://doi.org/10.1126/scisignal.2001707.
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    • Xiao, Kunhong, and Sudha K. Shenoy. “Beta2-adrenergic receptor lysosomal trafficking is regulated by ubiquitination of lysyl residues in two distinct receptor domains.” J Biol Chem 286, no. 14 (April 8, 2011): 12785–95. https://doi.org/10.1074/jbc.M110.203091.
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    • Shukla, Arun K., Jihee Kim, Seungkirl Ahn, Kunhong Xiao, Sudha K. Shenoy, Wolfgang Liedtke, and Robert J. Lefkowitz. “Arresting a transient receptor potential (TRP) channel: beta-arrestin 1 mediates ubiquitination and functional down-regulation of TRPV4.” J Biol Chem 285, no. 39 (September 24, 2010): 30115–25. https://doi.org/10.1074/jbc.M110.141549.
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    • Hernandez, M., A. Lachmann, S. Zhao, K. Xiao, and A. Ma’ayan. “Inferring the sign of kinase-substrate interactions by combining quantitative phosphoproteomics with a literature-based mammalian kinome network.” 10th Ieee International Conference on Bioinformatics and Bioengineering 2010, Bibe 2010, September 6, 2010, 180–84. https://doi.org/10.1109/BIBE.2010.75.
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    • Xiao, Kunhong, Jinpeng Sun, Jihee Kim, Sudarshan Rajagopal, Bo Zhai, Judit Villén, Wilhelm Haas, et al. “Global phosphorylation analysis of beta-arrestin-mediated signaling downstream of a seven transmembrane receptor (7TMR).” Proc Natl Acad Sci U S A 107, no. 34 (August 24, 2010): 15299–304. https://doi.org/10.1073/pnas.1008461107.
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    • Xie, Liang, Kunhong Xiao, Erin J. Whalen, Michael T. Forrester, Robert S. Freeman, Guohua Fong, Steven P. Gygi, Robert J. Lefkowitz, and Jonathan S. Stamler. “Oxygen-regulated beta(2)-adrenergic receptor hydroxylation by EGLN3 and ubiquitylation by pVHL.” Sci Signal 2, no. 78 (July 7, 2009): ra33. https://doi.org/10.1126/scisignal.2000444.
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    • Shenoy, Sudha K., Aalok S. Modi, Arun K. Shukla, Kunhong Xiao, Magali Berthouze, Seungkirl Ahn, Keith D. Wilkinson, William E. Miller, and Robert J. Lefkowitz. “Beta-arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2.” Proc Natl Acad Sci U S A 106, no. 16 (April 21, 2009): 6650–55. https://doi.org/10.1073/pnas.0901083106.
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    • Petrotchenko, Evgeniy V., Kunhong Xiao, Jennifer Cable, Yiwen Chen, Nikolay V. Dokholyan, and Christoph H. Borchers. “BiPS, a photocleavable, isotopically coded, fluorescent cross-linker for structural proteomics.” Mol Cell Proteomics 8, no. 2 (February 2009): 273–86. https://doi.org/10.1074/mcp.M800265-MCP200.
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    • Shenoy, Sudha K., Kunhong Xiao, Vidya Venkataramanan, Peter M. Snyder, Neil J. Freedman, and Allan M. Weissman. “Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor.” J Biol Chem 283, no. 32 (August 8, 2008): 22166–76. https://doi.org/10.1074/jbc.M709668200.
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    • Kovacs, Jeffrey J., Erin J. Whalen, Renshui Liu, Kunhong Xiao, Jihee Kim, Minyong Chen, Jiangbo Wang, Wei Chen, and Robert J. Lefkowitz. “Beta-arrestin-mediated localization of smoothened to the primary cilium.” Science 320, no. 5884 (June 27, 2008): 1777–81. https://doi.org/10.1126/science.1157983.
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    • Shenoy, Sudha K., Larry S. Barak, Kunhong Xiao, Seungkirl Ahn, Magali Berthouze, Arun K. Shukla, Louis M. Luttrell, and Robert J. Lefkowitz. “Ubiquitination of beta-arrestin links seven-transmembrane receptor endocytosis and ERK activation.” J Biol Chem 282, no. 40 (October 5, 2007): 29549–62. https://doi.org/10.1074/jbc.M700852200.
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    • Nobles, Kelly N., Ziqiang Guan, Kunhong Xiao, Terrence G. Oas, and Robert J. Lefkowitz. “The active conformation of beta-arrestin1: direct evidence for the phosphate sensor in the N-domain and conformational differences in the active states of beta-arrestins1 and -2.” J Biol Chem 282, no. 29 (July 20, 2007): 21370–81. https://doi.org/10.1074/jbc.M611483200.
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    • Xiao, Kunhong, Daniel B. McClatchy, Arun K. Shukla, Yang Zhao, Minyong Chen, Sudha K. Shenoy, John R. Yates, and Robert J. Lefkowitz. “Functional specialization of beta-arrestin interactions revealed by proteomic analysis.” Proc Natl Acad Sci U S A 104, no. 29 (July 17, 2007): 12011–16. https://doi.org/10.1073/pnas.0704849104.
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    • Elberry, Maria, Kunhung Xiao, Lothar Esser, Di Xia, Linda Yu, and Chang-An Yu. “Generation, characterization and crystallization of a highly active and stable cytochrome bc1 complex mutant from Rhodobacter sphaeroides.” Biochim Biophys Acta 1757, no. 7 (July 2006): 835–40. https://doi.org/10.1016/j.bbabio.2006.05.031.
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    • Shenoy, Sudha K., Matthew T. Drake, Christopher D. Nelson, Daniel A. Houtz, Kunhong Xiao, Srinivasan Madabushi, Eric Reiter, Richard T. Premont, Olivier Lichtarge, and Robert J. Lefkowitz. “beta-arrestin-dependent, G protein-independent ERK1/2 activation by the beta2 adrenergic receptor.” J Biol Chem 281, no. 2 (January 13, 2006): 1261–73. https://doi.org/10.1074/jbc.M506576200.
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    • Xiao, Kunhong, Sudha K. Shenoy, Kelly Nobles, and Robert J. Lefkowitz. “Activation-dependent conformational changes in {beta}-arrestin 2.” J Biol Chem 279, no. 53 (December 31, 2004): 55744–53. https://doi.org/10.1074/jbc.M409785200.
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    • Xiao, Kunhong, Xiaoying Liu, Chang-An Yu, and Linda Yu. “The extra fragment of the iron-sulfur protein (residues 96-107) of Rhodobacter sphaeroides cytochrome bc1 complex is required for protein stability.” Biochemistry 43, no. 6 (February 17, 2004): 1488–95. https://doi.org/10.1021/bi035378z.
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    • Xiao, Kunhong, Gregory Engstrom, Sany Rajagukguk, Chang-An Yu, Linda Yu, Bill Durham, and Francis Millett. “Effect of famoxadone on photoinduced electron transfer between the iron-sulfur center and cytochrome c1 in the cytochrome bc1 complex.” J Biol Chem 278, no. 13 (March 28, 2003): 11419–26. https://doi.org/10.1074/jbc.M211620200.
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    • Engstrom, Gregory, Ray Rajagukguk, Aleister J. Saunders, Chetan N. Patel, Sany Rajagukguk, Torsten Merbitz-Zahradnik, Kunhong Xiao, et al. “Design of a ruthenium-labeled cytochrome c derivative to study electron transfer with the cytochrome bc1 complex.” Biochemistry 42, no. 10 (March 18, 2003): 2816–24. https://doi.org/10.1021/bi027213g.
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    • Yu, Chang-An, Xiaolin Wen, Kunhong Xiao, Di Xia, and Linda Yu. “Inter- and intra-molecular electron transfer in the cytochrome bc(1) complex.” Biochim Biophys Acta 1555, no. 1–3 (September 10, 2002): 65–70. https://doi.org/10.1016/s0005-2728(02)00256-6.
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    • Engstrom, Gregory, Kunhong Xiao, Chang-An Yu, Linda Yu, Bill Durham, and Francis Millett. “Photoinduced electron transfer between the Rieske iron-sulfur protein and cytochrome c(1) in the Rhodobacter sphaeroides cytochrome bc(1) complex. Effects of pH, temperature, and driving force.” J Biol Chem 277, no. 34 (August 23, 2002): 31072–78. https://doi.org/10.1074/jbc.M202594200.
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    • Xiao, K., A. Chandrasekaran, L. Yu, and C. A. Yu. “Evidence for the intertwined dimer of the cytochrome bc(1) complex in solution.” J Biol Chem 276, no. 49 (December 7, 2001): 46125–31. https://doi.org/10.1074/jbc.M107436200.
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    • Xiao, K., L. Yu, and C. A. Yu. “Confirmation of the involvement of protein domain movement during the catalytic cycle of the cytochrome bc1 complex by the formation of an intersubunit disulfide bond between cytochrome b and the iron-sulfur protein.” J Biol Chem 275, no. 49 (December 8, 2000): 38597–604. https://doi.org/10.1074/jbc.M007444200.
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