Dr Jeff Nanson

Research Fellow

School of Chemistry and Molecular Biosciences
Faculty of Science
j.nanson@uq.edu.au
+61 7 334 69073

Overview

Qualifications

  • Doctor of Philosophy, Charles Sturt University

Publications

  • Muusse, Timothy W., Lee, Morris Y.L., Kim, Hyoyoung, Parat, Marie-Odile, Nanson, Jeffrey D., Kobe, Bostjan, Vajjhala, Parimala R. and Stacey, Katryn J. (2022). Flow cytometric reporter assays provide robust functional analysis of signaling complexes. Journal of Biological Chemistry, 298 (12) 102666, 102666. doi: 10.1016/j.jbc.2022.102666

  • Manik, Mohammad K., Shi, Yun, Li, Sulin, Zaydman, Mark A., Damaraju, Neha, Eastman, Samuel, Smith, Thomas G., Gu, Weixi, Masic, Veronika, Mosaiab, Tamim, Weagley, James S., Hancock, Steven J., Vasquez, Eduardo, Hartley-Tassell, Lauren, Kargios, Nestoras, Maruta, Natsumi, Lim, Bryan Y. J., Burdett, Hayden, Landsberg, Michael J., Schembri, Mark A., Prokes, Ivan, Song, Lijiang, Grant, Murray, DiAntonio, Aaron, Nanson, Jeffrey D., Guo, Ming, Milbrandt, Jeffrey, Ve, Thomas and Kobe, Bostjan (2022). Cyclic ADP ribose isomers: Production, chemical structures, and immune signaling. Science, 377 (6614) eadc8969, eadc8969-+. doi: 10.1126/science.adc8969

  • Shi, Yun, Kerry, Philip S., Nanson, Jeffrey D., Bosanac, Todd, Sasaki, Yo, Krauss, Raul, Saikot, Forhad K., Adams, Sarah E., Mosaiab, Tamim, Masic, Veronika, Mao, Xianrong, Rose, Faith, Vasquez, Eduardo, Furrer, Marieke, Cunnea, Katie, Brearley, Andrew, Gu, Weixi, Luo, Zhenyao, Brillault, Lou, Landsberg, Michael J., DiAntonio, Aaron, Kobe, Bostjan, Milbrandt, Jeffrey, Hughes, Robert O. and Ve, Thomas (2022). Structural basis of SARM1 activation, substrate recognition, and inhibition by small molecules. Molecular Cell, 82 (9), 1643-1659.e10. doi: 10.1016/j.molcel.2022.03.007

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Supervision

  • Doctor Philosophy

  • Doctor Philosophy

  • Doctor Philosophy

View all Supervision

Available Projects

  • Toll-like receptors (TLRs) detect pathogen- and endogenous danger-associated molecules (PAMPs/DAMPs) and initiate innate immune responses that lead to the production of pro-inflammatory cytokines. TLR signal transduction occurs through the cytoplasmic Toll/interleukin-1 receptor (TIR) domain of the receptor. Upon activation of TLRs, the TIR domain of the receptor recruits TIR-containing adaptor proteins. Recruitment of these adaptors via TIR domain:TIR domain interactions orchestrates downstream signaling pathways, leading to induction of the pro-inflammatory genes.

    Recent efforts directed at elucidating the structural basis of TIR domain self-association suggest signaling by TLR and adaptor protein TIR domains occurs through a higher-order assembly mechanism termed signaling by co-operative assembly formation (SCAF) [1]. The TIR domain of adapter protein MAL has been shown to spontaneously form filaments (helical assemblies) in vitro, form assemblies with other TIR domains, and induce the formation of large MyD88 (myddosome-like) assemblies [2].

    This project involves spectroscopy, electron microscopy, and crystallography to determine the structure of TLR signaling assemblies, and investigate the molecular mechanisms involved in the assembly formation and downstream signaling.

    References [1] Nimma, S,. et al. (2017). “Towards the structure of the TIR-domain signalosome”. Current Opinion in Structural Biology, 43: 122-130. doi:10.1016/j.sbi.2016.12.014 [2] Ve, T,. et al. (2017). “Structural basis of TIR-domain-assembly formation in MAL- and MyD88-dependent TLR4 signaling”. Nature Structural and Molecular Biology, 24 9: 743-751. doi:10.1038/nsmb.3444

View all Available Projects

Publications

Journal Article

PhD and MPhil Supervision

Current Supervision

  • Doctor Philosophy — Associate Advisor

    Other advisors:

  • Doctor Philosophy — Associate Advisor

    Other advisors:

  • Doctor Philosophy — Associate Advisor

    Other advisors:

  • Doctor Philosophy — Associate Advisor

    Other advisors:

  • Doctor Philosophy — Associate Advisor

    Other advisors:

  • Doctor Philosophy — Associate Advisor

    Other advisors:

  • Doctor Philosophy — Associate Advisor

    Other advisors:

  • Doctor Philosophy — Associate Advisor

    Other advisors:

Possible Research Projects

Note for students: The possible research projects listed on this page may not be comprehensive or up to date. Always feel free to contact the staff for more information, and also with your own research ideas.

  • Toll-like receptors (TLRs) detect pathogen- and endogenous danger-associated molecules (PAMPs/DAMPs) and initiate innate immune responses that lead to the production of pro-inflammatory cytokines. TLR signal transduction occurs through the cytoplasmic Toll/interleukin-1 receptor (TIR) domain of the receptor. Upon activation of TLRs, the TIR domain of the receptor recruits TIR-containing adaptor proteins. Recruitment of these adaptors via TIR domain:TIR domain interactions orchestrates downstream signaling pathways, leading to induction of the pro-inflammatory genes.

    Recent efforts directed at elucidating the structural basis of TIR domain self-association suggest signaling by TLR and adaptor protein TIR domains occurs through a higher-order assembly mechanism termed signaling by co-operative assembly formation (SCAF) [1]. The TIR domain of adapter protein MAL has been shown to spontaneously form filaments (helical assemblies) in vitro, form assemblies with other TIR domains, and induce the formation of large MyD88 (myddosome-like) assemblies [2].

    This project involves spectroscopy, electron microscopy, and crystallography to determine the structure of TLR signaling assemblies, and investigate the molecular mechanisms involved in the assembly formation and downstream signaling.

    References [1] Nimma, S,. et al. (2017). “Towards the structure of the TIR-domain signalosome”. Current Opinion in Structural Biology, 43: 122-130. doi:10.1016/j.sbi.2016.12.014 [2] Ve, T,. et al. (2017). “Structural basis of TIR-domain-assembly formation in MAL- and MyD88-dependent TLR4 signaling”. Nature Structural and Molecular Biology, 24 9: 743-751. doi:10.1038/nsmb.3444