Joseph (Joey) Davis

Joseph (Joey) Davis

Associate Professor of Biology

Joey Davis investigates how cells maintain a delicate internal balance of assembling and dismantling their own machinery — in particular, assemblages of many molecules known as macromolecular complexes.

617-258-6154

Phone

68-671

Office

jhdavis@mit.edu

Email

Building 68 - Koch Biology Building

Location

Lab Website
Gina Lee

Assistant

617-258-6473

Assistant Phone

Education

  • PhD, 2010, MIT
  • BA,  2003, Computer Science, University of California, Berkeley
  • BS, 2003, Biological Engineering, University of California, Berkeley

Research Summary

The Davis lab is working to uncover how cells construct and degrade complex molecular machines rapidly and efficiently. We apply a variety of biochemical, biophysical, and structural approaches including quantitative mass spectrometry and single particle cryo-electron microscopy to understand the detailed molecular mechanisms of these processes. Ongoing projects in the lab are focused on autophagy, an essential eukaryotic protein and organelle degradation pathway, and assembly of the ribosome, which is essential in all cells.

Awards

  • Sloan Research Fellowship, Alfred P. Sloan Foundation, 2021
  • National Institute on Aging R00 Fellowship, 2017
  • National Institute on Aging K99 Fellowship, 2015

Recent Publications

  1. Imaging structurally dynamic ribosomes with cryogenic electron microscopy. Webster, SM, May, MB, Powell, BM, Davis, JH. 2023. ArXiv , .
    PMID:37693176
  2. KsgA facilitates ribosomal small subunit maturation by proofreading a key structural lesion. Sun, J, Kinman, LF, Jahagirdar, D, Ortega, J, Davis, JH. 2023. Nat Struct Mol Biol , .
    doi: 10.1038/s41594-023-01078-5PMID:37653244
  3. Application of monolayer graphene to cryo-electron microscopy grids for high-resolution structure determination. Grassetti, AV, May, MB, Davis, JH. 2023. bioRxiv , .
    doi: 10.1101/2023.07.28.550908PMID:37546934
  4. Learning structural heterogeneity from cryo-electron sub-tomograms with tomoDRGN. Powell, BM, Davis, JH. 2023. bioRxiv , .
    doi: 10.1101/2023.05.31.542975PMID:37398315
  5. The SspB adaptor drives structural changes in the AAA+ ClpXP protease during ssrA-tagged substrate delivery. Ghanbarpour, A, Fei, X, Baker, TA, Davis, JH, Sauer, RT. 2023. Proc Natl Acad Sci U S A 120, e2219044120.
    doi: 10.1073/pnas.2219044120PMID:36730206
  6. Cryo-EM at ACA 2022. Subramaniam, S, Kotecha, A, Davis, JH. 2022. IUCrJ 9, 713-714.
    doi: 10.1107/S2052252522009721PMID:36381144
  7. Uncovering structural ensembles from single-particle cryo-EM data using cryoDRGN. Kinman, LF, Powell, BM, Zhong, ED, Berger, B, Davis, JH. 2023. Nat Protoc 18, 319-339.
    doi: 10.1038/s41596-022-00763-xPMID:36376590
  8. Conformational landscape of the yeast SAGA complex as revealed by cryo-EM. Vasyliuk, D, Felt, J, Zhong, ED, Berger, B, Davis, JH, Yip, CK. 2022. Sci Rep 12, 12306.
    doi: 10.1038/s41598-022-16391-0PMID:35853968
  9. CryoDRGN: reconstruction of heterogeneous cryo-EM structures using neural networks. Zhong, ED, Bepler, T, Berger, B, Davis, JH. 2021. Nat Methods 18, 176-185.
    doi: 10.1038/s41592-020-01049-4PMID:33542510
  10. Structures of radial spokes and associated complexes important for ciliary motility. Gui, M, Ma, M, Sze-Tu, E, Wang, X, Koh, F, Zhong, ED, Berger, B, Davis, JH, Dutcher, SK, Zhang, R et al.. 2021. Nat Struct Mol Biol 28, 29-37.
    doi: 10.1038/s41594-020-00530-0PMID:33318703
More Publications

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