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
Tori Yetman

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. An asymmetric nautilus-like HflK/C assembly controls FtsH proteolysis of membrane proteins. Ghanbarpour, A, Telusma, B, Powell, BM, Zhang, JJ, Bolstad, I, Vargas, C, Keller, S, Baker, TA, Sauer, RT, Davis, JH et al.. 2025. EMBO J 44, 2501-2513.
    doi: 10.1038/s44318-025-00408-1PMID:40082723
  2. Automated model-free analysis of cryo-EM volume ensembles with SIREn. Kinman, LF, Carreira, MV, Powell, BM, Davis, JH. 2025. Structure 33, 974-987.e4.
    doi: 10.1016/j.str.2025.02.004PMID:40068687
  3. Rapid structural analysis of bacterial ribosomes in situ. Powell, BM, Brant, TS, Davis, JH, Mosalaganti, S. 2025. Commun Biol 8, 131.
    doi: 10.1038/s42003-025-07586-yPMID:39875527
  4. A proteolytic AAA+ machine poised to unfold protein substrates. Ghanbarpour, A, Sauer, RT, Davis, JH. 2024. Nat Commun 15, 9681.
    doi: 10.1038/s41467-024-53681-9PMID:39516482
  5. Automated model-free analysis of cryo-EM volume ensembles with SIREn. Kinman, LF, Carreira, MV, Powell, BM, Davis, JH. 2024. bioRxiv , .
    doi: 10.1101/2024.10.08.617123PMID:39415986
  6. Bulk and selective autophagy cooperate to remodel a fungal proteome in response to changing nutrient availability. Telusma, B, Farre, JC, Cui, DS, Subramani, S, Davis, JH. 2024. bioRxiv , .
    doi: 10.1101/2024.09.24.614842PMID:39386609
  7. An asymmetric nautilus-like HflK/C assembly controls FtsH proteolysis of membrane proteins. Ghanbarpour, A, Telusma, B, Powell, BM, Zhang, JJ, Bolstad, I, Vargas, C, Keller, S, Baker, T, Sauer, RT, Davis, JH et al.. 2024. bioRxiv , .
    doi: 10.1101/2024.08.09.604662PMID:39149393
  8. NCOA4 initiates ferritinophagy by binding GATE16 using two highly avid short linear interaction motifs. Lee, A, Davis, JH. 2024. bioRxiv , .
    doi: 10.1101/2024.06.09.597909PMID:38895392
  9. Rapid structural analysis of bacterial ribosomes in situ. Powell, BM, Brant, TS, Davis, JH, Mosalaganti, S. 2024. bioRxiv , .
    doi: 10.1101/2024.03.22.586148PMID:38585831
  10. Learning structural heterogeneity from cryo-electron sub-tomograms with tomoDRGN. Powell, BM, Davis, JH. 2024. Nat Methods 21, 1525-1536.
    doi: 10.1038/s41592-024-02210-zPMID:38459385
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