Adam Yokom, PhD

Assistant Professor


Contact Information

Phone 573-882-6390
Address 117 Schweitzer
Websites Yokom Group
Google Scholar


  • BS, Biochemistry, Oakland University, Rochester, MI
  • PhD, Chemical Biology, University of Michigan, Ann Arbor, MI
  • Postdoctoral Fellow, University of California, Berkeley, Berkeley, CA

Research Area

Protein-protein interactions that drive neurodegeneration and organelle fusion, cell biology, structural biology, biophysics, autophagy

Research Description

We are interested in discovering and understanding how protein and protein complexes regulate cellular organelles particularly in the conserved cellular pathway, Autophagy. Autophagy is a complex cascade of proteins interactions which promote the formation of a new double lipid bilayer autophagosome to encapsulate and break down cellular debris. This pathway influences development, cellular health, and protects cells against invading pathogens. Additionally, the autophagy pathway is implicated in numerous human diseases including neurodegenerative disease which are a emphasis within the group.

Our main goal is to use a combination of biochemical, biophysical and cell biological tools to identify new therapeutic avenues to prevent or treat human diseases. Currently, we are focusing on the molecular details of the membrane tethering complexes which anchor organelles together and promote membrane fusion between targeted organelles. Investigating these interactions will use techniques including cryo-electron microscopy and tomography, as well as cellular and biochemical assays.

Notable Honors and Service

  • 2019-2021 Inclusive MCB+, Postdoctoral Co-lead
  • 2018-2021 Jane Coffin Child’s Memorial Fund Fellow
  • 2015-2017 American Heart Association Predoctoral Fellowship

Selected Publications

A full list of publications can be found on Pubmed.

  • Ren X., Nguyen T.N., Wai Kit Lam, Buffalo C.Z., Lazarou M., Yokom A. L. +, Hurley J.H.+ Structural basis for ATG9A recruitment to the ULK1 complex in mitophagy initiation. In press Science Advances. doi:10.1101/2022.07.12.499634 (Feb. 2023) [+ co-corresponding authors]
  • Yokom, A. L.*, Shi, X.*, Chang, C.*, Jensen, L. E. & Hurley, J. H. The autophagy adaptor NDP52 and the FIP200 coiled-coil allosterically activate ULK1 complex membrane recruitment. eLife (2020). [*co-first authors]
  • Yokom A.L.*, Shi X* Wang C, Young L.N., Youle R.J., Hurley J.H. ULK complex organization in autophagy by a C-shaped FIP200 N-terminal domain dimer. Journal of Cell Biology (2020). [*co-first authors]
  • Yokom A.L.*, Horst B.G.*, Rosenberg D.J., Morris K.L., Hammel M., Hurley J.H., Marletta M.A. Allosteric activation of the nitric oxide receptor soluble guanylate cyclase mapped by cryo-electron microscopy. eLife. (2019). [*co-first authors]
  • Yokom A.L.*, Gates S.N.*, Lin J., Jackrel M.E., Rizo A.N., Kendsersky N.M., Buell C.E., Sweeny E.A., Chuang E., Torrente M.P., Mack K.L., Su M., Shorter J., Southworth D.R. Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104. Science (2017). [*co-first authors]
  • Yokom A.L., Gates S.N., Jackrel M.E., Mack K.L., Su M., Shorter J., Southworth D.R. Spiral architecture of the Hsp104disaggregase reveals the basis for polypeptide translocation. Nature Structural and Molecular Biology. (2016).