Biography

Dr. Ohi graduated from Vanderbilt University in 1993 with a B.S. in Molecular Biology. He received his Ph.D. in 1998 in Cell Biology from Vanderbilt University and completed post-doctoral training at Harvard Medical School with Professor Tim Mitchison. Dr. Ohi established his independent research program at Vanderbilt in 2007, where he remained as a tenured faculty member until 2017. In 2017, Dr. Ohi relocated to the University of Michigan where he rose to the rank of Professor of Cell and Developmental Biology. Dr. Ohi also served as Associate Chair of Education and Training in the Department of Cell and Developmental Biology. In October, 2025, Dr. Ohi moved his laboratory to the University of New Mexico where he is a Professor of Internal Medicine. Dr. Ohi’s research focuses on the microtubule cytoskeleton and on mechanisms that underlie mitotic spindle assembly and function. Research in his laboratory is currently funded by an R35 grant from the National Institutes of Health.

Personal Statement

A living cell buzzes with activity. Cells crawl, sense their environment, and carry out essential processes such as DNA replication and division. More specialized cells form unique structures and display behaviors required for their specific functions. For example, neutrophils, a type of white blood cell, seek out and destroy bacterial and fungal invaders, playing a critical role in fighting infection. Neurons extend elaborate processes (axons and dendrites) that allow them to transmit information throughout the nervous system. Muscle cells contract and make up the three muscle systems in the human body: cardiac, skeletal, and smooth.

The biology of all cells depends on the coordinated actions of the cytoskeleton, a system of filaments—microtubules, actin, and intermediate filaments—that continually assemble and remodel on the timescale of seconds to minutes. Microtubules and actin are especially dynamic, making them indispensable for countless cellular processes.

Work in the Ohi laboratory focuses on the microtubule cytoskeleton. We are broadly interested in how cells construct complex cytoskeletal networks from microtubules and deploy them to achieve an astonishing range of functions. The Ohi lab has a long history of studying microtubule organization and regulation during mitosis, with particular attention to how cells build and maintain a bipolar mitotic spindle to segregate chromosomes. More recently, we have become interested in how cells mark subsets of microtubules with chemical modifications that alter their interactions with microtubule-associated proteins (MAPs). Through this “Tubulin Code,” the cell programs its microtubule cytoskeleton to accurately drive processes ranging from cell division to cell migration, neurite formation, and muscle contraction.

Areas of Specialty

Microtubule cytoskeleton
Post-translational modifications
Microtubule-associated proteins
Kinesins
Mitosis

Achievements & Awards

2000-2003 Ruth L. Kirchstein National Research Service Award from NIH/NIGMS
2004-2007 Special Fellow of the Leukemia and Lymphoma Society
2009 FASEB Young Investigator Award, FASEB Mitosis Conference, Lucca, Italy
2010 American Cancer Society, Research Scholar Grant (Declined for R01)
2011-2012 VICC Young Ambassadors’ Discovery Grant
2012 FASEB Young Investigator Award, FASEB Mitosis Conference, Steamboat Springs, CO
2013-2018 Scholar of the Leukemia and Lymphoma Society
2013 VICC High Impact Publication Award
2018-2024 Co-Chair, ASCB Public Information Committee (PIC, now SCOPE)
2022-2025 Standing Member, NCSD, CSF1 and MRAC Study Sections
2025 Fellow of the American Society for Cell Biology

Key Publications

Journal Article
Hotta, Takashi, Pimm, M, L Thomas, Elaine, Yue, Y, DeLear, P, Blasius, L, Cianfrocco, M, A DeSantis, M, E Horiuchi, R, Higaki, T, Sept, D, Ohi, Ryoma, Verhey, K, J 2025 Accessibility of the unstructured ?-tubulin C-terminal tail is controlled by microtubule lattice conformation. bioRxiv : the preprint server for biology
Journal Article
Hotta, Takashi, McAlear, T, S Yue, Y, Higaki, T, Haynes, S, E Nesvizhskii, A, I Sept, D, Verhey, K, J Bechstedt, S, Ohi, Ryoma, 2022 EML2-S constitutes a new class of proteins that recognizes and regulates the dynamics of tyrosinated microtubules. Current biology : CB, vol. 32, Issue 18, 3898-3910.e14
Journal Article
Yue, Y, Hotta, Takashi, Higaki, T, Verhey, K, J Ohi, Ryoma, 2023 Microtubule detyrosination by VASH1/SVBP is regulated by the conformational state of tubulin in the lattice. Current biology : CB, vol. 33, Issue 19, 4111-4123.e7
Journal Article
Solon, A, L Zaniewski, T, M O'Brien, P, Clasby, M, Hancock, W, O Ohi, Ryoma, 2022 Synergy between inhibitors of two mitotic spindle assembly motors undermines an adaptive response. Molecular biology of the cell, vol. 33, Issue 14, ar132
Journal Article
Sturgill, E, G Norris, S, R Guo, Y, Ohi, Ryoma, 2016 Kinesin-5 inhibitor resistance is driven by kinesin-12. The Journal of cell biology, vol. 213, Issue 2, 213-27

Gender

Male

Languages

  • English

Research and Scholarship

1) Yue, Y., Hotta, T., Higaki, T., Verhey, K.V., and Ohi, R. (2023) Microtubule detyrosination by VASH1/SVBP is regulated by the conformational state of tubulin in the lattice. Curr. Biol., 33(19):4111-4123.

2) Solon AL, Zaniewski TM, O'Brien P, Clasby M, Hancock WO, Ohi R. (2022) Synergy between inhibitors of two mitotic spindle assembly motors undermines an adaptive response. Mol. Biol. Cell., 33(14): ar132, 12/2022.

3) Hotta T, McAlear TS, Yue Y, Higaki T, Haynes SE, Nesvizhskii AI, Sept D, Verhey KJ, Bechstedt S, Ohi R. (2022) EML2-S constitutes a new class of proteins that recognizes and regulates the dynamics of tyrosinated microtubules. Curr. Biol., 32(18): 3898-3910.e14, 09/2022.

4) Solon AL, Tan Z, Schutt KL, Jepsen L, Haynes SE, Nesvizhskii AI, Sept D, Stumpff J, Ohi R, Cianfrocco MA. (2021) Kinesin-binding protein remodels the kinesin motor to prevent microtubule binding. Sci Adv., 7(47)11/2021.

5) Sturgill, E.G., Norris, S.R., Guo, Y., and Ohi, R. (2016) Kinesin-5 Inhibitor Resistance is Driven by Kinesin-12. J. Cell. Biol., 213:213-227.