Iain M. Cheeseman

Iain M. Cheeseman

Herman and Margaret Sokol Professor of Biology; Core Member, Whitehead Institute; Associate Department Head

Iain Cheeseman analyzes the process by which cells duplicate, focusing on how the molecular machinery that segregates the chromosomes is rewired across diverse physiological contexts.

617-324-2503

Phone

WI-401B

Office

icheese@wi.mit.edu

Email

Whitehead Institute for Biomedical Research

Location

Lab Website
Brittany Brady

Assistant

617-258-9243

Assistant Phone

Education

  • PhD, 2002, University of California, Berkeley
  • BS, 1997, Biology, Duke University

Research Summary 

Our lab is fascinated by the molecular machinery that directs core cellular processes, and in particular how these processes are modulated and rewired across different physiological contexts. Our work has focused on the proteins that direct chromosome segregation and cell division, including the macromolecular kinetochore structure that mediates chromosome-microtubule interactions. Although cell division is an essential cellular process, this machinery is remarkably flexible in its composition and properties, which can vary dramatically between species and are even modulated within the same organism — over the cell cycle, during development, and across diverse physiological situations. To define the basis by which the kinetochore and other core cellular structures are rewired to adapt to diverse situations and functional requirements, we are currently investigating diverse transcriptional, translational, and post-translational mechanisms that act to generate proteomic variability both within individual cells and across tissues, cell state, development, and disease.

Awards

  • Global Consortium for Reproductive Longevity and Equality (GCRLE) Scholar Award, 2020
  • MIT Undergraduate Research Opportunities Program (UROP) Outstanding Mentor - Faculty, 2019
  • American Society for Cell Biology (ASCB) Early Career Life Scientist Award, 2012
  • Searle Scholar Award, 2009-2012
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Recent Publications

  1. SRSF12 is a primate-specific splicing factor that induces a tissue-specific gene expression program. Ly, J, Cady, SL, Haug, S, Khalizeva, E, Cheeseman, IM. 2025. Mol Biol Cell , mbcE25070352.
    doi: 10.1091/mbc.E25-07-0352PMID:41060796
  2. The dynamics of centromere assembly and disassembly during quiescence. Marescal, O, Su, KC, Moodie, B, Taylor, NJL, Cheeseman, IM. 2025. bioRxiv , .
    doi: 10.1101/2025.09.08.674938PMID:40964289
  3. Global inhibition of deadenylation stabilizes the transcriptome in mitotic cells. Khalizeva, E, Latifkar, A, Bartel, DP, Ly, J, Cheeseman, IM. 2025. bioRxiv , .
    doi: 10.1101/2025.07.22.666109PMID:40777404
  4. SRSF12 is a primate-specific splicing factor that induces a tissue-specific gene expression program. Ly, J, Cady, SL, Khalizeva, E, Haug, S, Cheeseman, IM. 2025. bioRxiv , .
    doi: 10.1101/2025.07.25.666902PMID:40777280
  5. 19S proteasome loss regulates mitotic spindle assembly through a ubiquitin-independent degradation mechanism. Marescal, O, Cheeseman, IM. 2025. Cell Rep 44, 116041.
    doi: 10.1016/j.celrep.2025.116041PMID:40705606
  6. Alternative start codon selection shapes mitochondrial function during evolution, homeostasis, and disease. Ly, J, Tao, YF, Di Bernardo, M, Khalizeva, E, Giuliano, CJ, Lourido, S, Fleming, MD, Cheeseman, IM. 2025. bioRxiv , .
    doi: 10.1101/2025.03.27.645657PMID:40196624
  7. Molecular determinants of RNase MRP specificity and function. Smith, EM, Ly, J, Haug, S, Cheeseman, IM. 2025. bioRxiv , .
    doi: 10.1101/2025.01.28.635360PMID:39974906
  8. 19S proteasome loss causes monopolar spindles through ubiquitin-independent KIF11 degradation. Marescal, O, Cheeseman, IM. 2025. bioRxiv , .
    doi: 10.1101/2025.01.08.632038PMID:39829864
  9. Co-essentiality analysis identifies PRR12 as a cohesin interacting protein and contributor to genomic integrity. Nguyen, AL, Smith, EM, Cheeseman, IM. 2025. Dev Cell 60, 1217-1233.e7.
    doi: 10.1016/j.devcel.2024.12.015PMID:39742660
  10. Functional genetics reveals modulators of antimicrotubule drug sensitivity. Su, KC, Radul, E, Maier, NK, Tsang, MJ, Goul, C, Moodie, B, Marescal, O, Keys, HR, Cheeseman, IM. 2025. J Cell Biol 224, .
    doi: 10.1083/jcb.202403065PMID:39570287
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Photo credit: Gretchen Ertl/Whitehead Institute

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