David Pellman

David Pellman, M.D.

Margaret M. Dyson Professor of Pediatric Oncology (Dana-Farber Cancer Institute)
Professor of Cell Biology (HMS)
HHMI Investigator

David Pellman, M.D. is the Margaret M. Dyson Professor of Pediatric Oncology at the Dana-Farber Cancer Institute, a Professor of Cell Biology at Harvard Medical School, an Investigator of the Howard Hughes Medical Institute, and the Associate Director for Basic Science at the Dana-Farber/Harvard Cancer Center.  He received his undergraduate and medical degrees from the University of Chicago.  During medical school, he did research at the Rockefeller University.  His postdoctoral fellowship was at the Whitehead Institute/Massachusetts Institute of Technology.

The Pellman Lab works on the mechanism of cell division and how certain cell division errors drive rapid genome evolution.  The normal processes studied in the laboratory have included spindle positioning and asymmetric cell division, the mechanism of spindle assembly and cytokinesis, and the mechanism of nuclear envelope assembly and how it is coordinated with chromosome segregation.  The mutational processes studied in David’s group are particularly important for cancer, but have relevance for genome evolution in other contexts.  Current projects include: the mechanism of a newly discovered mutational process called “chromothripsis”, how the architecture and integrity of the nuclear envelope impacts genome maintenance, and the role of cytoplasmic chromatin in triggering innate immune proinflammatory signaling. The lab uses a variety of approaches which include, molecular genetics, biochemistry, and imaging.  Currently there is a heavy emphasis on using a combination of live-cell imaging and single-cell genome sequencing developed in the lab (“Look-Seq”) to relate the consequences of cell division errors to genome alterations. 

Dana Farber Cancer Institute

Dept. of Pediatrics, Mayer-612

450 Brookline Ave

Boston, MA 02115

Lab phone: 617-632-4918

Lab fax: 617-632-5363

An actin nucleation mechanism mediated by Bni1 and profilin.
Authors: Authors: Sagot I, Rodal AA, Moseley J, Goode BL, Pellman D.
Nat Cell Biol
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Yeast formins regulate cell polarity by controlling the assembly of actin cables.
Authors: Authors: Sagot I, Klee SK, Pellman D.
Nat Cell Biol
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Analysis of the size and shape of protein complexes from yeast.
Authors: Authors: Schuyler SC, Pellman D.
Methods Enzymol
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Polyploids require Bik1 for kinetochore-microtubule attachment.
Authors: Authors: Lin H, de Carvalho P, Kho D, Tai CY, Pierre P, Fink GR, Pellman D.
J Cell Biol
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The social life of actin and microtubules: interaction versus cooperation.
Authors: Authors: Yarm F, Sagot I, Pellman D.
Curr Opin Microbiol
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A two-tiered mechanism by which Cdc42 controls the localization and activation of an Arp2/3-activating motor complex in yeast.
Authors: Authors: Lechler T, Jonsdottir GA, Klee SK, Pellman D, Li R.
J Cell Biol
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Separase anxiety: dissolving the sister bond and more.
Authors: Authors: Pellman D, Christman MF.
Nat Cell Biol
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Activity of the APC(Cdh1) form of the anaphase-promoting complex persists until S phase and prevents the premature expression of Cdc20p.
Authors: Authors: Huang JN, Park I, Ellingson E, Littlepage LE, Pellman D.
J Cell Biol
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Microtubule "plus-end-tracking proteins": The end is just the beginning.
Authors: Authors: Schuyler SC, Pellman D.
Cell
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Rvb1p and Rvb2p are essential components of a chromatin remodeling complex that regulates transcription of over 5% of yeast genes.
Authors: Authors: Jónsson ZO, Dhar SK, Narlikar GJ, Auty R, Wagle N, Pellman D, Pratt RE, Kingston R, Dutta A.
J Biol Chem
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