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Mikko Taipale


  • CIFAR Azrieli Global Scholar 2016-2018
  • Molecular Architecture of Life


Taipale Lab


Mikko Taipale is fascinated with the birth, life and death of proteins. Right after their birth, all proteins need to adopt their intricate three-dimensional shape and find the right localization in the cell. They do so with the help of an ancient network of highly conserved chaperones and co-chaperones. After adopting the right shape in the right place, all proteins must interact with other proteins and biomolecules within the greater context of cellular interaction networks. And when their time has come, all proteins must be degraded in an orderly manner through the ubiquitin-proteasome system.

Taipale’s laboratory is using modern high-throughput functional proteomics tools to characterize how these networks of chaperones, co-chaperones and the ubiquitin-proteasome system are organized, and also how protein-protein interaction specificity is achieved in the crowded environment of the cell. In particular, Taipale is interested in understanding how these networks are rewired in cancer and in rare Mendelian disorders. The Taipale lab also has a strong emphasis on technology development for detecting and characterizing new biomolecular interactions.


  • Canada Research Chair in Functional Proteomics and Proteostasis, 2016
  • Ontario Research Foundation Early Researcher Award, 2016
  • Margaret and Herman Sokol Postdoctoral Award, 2012
  • Human Frontier Science Program Postdoctoral Award, 2007

Relevant Publications

  • Sahni, N. et al. "Widespread macromolecular interaction perturbations in human genetic disorders." Cell 161, no. 3 (2015): 647–60.
  • Taipale, M. et al. "A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways." Cell 158, no. 2 (2014): 434–48.
  • Taipale, M. et al. "Chaperones as thermodynamic sensors of drug-target interactions reveal kinase inhibitor specificities in living cells." Nature Biotechnology 31, no. 7 (2013): 630–37.
  • Taipale, M. et al. "Quantitative analysis of Hsp90-client interactions reveals principles of substrate recognition." Cell 150, no. 5 (2012): 987–1001.
  • Taipale, M., D.F. Jarosz, and S. Lindquist. "Hsp90 at the hub of protein homeostasis: emerging mechanistic insights." Nat. Rev. Mol. Cell Biol. 11, no. 7 (2010): 515–28.

Support Us

CIFAR is a registered charitable organization supported by the governments of Canada, Alberta and Quebec, as well as foundations, individuals, corporations and Canadian and international partner organizations.

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