TULIPs: tunable, light-controlled interacting protein tags for cell biology

Nat Methods. 2012 Mar 4;9(4):379-84. doi: 10.1038/nmeth.1904.


Naturally photoswitchable proteins offer a means of directly manipulating the formation of protein complexes that drive a diversity of cellular processes. We developed tunable light-inducible dimerization tags (TULIPs) based on a synthetic interaction between the LOV2 domain of Avena sativa phototropin 1 (AsLOV2) and an engineered PDZ domain (ePDZ). TULIPs can recruit proteins to diverse structures in living yeast and mammalian cells, either globally or with precise spatial control using a steerable laser. The equilibrium binding and kinetic parameters of the interaction are tunable by mutation, making TULIPs readily adaptable to signaling pathways with varying sensitivities and response times. We demonstrate the utility of TULIPs by conferring light sensitivity to functionally distinct components of the yeast mating pathway and by directing the site of cell polarization.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Avena / chemistry
  • Cell Biology*
  • Cell Polarity
  • Enzyme Activation
  • Kinetics
  • Lasers
  • Light*
  • Mitogen-Activated Protein Kinases / metabolism
  • Models, Molecular
  • Mutation
  • PDZ Domains
  • Phototropins / chemistry
  • Phototropins / genetics
  • Phototropins / metabolism
  • Protein Binding / genetics
  • Protein Binding / radiation effects
  • Protein Engineering*
  • Protein Transport / radiation effects
  • Proteins / chemistry
  • Proteins / genetics
  • Proteins / metabolism*
  • Saccharomyces cerevisiae / cytology
  • Saccharomyces cerevisiae / enzymology


  • Phototropins
  • Proteins
  • Mitogen-Activated Protein Kinases