Light regulation of protein dimerization and kinase activity in living cells using photocaged rapamycin and engineered FKBP

J Am Chem Soc. 2011 Jan 26;133(3):420-3. doi: 10.1021/ja109630v. Epub 2010 Dec 16.

Abstract

We developed a new system for light-induced protein dimerization in living cells using a photocaged analogue of rapamycin together with an engineered rapamycin binding domain. Using focal adhesion kinase as a target, we demonstrated successful light-mediated regulation of protein interaction and localization in living cells. Modification of this approach enabled light-triggered activation of a protein kinase and initiation of kinase-induced phenotypic changes in vivo.

Publication types

  • Research Support, American Recovery and Reinvestment Act
  • Research Support, N.I.H., Extramural

MeSH terms

  • Dimerization
  • Focal Adhesion Protein-Tyrosine Kinases / metabolism*
  • HEK293 Cells
  • Humans
  • Light*
  • Models, Molecular
  • Molecular Dynamics Simulation
  • Sirolimus / chemistry*
  • Tacrolimus Binding Proteins / chemistry
  • Tacrolimus Binding Proteins / metabolism*

Substances

  • Focal Adhesion Protein-Tyrosine Kinases
  • Tacrolimus Binding Proteins
  • Sirolimus