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Sci. Signal., 26 October 2010
[DOI: 10.1126/scisignal.2000738]

Supplementary Materials for:

Regulation of 3-Phosphoinositide–Dependent Protein Kinase 1 Activity by Homodimerization in Live Cells

Thomas A. Masters, Véronique Calleja, Daven A. Armoogum, Richard J. Marsh, Christopher J. Applebee, Michel Laguerre, Angus J. Bain,* Banafshé Larijani*

*To whom correspondence should be addressed. E-mail: banafshe.larijani{at}cancer.org.uk (B.L.); a.bain{at}ucl.ac.uk (A.J.B.)

This PDF file includes:

  • Methods
  • Fig. S1. Coimmunoprecipitation of myc-PDK1 with GFP-myc-PDK1 from COS-7 cells.
  • Fig. S2. In vitro phosphorylation of the PDKtide peptide by recombinant tagged PDK1.
  • Fig. S3. Analysis of sensitized acceptor fluorescence.
  • Fig. S4. Molecular modeling of the PDK1 homodimer.
  • Fig. S5. Example of the calculation of pixel enrichment.
  • Fig. S6. Probabilities that a PDK1 dimer can be detected by hetero-FRET.
  • Reference

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Technical Details

Format: Adobe Acrobat PDF

Size: 423 KB

Citation: T. A. Masters, V. Calleja, D. A. Armoogum, R. J. Marsh, C. J. Applebee, M. Laguerre, A. J. Bain, B. Larijani, Regulation of 3-Phosphoinositide–Dependent Protein Kinase 1 Activity by Homodimerization in Live Cells. Sci. Signal. 3, ra78 (2010).

© 2010 American Association for the Advancement of Science

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