Supplementary Materials

Supplementary Materials for:

Bimolecular complementation affinity purification (BiCAP) reveals dimer-specific protein interactions for ERBB2 dimers

David R. Croucher,* Mary Iconomou, Jordan F. Hastings, Sean P. Kennedy, Jeremy Z. R. Han, Robert F. Shearer, Jessie McKenna, Adrian Wan, Joseph Lau, Samuel Aparicio, Darren N. Saunders*

*Corresponding author. Email: d.croucher{at}garvan.org.au (D.R.C.); d.saunders{at}unsw.edu.au (D.N.S.)

This PDF file includes:

  • Fig. S1. BiFC detection of ERBB2 dimers.
  • Fig. S2. BiFC analysis of ERBB3:ERBB2 heterodimer and costaining with an antibody toward the Golgi body marker GM-130.
  • Fig. S3. Validation of novel interactors from MS data.
  • Fig. S4. ERBB2 coimmunoprecipitation of ERBB3.
  • Fig. S5. PLA controls.
  • Fig. S6. Validation of FAM59A knockdown in SKBR3 cells.
  • Fig. S7. BiFC vector construction.
  • Fig. S8. Pegasus statistical analysis workflow.
  • Table S1. MaxQuant parameters.
  • Legends for tables S2 and S3
  • Reference (66)

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Technical Details

Format: Adobe Acrobat PDF

Size: 1.2 MB

Other Supplementary Material for this manuscript includes the following:

  • Table S2 (Microsoft Excel format). MaxQuant output.
  • Table S3 (Microsoft Excel format). LFQ proteomics analysis of ERBB2 dimer interactomes isolated by BiCAP.

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Citation: D. R. Croucher, M. Iconomou, J. F. Hastings, S. P. Kennedy, J. Z. R. Han, R. F. Shearer, J. McKenna, A. Wan, J. Lau, S. Aparicio, D. N. Saunders, Bimolecular complementation affinity purification (BiCAP) reveals dimer-specific protein interactions for ERBB2 dimers. Sci. Signal. 9, ra69 (2016).

© 2016 American Association for the Advancement of Science