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Related Experiment Video

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

David R Croucher1, Mary Iconomou2, Jordan F Hastings2

  • 1The Kinghorn Cancer Centre, Garvan Institute of Medical Research, Sydney, New South Wales 2010, Australia. St. Vincent's Hospital Clinical School, University of New South Wales, Sydney, New South Wales 2052, Australia. School of Medicine, University College Dublin, Belfield, Dublin D4, Ireland. d.croucher@garvan.org.au d.saunders@unsw.edu.au.

Science Signaling
|July 14, 2016
PubMed
Summary

Researchers developed a new method, bimolecular complementation affinity purification (BiCAP), to study protein interactions. This technique identified novel signaling pathways involving ERBB2 dimers, including a new mechanism for extracellular signal-regulated kinase (ERK) activation in breast cancer.

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Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Proteomics

Background:

  • Multiprotein complex assembly is crucial for cell signaling specificity and adaptability.
  • Existing methods struggle to isolate specific interacting protein pairs from complex cellular environments.

Purpose of the Study:

  • To introduce and validate a novel technique, bimolecular complementation affinity purification (BiCAP), for isolating specific protein-protein interactions.
  • To characterize the unique interactomes of ERBB2 homodimers and heterodimers with EGFR and ERBB3.

Main Methods:

  • Developed BiCAP, integrating conformation-specific nanobodies with protein-fragment complementation assay and affinity purification.
  • Applied BiCAP to isolate and proteomically characterize ERBB2 homodimers and ERBB2:EGFR and ERBB2:ERBB3 heterodimers.
  • Performed functional analysis on newly identified interacting partners.

Main Results:

  • BiCAP successfully isolated specific interacting protein pairs, excluding non-specific binders.
  • Identified dimer-specific interaction patterns for adaptor proteins associated with ERBB2 dimers.
  • Discovered previously unknown interacting partners and a novel, dimer-specific ERK activation mechanism mediated by FAM59A in ERBB2:ERBB3 heterodimers within breast cancer cells.

Conclusions:

  • BiCAP is an effective method for studying specific protein-protein interactions within dynamic signaling pathways.
  • ERBB2 dimerization status dictates specific protein interactions and signaling outputs.
  • A novel FAM59A-dependent, ERBB2:ERBB3 heterodimer-specific ERK activation pathway exists in breast cancer.