Strong dimerization of wild-type ErbB2/Neu transmembrane domain and the oncogenic Val664Glu mutant in mammalian plasma membranes

Jesse Placone, Lijuan He, Nuala Del Piccolo, Kalina Hristova

Research output: Contribution to journalArticle

Abstract

Here, we study the homodimerization of the transmembrane domain of Neu, as well as an oncogenic mutant (V664E), in vesicles derived from the plasma membrane of mammalian cells. For the characterization, we use a Förster resonance energy transfer (FRET)-based method termed Quantitative Imaging-FRET (QI-FRET), which yields the donor and acceptor concentrations in addition to the FRET efficiencies in individual plasma membrane-derived vesicles. Our results demonstrate that both the wild-type and the mutant are 100% dimeric, suggesting that the Neu TM helix dimerizes more efficiently than other RTK TM domains in mammalian membranes. Furthermore, the data suggest that the V664E mutation causes a very small, but statistically significant change in dimer structure. This article is part of a Special Issue entitled: Interfacially Active Peptides and Proteins. Guest Editors: William C. Wimley and Kalina Hristova.

Original languageEnglish (US)
Pages (from-to)2326-2330
Number of pages5
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1838
Issue number9
DOIs
StatePublished - Sep 2014

Keywords

  • Dimerization
  • Transmembrane domain

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

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