Homomeric and heteromeric interactions of the extracellular domains of death receptors and death decoy receptors

Hyun Wook Lee, Seung Hyun Lee, Hae Won Lee, Yeon Woo Ryu, Myung Hee Kwon, Yong Sung Kim

Research output: Contribution to journalArticlepeer-review

55 Scopus citations

Abstract

Death receptors (DRs) can induce apoptosis by oligomerization with TRAIL, whereas death decoy receptors (DcRs) cannot, due to their lack of functional intracellular death domains. However, it is not known whether DRs and DcRs can interact with one another to form oligomeric complexes prior to TRAIL binding. To address this issue, the extracellular domains (ECDs) of DR4 (sDR4), DR5 (sDR5), DcR1 (sDcR1), and DcR2 (sDcR2) were expressed in a soluble, monomeric form, and their binding interactions were quantified by surface plasmon resonance. The purified sDRs and sDcRs exhibited native-like secondary structure and bound to TRAIL with binding affinities in the nanomolar range (K D = ∼10-62 nM), suggesting that they were properly folded and functional. The soluble receptors interacted homophilically and heterophilically with similar micromolar range affinities (KD = ∼1-9 μM), with the exception that sDR5 did not interact with the sDcRs. Our results suggest that most DRs and DcRs can laterally interact through their ECDs to form homomeric and/or heteromeric complexes in the absence of TRAIL binding.

Original languageEnglish (US)
Pages (from-to)1205-1212
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume330
Issue number4
DOIs
StatePublished - May 20 2005

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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