TRAIL-R4-beta: a new splice variant of TRAIL-receptor 4 lacking the cysteine rich domain 1

Biochem Biophys Res Commun. 2006 Oct 13;349(1):115-21. doi: 10.1016/j.bbrc.2006.08.031. Epub 2006 Aug 14.

Abstract

Transcriptional modification by alternative splicing is known to be involved in the regulation of programmed cell death. Recently, alternative splice variants of the TNF-related apoptosis inducing ligand (TRAIL/APO2L) and of the death receptor TRAIL-R2/DR5 have been identified. In this study, we report the identification of a novel alternative splice variant of the decoy receptor with a truncated death domain TRAIL-R4 lacking exon 3, which we designated TRAIL-R4-beta. As revealed by BLAST search we identified the genomic organisation of the TRAIL-R4 gene which consists of 9 exons. Loss of exon 3 resulted in the truncation of the first complete cysteine rich domain 1 which is known to be involved in ligand-receptor-complex. In conclusion, alternative splicing might be involved in functional fine-tuning of TRAIL-induced programmed cell death.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alternative Splicing
  • Amino Acid Sequence
  • Base Sequence
  • Cell Line, Tumor
  • Cysteine / chemistry*
  • Exons
  • Humans
  • Introns
  • Ligands
  • Molecular Sequence Data
  • Protein Isoforms
  • Protein Structure, Tertiary
  • Receptors, Tumor Necrosis Factor / biosynthesis*
  • Receptors, Tumor Necrosis Factor / genetics*
  • Sequence Homology, Amino Acid
  • Tumor Necrosis Factor Decoy Receptors

Substances

  • Ligands
  • Protein Isoforms
  • Receptors, Tumor Necrosis Factor
  • TNFRSF10D protein, human
  • Tumor Necrosis Factor Decoy Receptors
  • Cysteine