Photoreceptor synaptic protein HRG4 (UNC119) interacts with ARL2 via a putative conserved domain

Akira Kobayashi, Shinya Kubota, Naoki Mori, Margaret J. McLaren, George Inana

Research output: Contribution to journalArticle

40 Scopus citations

Abstract

Human retinal gene 4 (HRG4) (UNC119) is a photoreceptor synaptic protein of unknown function, shown when mutated to cause retinal degeneration in a patient and in a confirmatory transgenic model. ADP-ribosylation factor-like protein 2 (ARL2) was identified as an interactor of HRG4 by the yeast two-hybrid strategy. The presence of ARL2 in the retina and co-localization with HRG4 was confirmed by Western blot and double immunofluorescence analysis, respectively. The interaction of ARL2 with HRG4 was further confirmed by co-immunoprecipitation and direct binding analysis. Phosphodiesterase δ (PDEδ) is an ARL2-binding protein homologous to HRG4. Amino acid residues of PDEδ involved in binding ARL2 and forming a hydrophobic pocket were shown to be highly conserved in HRG4, suggesting similarity in binding mechanism and function.

Original languageEnglish (US)
Pages (from-to)26-32
Number of pages7
JournalFEBS letters
Volume534
Issue number1-3
DOIs
StatePublished - Jan 16 2003

Keywords

  • ADP-ribosylation factor-like protein 2
  • Human retinal gene 4
  • Interactor
  • Phosphodiesterase δ
  • UNC119
  • Yeast two-hybrid

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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