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

FEBS Letters

Mori, Naoki¹  McLaren, Margaret J.²  Kobayashi, Akira¹  Inana, George¹  Kubota, Shinya¹ 

[1] Bascom Palmer Eye Institute, University of Miami School of Medicine, 1638 N.W. 10th Avenue, Miami, FL 33136, USA;Gray Matter Research, 18495 S. Dixie Hwy, #161, Miami, FL 33157, USA

关键词: Human retinal gene 4;    UNC119;    Phosphodiesterase δ;    ADP-ribosylation factor-like protein 2;    Interactor;    Yeast two-hybrid;    HRG4;    human retinal gene 4;    PDEδ;    phosphodiesterase δ;    ARL2;    ADP-ribosylation factor-like protein 2;    TE;    Tris–ethylenediamine tetraacetic acid (EDTA);   

DOI  :  10.1016/S0014-5793(02)03766-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown