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

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

doi:10.1016/S0014-5793(02)03766-3

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

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

Ophthalmology

Research output: Contribution to journal › Article › peer-review

41 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 language	English (US)
Pages (from-to)	26-32
Number of pages	7
Journal	FEBS letters
Volume	534
Issue number	1-3
DOIs	https://doi.org/10.1016/S0014-5793(02)03766-3
State	Published - 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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@article{9b01890f3ecb4796affff2a258161e6f,

title = "Photoreceptor synaptic protein HRG4 (UNC119) interacts with ARL2 via a putative conserved domain",

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.",

keywords = "ADP-ribosylation factor-like protein 2, Human retinal gene 4, Interactor, Phosphodiesterase δ, UNC119, Yeast two-hybrid",

author = "Akira Kobayashi and Shinya Kubota and Naoki Mori and McLaren, {Margaret J.} and George Inana",

note = "Funding Information: This work was supported by the NIH (EY10848), the Foundation Fighting Blindness, Inc., and the Research to Prevent Blindness, Inc.",

year = "2003",

month = jan,

day = "16",

doi = "10.1016/S0014-5793(02)03766-3",

language = "English (US)",

volume = "534",

pages = "26--32",

journal = "FEBS Letters",

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T1 - Photoreceptor synaptic protein HRG4 (UNC119) interacts with ARL2 via a putative conserved domain

AU - Kobayashi, Akira

AU - Kubota, Shinya

AU - Mori, Naoki

AU - McLaren, Margaret J.

AU - Inana, George

N1 - Funding Information: This work was supported by the NIH (EY10848), the Foundation Fighting Blindness, Inc., and the Research to Prevent Blindness, Inc.

PY - 2003/1/16

Y1 - 2003/1/16

N2 - 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.

AB - 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.

KW - ADP-ribosylation factor-like protein 2

KW - Human retinal gene 4

KW - Interactor

KW - Phosphodiesterase δ

KW - UNC119

KW - Yeast two-hybrid

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