Abstract
Arl2 and Arl3, members of the Arf subfamily of small G proteins, are believed to be involved in ciliary and microtubule-dependent processes. Recently, we could identify RP2, responsible for a variant of X-linked retinitis pigmentosa, as the Arl3-specific GAP. Here, we have characterized Arl2/3 interactions. We show the formation of a ternary complex between Arl3, its cognate GAP RP2 and its retinal effector HRG4. This complex seems to be important for photoreceptor function.
MeSH terms
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ADP-Ribosylation Factors / metabolism*
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Adaptor Proteins, Signal Transducing
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Amino Acid Sequence
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Cyclic Nucleotide Phosphodiesterases, Type 6 / metabolism
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Eye Proteins / metabolism*
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GTP-Binding Proteins / metabolism*
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GTPase-Activating Proteins / metabolism*
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Guanosine Diphosphate / metabolism
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Humans
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Intracellular Signaling Peptides and Proteins / metabolism*
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Membrane Proteins / metabolism*
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Molecular Sequence Data
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Photoreceptor Cells, Vertebrate / enzymology*
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Protein Conformation
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Signal Transduction
Substances
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Adaptor Proteins, Signal Transducing
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Eye Proteins
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GTPase-Activating Proteins
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Intracellular Signaling Peptides and Proteins
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Membrane Proteins
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RP2 protein, human
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UNC119 protein, human
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Guanosine Diphosphate
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PDE6D protein, human
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Cyclic Nucleotide Phosphodiesterases, Type 6
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ARL2 protein, human
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GTP-Binding Proteins
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ADP-Ribosylation Factors
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ARL3 protein, human