Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3-effector-GAP complex

FEBS Lett. 2008 Jul 23;582(17):2501-7. doi: 10.1016/j.febslet.2008.05.053. Epub 2008 Jun 25.

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

  • ADP-Ribosylation Factors / metabolism*
  • Adaptor Proteins, Signal Transducing
  • Amino Acid Sequence
  • Cyclic Nucleotide Phosphodiesterases, Type 6 / metabolism
  • Eye Proteins / metabolism*
  • GTP-Binding Proteins / metabolism*
  • GTPase-Activating Proteins / metabolism*
  • Guanosine Diphosphate / metabolism
  • Humans
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Membrane Proteins / metabolism*
  • Molecular Sequence Data
  • Photoreceptor Cells, Vertebrate / enzymology*
  • Protein Conformation
  • Signal Transduction

Substances

  • Adaptor Proteins, Signal Transducing
  • Eye Proteins
  • GTPase-Activating Proteins
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • RP2 protein, human
  • UNC119 protein, human
  • Guanosine Diphosphate
  • PDE6D protein, human
  • Cyclic Nucleotide Phosphodiesterases, Type 6
  • ARL2 protein, human
  • GTP-Binding Proteins
  • ADP-Ribosylation Factors
  • ARL3 protein, human