Sorting of lipidated cargo by the Arl2/Arl3 system.
Arl2 and Arl3 are Arf-like small GTP-binding proteins of the Arf subfamily of the Ras superfamily. Despite their structural similarity and sharing of many interacting partners, Arl2 and Arl3 have different biochemical properties and biological functions. Growing evidence suggest that Arl2 and Arl3 play a fundamental role as regulators of trafficking of lipid modified proteins between different compartments. Here we highlight the similarities and differences between these 2 homologous proteins and discuss the sorting mechanism of lipidated cargo into the ciliary compartment through the carriers PDE6δ and Unc119 and the release factors Arl2 and Arl3.
a Max Planck Institute of Molecular Physiology , Dortmund , Germany.
Eyad K
EK
Fansa
a Max Planck Institute of Molecular Physiology , Dortmund , Germany.
Alfred
A
Wittinghofer
D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D002923:Cilia / Q000378:metabolism; D054707:Cyclic Nucleotide Phosphodiesterases, Type 6 / Q000737:chemistry / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D011485:Protein Binding; D021381:Protein Transport
D048868:Adaptor Proteins, Signal Transducing; C098032:UNC119 protein, human; C517432:PDE6D protein, human; D054707:Cyclic Nucleotide Phosphodiesterases, Type 6; D019204:GTP-Binding Proteins
Arl2; Arl3; Arls; PDE6б prenyl transferases; Unc119; cargo release; cilia; myristoylation; prenylation; small GTPases and their effector proteins; sorting signal; structural biology and protein-protein interactions; structure/function studies