title: The Function of Arf-like Proteins ARL2 and ARL3 in Photoreceptors.
abstract: Arf-like proteins (ARLs) are ubiquitously expressed small G proteins of the RAS superfamily. In photoreceptors, ARL2 and ARL3 participate in the trafficking of lipidated membrane-associated proteins and colocalize in the inner segment with UNC119A and PDEδ. UNC119A and PDEδ are acyl- and prenyl-binding proteins, respectively, involved in trafficking of acylated (transducin-α subunit, nephrocystin NPHP3) and prenylated proteins (GRK1, PDE6). Germline Arl3 knockout mice do not survive beyond postnatal day 21 and display ciliary defects in multiple organs (kidney, liver and pancreas) as well as retinal degeneration. Conditional knockouts will be necessary to delineate mechanisms of protein transport in retina disease.
authors.affiliation: Department of Physical Biochemistry, University of Potsdam, Karl-Liebknecht-Strasse 24-25, 14476, Potsdam, Germany. christin.hanke@hsc.utah.edu.|Department of Ophthalmology, John A. Moran Eye Center, University of Utah Health Science Center, 65 Mario Capecchi Drive, 84132, Salt Lake City, UT, USA. christin.hanke@hsc.utah.edu.
authors.forename: Christin
authors.initials: C
authors.lastname: Hanke-Gogokhia
authors.affiliation: Sichuan Academy of Medical Sciences & Sichuan Provincial People's Hospital, Chengdu, Sichuan, China.
authors.forename: Houbin
authors.initials: H
authors.lastname: Zhang
authors.affiliation: Department of Ophthalmology, John A. Moran Eye Center, University of Utah Health Science Center, 65 Mario Capecchi Drive, 84132, Salt Lake City, UT, USA. Jeanne.frederick@hsc.utah.edu.
authors.forename: Jeanne M
authors.initials: JM
authors.lastname: Frederick
authors.affiliation: Department of Ophthalmology, John A. Moran Eye Center, University of Utah Health Science Center, 65 Mario Capecchi Drive, 84132, Salt Lake City, UT, USA. wbaehr@hsc.utah.edu.|Department of Neurobiology and Anatomy, University of Utah Health Science Center, 20 North 1900 East, Room 401 MREB, 84132, Salt Lake City, UT, USA. wbaehr@hsc.utah.edu.|Department of Biology, University of Utah, 257 South 1400 East, 84112, Salt Lake City, UT, USA. wbaehr@hsc.utah.edu.
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Baehr
mesh_terms: D020727:ADP-Ribosylation Factors / Q000235:genetics / Q000378:metabolism*; D048868:Adaptor Proteins, Signal Transducing / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D054707:Cyclic Nucleotide Phosphodiesterases, Type 6 / Q000378:metabolism; D005136:Eye Proteins / Q000235:genetics / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000235:genetics / Q000378:metabolism; D018345:Mice, Knockout; D008969:Molecular Sequence Data; D020419:Photoreceptor Cells, Vertebrate / Q000378:metabolism*; D011485:Protein Binding; D021381:Protein Transport; D017386:Sequence Homology, Amino Acid
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D005136:Eye Proteins; C489115:Unc119 protein, mouse; D054707:Cyclic Nucleotide Phosphodiesterases, Type 6; C485819:Arl2 protein, mouse; D019204:GTP-Binding Proteins; C490248:Arl3 protein, mouse; D020727:ADP-Ribosylation Factors
keywords: Arf-like protein 2 (ARL2); Arf-like protein 3 (ARL3); Phosphodiesterase δ-subunit (PDEδ); Retinitis pigmentosa protein 2 (RP2); Rod photoreceptor; unc-119 homolog (C. elegans) (UNC119A)