The Gos28 SNARE protein mediates intra-Golgi transport of rhodopsin and is required for photoreceptor survival.

Nansi Colley // Publications // Nov 21 2014

PubMed ID: 25261468

Author(s): Rosenbaum EE, Vasiljevic E, Cleland SC, Flores C, Colley NJ. The Gos28 SNARE protein mediates intra-Golgi transport of rhodopsin and is required for photoreceptor survival. J Biol Chem. 2014 Nov 21;289(47):32392-409. doi: 10.1074/jbc.M114.585166. Epub 2014 Sep 26. PMID 25261468

Journal: The Journal Of Biological Chemistry, Volume 289, Issue 47, Nov 2014

SNARE proteins play indispensable roles in membrane fusion events in many cellular processes, including synaptic transmission and protein trafficking. Here, we characterize the Golgi SNARE protein, Gos28, and its role in rhodopsin (Rh1) transport through Drosophila photoreceptors. Mutations in gos28 lead to defective Rh1 trafficking and retinal degeneration. We have pinpointed a role for Gos28 in the intra-Golgi transport of Rh1, downstream from α-mannosidase-II in the medial- Golgi. We have confirmed the necessity of key residues in Gos28’s SNARE motif and demonstrate that its transmembrane domain is not required for vesicle fusion, consistent with Gos28 functioning as a t-SNARE for Rh1 transport. Finally, we show that human Gos28 rescues both the Rh1 trafficking defects and retinal degeneration in Drosophila gos28 mutants, demonstrating the functional conservation of these proteins. Our results identify Gos28 as an essential SNARE protein in Drosophila photoreceptors and provide mechanistic insights into the role of SNAREs in neurodegenerative disease.

© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.