Yamasaki A, Hara T, Maejima I, Sato K (Lab. Mol. Traffic, IMCR, Gunma Univ.) Sato M, Sato K (Lab. Mol. Memb. Biol., IMCR, Gunma Univ.)
About
Rhodopsin is a pigment in photoreceptor cells. Some rhodopsin mutations cause the protein to accumulate in the endoplasmic reticulum (ER), leading to photoreceptor degeneration. Although several mutations have been reported, how mutant rhodopsin is retained in the ER remains unclear. In this study, we identified Rer1p as a modulator of ER retention and rhodopsin trafficking. Loss of Rer1p increased the transport of wild-type rhodopsin to post-Golgi compartments. Overexpression of Rer1p caused immature wild-type rhodopsin to accumulate in the ER. Interestingly, the G51R rhodopsin mutant, which has a mutation in the first transmembrane domain and accumulates in the ER, was released to the plasma membrane or lysosomes in Rer1-knockdown cells. Consistent with these results, Rer1p interacted with both wild-type and mutant rhodopsin. These results suggest that Rer1p regulates the ER retention of immature or misfolded rhodopsin and modulates its intracellular trafficking through the early secretory pathway.
Paper information
Rer1p regulates the ER retention of immature rhodopsin and modulates its intracellular trafficking.
Yamasaki A, Hara T, Maejima I, Sato M, Sato K, Sato K*.
Sci Rep. 6;4:5973. 2014
Online URL
http://www.ncbi.nlm.nih.gov/pubmed/25096327
