The N-terminal region of RTP1S plays important roles in dimer formation and odorant receptor-trafficking.

Published

Journal Article

Receptor-transporting protein 1S (RTP1S) is an accessory protein that mediates the transport of mammalian odorant receptors (ORs) into the plasma membrane. Although most ORs fail to localize to the cell surface when expressed alone in nonolfactory cells, functional expression of ORs is achieved with the coexpression of RTP1S. However, the mechanism for RTP1S-mediated OR trafficking remains unclear. In this study, we attempted to reveal the mode of action and critical residues of RTP1S in OR trafficking. Experiments using N-terminal truncation and Ala substitution mutants of RTP1S demonstrated that four N-terminal amino acids have essential roles in OR trafficking. Additionally, using recombinant proteins and split luciferase assays in mammalian cells, we provided evidence for the dimer formation of RTP1S. Furthermore, we determined that the 2nd Cys residue is required for the efficient dimerization of RTP1S. Altogether, these findings provide insights into the mechanism for plasma membrane transport of ORs by RTP1S.

Full Text

Duke Authors

Cited Authors

  • Fukutani, Y; Tamaki, R; Inoue, R; Koshizawa, T; Sakashita, S; Ikegami, K; Ohsawa, I; Matsunami, H; Yohda, M

Published Date

  • October 4, 2019

Published In

Volume / Issue

  • 294 / 40

Start / End Page

  • 14661 - 14673

PubMed ID

  • 31395660

Pubmed Central ID

  • 31395660

Electronic International Standard Serial Number (EISSN)

  • 1083-351X

Digital Object Identifier (DOI)

  • 10.1074/jbc.RA118.007110

Language

  • eng

Conference Location

  • United States