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

Publication ,  Journal Article
Fukutani, Y; Tamaki, R; Inoue, R; Koshizawa, T; Sakashita, S; Ikegami, K; Ohsawa, I; Matsunami, H; Yohda, M
Published in: J Biol Chem
October 4, 2019

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.

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Published In

J Biol Chem

DOI

EISSN

1083-351X

Publication Date

October 4, 2019

Volume

294

Issue

40

Start / End Page

14661 / 14673

Location

United States

Related Subject Headings

  • Receptors, Odorant
  • Receptors, G-Protein-Coupled
  • Protein Transport
  • Odorants
  • Molecular Chaperones
  • Mice
  • Membrane Transport Proteins
  • Humans
  • HEK293 Cells
  • Flow Cytometry
 

Citation

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Fukutani, Y., Tamaki, R., Inoue, R., Koshizawa, T., Sakashita, S., Ikegami, K., … Yohda, M. (2019). The N-terminal region of RTP1S plays important roles in dimer formation and odorant receptor-trafficking. J Biol Chem, 294(40), 14661–14673. https://doi.org/10.1074/jbc.RA118.007110
Fukutani, Yosuke, Ryohei Tamaki, Ryosuke Inoue, Tomoyo Koshizawa, Shuto Sakashita, Kentaro Ikegami, Ikuroh Ohsawa, Hiroaki Matsunami, and Masafumi Yohda. “The N-terminal region of RTP1S plays important roles in dimer formation and odorant receptor-trafficking.J Biol Chem 294, no. 40 (October 4, 2019): 14661–73. https://doi.org/10.1074/jbc.RA118.007110.
Fukutani Y, Tamaki R, Inoue R, Koshizawa T, Sakashita S, Ikegami K, et al. The N-terminal region of RTP1S plays important roles in dimer formation and odorant receptor-trafficking. J Biol Chem. 2019 Oct 4;294(40):14661–73.
Fukutani, Yosuke, et al. “The N-terminal region of RTP1S plays important roles in dimer formation and odorant receptor-trafficking.J Biol Chem, vol. 294, no. 40, Oct. 2019, pp. 14661–73. Pubmed, doi:10.1074/jbc.RA118.007110.
Fukutani Y, Tamaki R, Inoue R, Koshizawa T, Sakashita S, Ikegami K, Ohsawa I, Matsunami H, Yohda M. The N-terminal region of RTP1S plays important roles in dimer formation and odorant receptor-trafficking. J Biol Chem. 2019 Oct 4;294(40):14661–14673.

Published In

J Biol Chem

DOI

EISSN

1083-351X

Publication Date

October 4, 2019

Volume

294

Issue

40

Start / End Page

14661 / 14673

Location

United States

Related Subject Headings

  • Receptors, Odorant
  • Receptors, G-Protein-Coupled
  • Protein Transport
  • Odorants
  • Molecular Chaperones
  • Mice
  • Membrane Transport Proteins
  • Humans
  • HEK293 Cells
  • Flow Cytometry