ArticleThe Journal of biological chemistry2019
The N-terminal region of RTP1S plays important roles in dimer formation and odorant receptor-trafficking.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- Roles of sensory receptors in non-sensory organs: the kidney and beyond.Nature reviews. Nephrology · 2025Review
- Harnessing Odorant Receptor Activation to Suppress Real Malodor.International journal of molecular sciences · 2025Article
- Structural Rearrangement of the Olfactory Epithelium in Male Baikal Yellowfin Sculpins Across the Reproductive Period.Biology · 2025Article
- A Comparative Genomics Approach to Understanding the Evolution of Olfaction in Cetaceans.Journal of molecular evolution · 2024Article
- AAV-delivered muscone-induced transgene system for treating chronic diseases in mice via inhalation.Nature communications · 2024Article
- Antagonistic interactions between odorants alter human odor perception.Current biology : CB · 2023Article
- Identification and Characterization of Proteins That Are Involved in RTP1S-Dependent Transport of Olfactory Receptors.International journal of molecular sciences · 2023Article
- Interactions among key residues regulate mammalian odorant receptor trafficking.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Hot Spot Mutagenesis Improves the Functional Expression of Unique Mammalian Odorant Receptors.International journal of molecular sciences · 2021Article
- Structural instability and divergence from conserved residues underlie intracellular retention of mammalian odorant receptors.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Sensing Liver: Localization and Ligands for Hepatic Murine Olfactory and Taste Receptors.Frontiers in physiology · 2020Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
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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