ArticleScientific reports2016
Mechanism for insulin-like peptide 5 distinguishing the homologous relaxin family peptide receptor 3 and 4.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 23 citations in OpenAlex.
- Mechanism-guided identification of antidepressant G protein-coupled receptor drug targets.Cell · 2026Article
- Molecular mechanism underlying non-discriminatory recognition of relaxin-3 by RXFP3 and RXFP4.Communications biology · 2025Article
- Maternal Fed Zinc-Deficient Diet: Effects on Relaxin Family Peptides and Oxidant System in the Testis and Liver Tissue of Male Offspring.Biological trace element research · 2024Article
- Article
- Engineering of chimeric peptides as antagonists for the G protein-coupled receptor, RXFP4.Scientific reports · 2019Article
- Development of a selective agonist for relaxin family peptide receptor 3.Scientific reports · 2017Article
- Relaxin family peptides: structure-activity relationship studies.British journal of pharmacology · 2017Review
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The relaxin family peptides play a variety of biological functions by activating four G protein-coupled receptors, RXFP1-4. Among them, insulin-like peptide 5 (INSL5) and relaxin-3 share the highest sequence homology, but they have distinct receptor preference: INSL5 can activate RXFP4 only, while relaxin-3 can activate RXFP3, RXFP4, and RXFP1. Previous studies suggest that the A-chain is responsible for their different selectivity for RXFP1. However, the mechanism by which INSL5 distinguishes the homologous RXFP4 and RXFP3 remains unknown. In the present work, we chemically evolved INSL5 in vitro to a strong agonist of both RXFP4 and RXFP3 through replacement of its five B-chain residues with the corresponding residues of relaxin-3. We identified four determinants (B2Glu, B9Leu, B17Tyr, and a rigid B-chain C-terminus) on INSL5 that are responsible for its inactivity at RXFP3. In reverse experiments, we grafted these determinants onto a chimeric R3/I5 peptide, which contains the B-chain of relaxin-3 and the A-chain of INSL5, and retains full activation potency at RXFP3 and RXFP4. All resultant R3/I5 mutants retained high activation potency towards RXFP4, but most displayed significantly decreased or even abolished activation potency towards RXFP3, confirming the role of these four INSL5 determinants in distinguishing RXFP4 from RXFP3.
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