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    Distinct activation modes of the Relaxin Family Peptide Receptor 2 in response to insulin-like peptide 3 and relaxin

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    Author
    Bruell, S; Sethi, A; Smith, N; Scott, DJ; Hossain, MA; Wu, Q-P; Guo, Z-Y; Petrie, EJ; Gooley, PR; Bathgate, RAD
    Date
    2017-06-12
    Source Title
    Scientific Reports
    Publisher
    NATURE PUBLISHING GROUP
    University of Melbourne Author/s
    Sethi, Ashish; Scott, Daniel; Hossain, Mohammed; Petrie, Emma; Gooley, Paul; Bathgate, Ross; Bruell, Shoni
    Affiliation
    Florey Department of Neuroscience and Mental Health
    Biochemistry and Molecular Biology
    Medical Biology (W.E.H.I.)
    Metadata
    Show full item record
    Document Type
    Journal Article
    Citations
    Bruell, S., Sethi, A., Smith, N., Scott, D. J., Hossain, M. A., Wu, Q. -P., Guo, Z. -Y., Petrie, E. J., Gooley, P. R. & Bathgate, R. A. D. (2017). Distinct activation modes of the Relaxin Family Peptide Receptor 2 in response to insulin-like peptide 3 and relaxin. SCIENTIFIC REPORTS, 7 (1), https://doi.org/10.1038/s41598-017-03638-4.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/256199
    DOI
    10.1038/s41598-017-03638-4
    Abstract
    Relaxin family peptide receptor 2 (RXFP2) is a GPCR known for its role in reproductive function. It is structurally related to the human relaxin receptor RXFP1 and can be activated by human gene-2 (H2) relaxin as well as its cognate ligand insulin-like peptide 3 (INSL3). Both receptors possess an N-terminal low-density lipoprotein type a (LDLa) module that is necessary for activation and is joined to a leucine-rich repeat domain by a linker. This linker has been shown to be important for H2 relaxin binding and activation of RXFP1 and herein we investigate the role of the equivalent region of RXFP2. We demonstrate that the linker's highly-conserved N-terminal region is essential for activation of RXFP2 in response to both ligands. In contrast, the linker is necessary for H2 relaxin, but not INSL3, binding. Our results highlight the distinct mechanism by which INSL3 activates RXFP2 whereby ligand binding mediates reorientation of the LDLa module by the linker region to activate the RXFP2 transmembrane domains in conjunction with the INSL3 A-chain. In contrast, relaxin activation of RXFP2 involves a more RXFP1-like mechanism involving binding to the LDLa-linker, reorientation of the LDLa module and activation of the transmembrane domains by the LDLa alone.

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