scholarly journals The Annexin I Sequence Gln9-Ala10-Trp11-Phe12Is a Core Structure for Interaction with the Formyl Peptide Receptor 1

2010 ◽  
Vol 285 (19) ◽  
pp. 14338-14345 ◽  
Author(s):  
Charlotta Movitz ◽  
Lars Brive ◽  
Kristoffer Hellstrand ◽  
Marie-Josèphe Rabiet ◽  
Claes Dahlgren
Keyword(s):  
Core Structure ◽  
Formyl Peptide Receptor ◽  
Peptide Receptor ◽  
Annexin I ◽  
Formyl Peptide

scholarly journals From immune to olfactory expression: neofunctionalization of formyl peptide receptors

2021 ◽  
Vol 383 (1) ◽  
pp. 387-393
Author(s):  
Madlaina Boillat ◽  
Alan Carleton ◽  
Ivan Rodriguez
Keyword(s):  
Expression Patterns ◽  
Vomeronasal Organ ◽  
Formyl Peptide Receptor ◽  
Regulatory Sequence ◽  
Powerful Source ◽  
Peptide Receptor ◽  
Gene Shuffling ◽  
Evolutionary Innovation ◽  
Vomeronasal Receptor ◽  
Formyl Peptide

Abstract Variations in gene expression patterns represent a powerful source of evolutionary innovation. In a rodent living about 70 million years ago, a genomic accident led an immune formyl peptide receptor (FPR) gene to hijack a vomeronasal receptor regulatory sequence. This gene shuffling event forced an immune pathogen sensor to transition into an olfactory chemoreceptor, which thus moved from sensing the internal world to probing the outside world. We here discuss the evolution of the FPR gene family, the events that led to their neofunctionalization in the vomeronasal organ and the functions of immune and vomeronasal FPRs.

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