FPR3 Membrane Protein Introduction

Introduction of FPR3

FPR3, also referred to formyl peptide receptor 3, formyl peptide receptor-like 2 (FPRL2), FMLP-related receptor II (FMLP-R-II), FMLPY or FML2_HUMAN, is a 40 kDa receptor protein composed of 353 amino acids. In humans, this gene is encoded on the chromosome of 19q13.41. FPR3 is a low-affinity receptor for N-formyl-methionyl peptides which are believed to be powerful neutrophils chemotactic factors. It is a member of the formyl peptide receptor (FPR) family, involved in the antibacterial host defense and inflammatory reaction, which also comprises FPR1and FPR2. They are all Gi-protein-coupled receptors that are mainly expressed in phagocytic leukocytes of mammalian.

Function of FPR3 Membrane Protein

FPR3, together with other two homologs FPR1 and FPR2, constitutes the FPR family that is a group of seven transmembrane G protein-coupled receptors. FPR2 and FPR3 are two structural homologs of FMLP receptor because both of them do not recognize the ligand FMLP, they referred to orphan receptors. However, they two may function as chemotactic receptor roles. The FPR3 gene has 69% identity with FPRs and shares 83% identity with FPR2. FPR3 is a potential player in innate immune systems and presents with FPR2 as a FPR cluster during primate evolution. There are three different FPR described in humans, while at least eight FPR appear in mice (mFPR), designated FPR1 (FPR1), FPR-rs1 (FPR3 or LXA4 receptor), FPR-rs2 (FPR2), and FPR-rs3 to FPR-rs7. Among them, FPR-rs3 to FPR-rs7 show no counterparts in humans. Several associated pathways of FPR3 are peptide ligand-binding receptors and signaling by GPCR.

Application of FPR3 Membrane Protein in Literature

1. Chen Y. C., et al. Defective formyl peptide receptor 2/3 and annexin A1 expressions associated with M2a polarization of blood immune cells in patients with chronic obstructive pulmonary disease. J Transl Med. 2018, 16(1): 69. PubMed ID: 29544524
   
   

   Their findings provided some evidence for the defective FPR2/3 and annexin A1 expression, correlated with decreased M2a polarization, may be implicated in the development of cigarette smoking caused persistent airflow restrictions in chronic obstructive pulmonary disease (COPD).

2. Lee H. Y., et al. Intracellular formyl peptide receptor regulates naïve CD4 T cell migration. Biochem Biophys Res Commun. 2018, 497(1): 226-232. PubMed ID: 29427663
   
   

   This review found that formyl peptide receptor 1 and 3 (FPR1 and FPR3) are expressed intracellularly, as well as the nucleus of CD4 T cells. In conclusion, their data suggested that intracellular FPR in naïve CD4 T cells and surface FPRs in activated CD4 T cells possibly regulate immune responses depending on regulating the activity of CD4 T cells.

3. Stempel H., et al. Strain-specific loss of formyl peptide receptor 3 in the murine vomeronasal and immune systems. J Biol Chem. 2016, 291(18): 9762-9675. PubMed ID: 26957543
   
   

   Formyl peptide receptor 3 (Fpr3/Fpr-rs1) is a type of G protein-coupled receptor found in the subset of sensory neurons of mouse vomeronasal organs, and it is an olfactory substructure required for social recognition. All this information offers a foundation to further understand the function of Fpr3 in vivo.

4. Park S. K., et al. Nuclear FKBPs, Fpr3 and Fpr4 affect genome-wide genes transcription. Mol Genet Genomics. 2014, 289(2): 125-136. PubMed ID: 24297734
   
   

   The results in this report showed that both Fpr3 and Fpr4 proteins can modulate the expression of quantities of genes randomly distributed overall the genome. PPIase domain represses the transcriptional activity when tethered to the promoter of a reporter gene. The data further demonstrated evidence for the confused role of Fpr3 and Fpr4 in histone chaperones.

5. Ohkuni K., et al. Degradation of centromeric histone H3 variant Cse4 requires the Fpr3 peptidyl-prolyl Cis-Trans isomerase. Genetics. 2014, 196(4): 1041-1045. PubMed ID: 24514906
   
   

   The centromeric histone H3 variant Cse4 in Saccharomyces cerevisiae (S. cerevisiae) is polyubiquitylated and degraded by a proteasome-dependent way. This paper here reported that the proline isomerase Fpr3 can regulate Cse4 proteolysis. Structural change of Cse4 through Fpr3 may be essential for the interaction between the Cse4 and E3 ubiquitin ligase, Psh1.

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