Cited by 221Receptor Mechanisms and SignalingFungal and yeast genetics researchGenomics and Phylogenetic Studies

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The Origin of GPCRs: Identification of Mammalian like Rhodopsin, Adhesion, Glutamate and Frizzled GPCRs in Fungi

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Krishnan, Arunkumar, Almén, Markus Sällman, Fredriksson, Robert, Schiöth, Helgi B.·2012·PLoS ONE

DOI 10.1371/journal.pone.0029817PMC PMC3251606

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Abstract

G protein-coupled receptors (GPCRs) in humans are classified into the five main families named Glutamate, Rhodopsin, Adhesion, Frizzled and Secretin according to the GRAFS classification. Previous results show that these mammalian GRAFS families are well represented in the Metazoan lineages, but they have not been shown to be present in Fungi. Here, we systematically mined 79 fungal genomes and provide the first evidence that four of the five main mammalian families of GPCRs, namely Rhodopsin, Adhesion, Glutamate and Frizzled, are present in Fungi and found 142 novel sequences between them. Significantly, we provide strong evidence that the Rhodopsin family emerged from the cAMP receptor family in an event close to the split of Opisthokonts and not in Placozoa, as earlier assumed. The Rhodopsin family then expanded greatly in Metazoans while the cAMP receptor family is found in 3 invertebrate species and lost in the vertebrates. We estimate that the Adhesion and Frizzled families evolved before the split of Unikonts from a common ancestor of all major eukaryotic lineages. Also, the study highlights that the fungal Adhesion receptors do not have N-terminal domains whereas the fungal Glutamate receptors have a broad repertoire of mammalian-like N-terminal domains. Further, mining of the close unicellular relatives of the Metazoan lineage, Salpingoeca rosetta and Capsaspora owczarzaki, obtained a rich group of both the Adhesion and Glutamate families, which in particular provided insight to the early emergence of the N-terminal domains of the Adhesion family. We identified 619 Fungi specific GPCRs across 79 genomes and revealed that Blastocladiomycota and Chytridiomycota phylum have Metazoan-like GPCRs rather than the GPCRs specific for Fungi. Overall, this study provides the first evidence of the presence of four of the five main GRAFS families in Fungi and clarifies the early evolutionary history of the GPCR superfamily.

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Li, W.-Z., & Godzik, A. (2006) · Bioinform. · doi:10.1093/bioinformatics/btl158 · Cited by 10,996
Profile hidden Markov models
Eddy, S. R. (1998) · Bioinformatics · doi:10.1093/bioinformatics/14.9.755 · Cited by 5,515
MAFFT version 5: improvement in accuracy of multiple sequence alignment
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Additional file 11 of Diversely evolved xibalbin variants from remipede venom inhibit potassium channels and activate PKA-II and Erk1/2 signaling
Pinheiro-Júnior, E. L., Alirahimi, E., Peigneur, S., Isensee, J., Schiffmann, S., Erkoc, P., Fürst, R., Vilcinskas, A., Sennoner, T., Koludarov, I., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26755336
Additional file 12 of Diversely evolved xibalbin variants from remipede venom inhibit potassium channels and activate PKA-II and Erk1/2 signaling
Pinheiro-Júnior, E. L., Alirahimi, E., Peigneur, S., Isensee, J., Schiffmann, S., Erkoc, P., Fürst, R., Vilcinskas, A., Sennoner, T., Koludarov, I., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26755339
Additional file 20 of Diversely evolved xibalbin variants from remipede venom inhibit potassium channels and activate PKA-II and Erk1/2 signaling
Pinheiro-Júnior, E. L., Alirahimi, E., Peigneur, S., Isensee, J., Schiffmann, S., Erkoc, P., Fürst, R., Vilcinskas, A., Sennoner, T., Koludarov, I., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26755363
Additional file 16 of Diversely evolved xibalbin variants from remipede venom inhibit potassium channels and activate PKA-II and Erk1/2 signaling
Pinheiro-Júnior, E. L., Alirahimi, E., Peigneur, S., Isensee, J., Schiffmann, S., Erkoc, P., Fürst, R., Vilcinskas, A., Sennoner, T., Koludarov, I., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26755351
Additional file 22 of Diversely evolved xibalbin variants from remipede venom inhibit potassium channels and activate PKA-II and Erk1/2 signaling
Pinheiro-Júnior, E. L., Alirahimi, E., Peigneur, S., Isensee, J., Schiffmann, S., Erkoc, P., Fürst, R., Vilcinskas, A., Sennoner, T., Koludarov, I., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26755369
Additional file 7 of Diversely evolved xibalbin variants from remipede venom inhibit potassium channels and activate PKA-II and Erk1/2 signaling
Pinheiro-Júnior, E. L., Alirahimi, E., Peigneur, S., Isensee, J., Schiffmann, S., Erkoc, P., Fürst, R., Vilcinskas, A., Sennoner, T., Koludarov, I., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26755324
Additional file 19 of Diversely evolved xibalbin variants from remipede venom inhibit potassium channels and activate PKA-II and Erk1/2 signaling
Pinheiro-Júnior, E. L., Alirahimi, E., Peigneur, S., Isensee, J., Schiffmann, S., Erkoc, P., Fürst, R., Vilcinskas, A., Sennoner, T., Koludarov, I., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26755360
Additional file 17 of Diversely evolved xibalbin variants from remipede venom inhibit potassium channels and activate PKA-II and Erk1/2 signaling
Pinheiro-Júnior, E. L., Alirahimi, E., Peigneur, S., Isensee, J., Schiffmann, S., Erkoc, P., Fürst, R., Vilcinskas, A., Sennoner, T., Koludarov, I., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26755354
Additional file 14 of Diversely evolved xibalbin variants from remipede venom inhibit potassium channels and activate PKA-II and Erk1/2 signaling
Pinheiro-Júnior, E. L., Alirahimi, E., Peigneur, S., Isensee, J., Schiffmann, S., Erkoc, P., Fürst, R., Vilcinskas, A., Sennoner, T., Koludarov, I., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26755345
Additional file 1 of Diversely evolved xibalbin variants from remipede venom inhibit potassium channels and activate PKA-II and Erk1/2 signaling
Pinheiro-Júnior, E. L., Alirahimi, E., Peigneur, S., Isensee, J., Schiffmann, S., Erkoc, P., Fürst, R., Vilcinskas, A., Sennoner, T., Koludarov, I., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26755303
Additional file 5 of Diversely evolved xibalbin variants from remipede venom inhibit potassium channels and activate PKA-II and Erk1/2 signaling
Pinheiro-Júnior, E. L., Alirahimi, E., Peigneur, S., Isensee, J., Schiffmann, S., Erkoc, P., Fürst, R., Vilcinskas, A., Sennoner, T., Koludarov, I., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26755318
Additional file 2 of Diversely evolved xibalbin variants from remipede venom inhibit potassium channels and activate PKA-II and Erk1/2 signaling
Pinheiro-Júnior, E. L., Alirahimi, E., Peigneur, S., Isensee, J., Schiffmann, S., Erkoc, P., Fürst, R., Vilcinskas, A., Sennoner, T., Koludarov, I., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26755306
Additional file 21 of Diversely evolved xibalbin variants from remipede venom inhibit potassium channels and activate PKA-II and Erk1/2 signaling
Pinheiro-Júnior, E. L., Alirahimi, E., Peigneur, S., Isensee, J., Schiffmann, S., Erkoc, P., Fürst, R., Vilcinskas, A., Sennoner, T., Koludarov, I., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26755366
Additional file 15 of Diversely evolved xibalbin variants from remipede venom inhibit potassium channels and activate PKA-II and Erk1/2 signaling
Pinheiro-Júnior, E. L., Alirahimi, E., Peigneur, S., Isensee, J., Schiffmann, S., Erkoc, P., Fürst, R., Vilcinskas, A., Sennoner, T., Koludarov, I., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26755348
Additional file 23 of Diversely evolved xibalbin variants from remipede venom inhibit potassium channels and activate PKA-II and Erk1/2 signaling
Pinheiro-Júnior, E. L., Alirahimi, E., Peigneur, S., Isensee, J., Schiffmann, S., Erkoc, P., Fürst, R., Vilcinskas, A., Sennoner, T., Koludarov, I., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26755372
Additional file 18 of Diversely evolved xibalbin variants from remipede venom inhibit potassium channels and activate PKA-II and Erk1/2 signaling
Pinheiro-Júnior, E. L., Alirahimi, E., Peigneur, S., Isensee, J., Schiffmann, S., Erkoc, P., Fürst, R., Vilcinskas, A., Sennoner, T., Koludarov, I., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26755357

Authors: Krishnan, A., Almén, M. S., Fredriksson, R., & Schiöth, H. B.
Affiliations: Uppsala University (SE)
Corresponding author: Schiöth, Helgi B.
ORCID: Krishnan, Arunkumar
Almén, Markus Sällman
Fredriksson, Robert
Venue: PLoS ONE
Publisher: Public Library of Science (PLoS)
Published: 2012-01-04
Volume: 7
Issue: 1
Pages: e29817
ISSN: 1932-6203 (ISSN-L)
DOI: 10.1371/journal.pone.0029817
PMC: PMC3251606
OpenAlex: W1983820999
Cited by: 204
References: 47
Citations by year: 2026: 6 · 2025: 11 · 2024: 16 · 2023: 11 · 2022: 11 · 2021: 7 · 2020: 16 · 2019: 14 · 2018: 8 · 2017: 14 · 2016: 23 · 2015: 20 · 2014: 18 · 2013: 18 · 2012: 10
FWCI: 8.48
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (unspecified)
Locations: PLoS ONE (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
Uppsala University Publications (Uppsala University) (submittedVersion, other-oa)
RePEc: Research Papers in Economics (submittedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Figshare (submittedVersion, cc-by)
Funders: Novo Nordisk
Vetenskapsrådet
Magnus Bergvalls Stiftelse
Uppsala Universitet
Novo Nordisk Fonden
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Phylogenetic Studies
Keywords: G protein-coupled receptors, GPCR evolution, rhodopsin family, cell adhesion receptors, glutamate receptors, Frizzled receptors, N-terminal domain, Salpingoeca rosetta, Capsaspora owczarzaki, Blastocladiomycota, Chytridiomycota, fungal genome
MeSH terms: Amino Acid Sequence, Animals, Cloning, Molecular, Fungi, Genes, Fungal, Humans, Mammals, Molecular Sequence Data, Phylogeny, Rhodopsin, Cell Adhesion Molecules, Genome, Fungal, Receptors, Glutamate, Evolution, Molecular, Receptors, G-Protein-Coupled, Frizzled Receptors

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The Origin of GPCRs: Identification of Mammalian like Rhodopsin, Adhesion, Glutamate and Frizzled GPCRs in Fungi

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