The venus kinase receptor (VKR) family: structure and evolution

Vanderstraete, Mathieu, Gouignard, Nadège, Ahier, Arnaud, Morel, Marion, Vicogne, Jérôme and Dissous, Colette (2013) The venus kinase receptor (VKR) family: structure and evolution. BMC Genomics, 14 1: 361.1-361.13. doi:10.1186/1471-2164-14-361

Author Vanderstraete, Mathieu
Gouignard, Nadège
Ahier, Arnaud
Morel, Marion
Vicogne, Jérôme
Dissous, Colette
Title The venus kinase receptor (VKR) family: structure and evolution
Journal name BMC Genomics   Check publisher's open access policy
ISSN 1471-2164
Publication date 2013-05-01
Sub-type Article (original research)
DOI 10.1186/1471-2164-14-361
Open Access Status DOI
Volume 14
Issue 1
Start page 361.1
End page 361.13
Total pages 13
Place of publication London, United Kingdom
Publisher BioMed Central
Formatted abstract
Background: Receptor tyrosine kinases (RTK) form a family of transmembrane proteins widely conserved in Metazoa, with key functions in cell-to-cell communication and control of multiple cellular processes. A new family of RTK named Venus Kinase Receptor (VKR) has been described in invertebrates. The VKR receptor possesses a Venus Fly Trap (VFT) extracellular module, a bilobate structure that binds small ligands to induce receptor kinase activity. VKR was shown to be highly expressed in the larval stages and gonads of several invertebrates, suggesting that it could have functions in development and/or reproduction.

Results: Analysis of recent genomic data has allowed us to extend the presence of VKR to five bilaterian phyla (Platyhelminthes, Arthropoda, Annelida, Mollusca, Echinodermata) as well as to the Cnidaria phylum. The presence of NveVKR in the early-branching metazoan Nematostella vectensis suggested that VKR arose before the bilaterian radiation. Phylogenetic and gene structure analyses showed that the 40 receptors identified in 36 animal species grouped monophyletically, and likely evolved from a common ancestor. Multiple alignments of tyrosine kinase (TK) and VFT domains indicated their important level of conservation in all VKRs identified up to date. We showed that VKRs had inducible activity upon binding of extracellular amino-acids and molecular modeling of the VFT domain confirmed the structure of the conserved amino-acid binding site.

Conclusions: This study highlights the presence of VKR in a large number of invertebrates, including primitive metazoans like cnidarians, but also its absence from nematodes and chordates. This little-known RTK family deserves to be further explored in order to determine its evolutionary origin, its possible interest for the emergence and specialization of Metazoa, and to understand its function in invertebrate development and/or reproductive biology.
Keyword Receptor tyrosine kinases (RTK)
Invertebrate development
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Queensland Brain Institute Publications
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Citation counts: TR Web of Science Citation Count  Cited 14 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 12 times in Scopus Article | Citations
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Created: Tue, 06 Jun 2017, 19:26:33 EST by Arnaud Ahier on behalf of Learning and Research Services (UQ Library)