A New Family of Receptor Tyrosine Kinases with a Venus Flytrap Binding Domain in Insects and Other Invertebrates Activated by Aminoacids

BACKGROUND: Tyrosine kinase receptors (RTKs) comprise a large family of membrane receptors that regulate various cellular processes in cell biology of diverse organisms. We previously described an atypical RTK in the platyhelminth parasite Schistosoma mansoni, composed of an extracellular Venus flyt...

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Autori principali: Ahier, Arnaud, Rondard, Philippe, Gouignard, Nadège, Khayath, Naji, Huang, Siluo, Trolet, Jacques, Donoghue, Daniel J., Gauthier, Monique, Pin, Jean-Philippe, Dissous, Colette
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Lingua:English
Pubblicazione: Public Library of Science 2009
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Research Article
Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC2680970/
https://ncbi.nlm.nih.gov/pubmed/19461966
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1371/journal.pone.0005651
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spelling pubmed-26809702009-05-21 A New Family of Receptor Tyrosine Kinases with a Venus Flytrap Binding Domain in Insects and Other Invertebrates Activated by Aminoacids Ahier, Arnaud Rondard, Philippe Gouignard, Nadège Khayath, Naji Huang, Siluo Trolet, Jacques Donoghue, Daniel J. Gauthier, Monique Pin, Jean-Philippe Dissous, Colette PLoS One Research Article BACKGROUND: Tyrosine kinase receptors (RTKs) comprise a large family of membrane receptors that regulate various cellular processes in cell biology of diverse organisms. We previously described an atypical RTK in the platyhelminth parasite Schistosoma mansoni, composed of an extracellular Venus flytrap module (VFT) linked through a single transmembrane domain to an intracellular tyrosine kinase domain similar to that of the insulin receptor. METHODS AND FINDINGS: Here we show that this receptor is a member of a new family of RTKs found in invertebrates, and particularly in insects. Sixteen new members of this family, named Venus Kinase Receptor (VKR), were identified in many insects. Structural and phylogenetic studies performed on VFT and TK domains showed that VKR sequences formed monophyletic groups, the VFT group being close to that of GABA(B) receptors and the TK one being close to that of insulin receptors. We show that a recombinant VKR is able to autophosphorylate on tyrosine residues, and report that it can be activated by L-arginine. This is in agreement with the high degree of conservation of the alpha amino acid binding residues found in many amino acid binding VFTs. The presence of high levels of vkr transcripts in larval forms and in female gonads indicates a putative function of VKR in reproduction and/or development. CONCLUSION: The identification of RTKs specific for parasites and insect vectors raises new perspectives for the control of human parasitic and infectious diseases. Public Library of Science 2009-05-21 /pmc/articles/PMC2680970/ /pubmed/19461966 http://dx.doi.org/10.1371/journal.pone.0005651 Text en Ahier et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
institution US National Library of Medicine
collection PubMed Central
language English
format Article
topic Research Article
spellingShingle Research Article
Ahier, Arnaud
Rondard, Philippe
Gouignard, Nadège
Khayath, Naji
Huang, Siluo
Trolet, Jacques
Donoghue, Daniel J.
Gauthier, Monique
Pin, Jean-Philippe
Dissous, Colette
A New Family of Receptor Tyrosine Kinases with a Venus Flytrap Binding Domain in Insects and Other Invertebrates Activated by Aminoacids
description BACKGROUND: Tyrosine kinase receptors (RTKs) comprise a large family of membrane receptors that regulate various cellular processes in cell biology of diverse organisms. We previously described an atypical RTK in the platyhelminth parasite Schistosoma mansoni, composed of an extracellular Venus flytrap module (VFT) linked through a single transmembrane domain to an intracellular tyrosine kinase domain similar to that of the insulin receptor. METHODS AND FINDINGS: Here we show that this receptor is a member of a new family of RTKs found in invertebrates, and particularly in insects. Sixteen new members of this family, named Venus Kinase Receptor (VKR), were identified in many insects. Structural and phylogenetic studies performed on VFT and TK domains showed that VKR sequences formed monophyletic groups, the VFT group being close to that of GABA(B) receptors and the TK one being close to that of insulin receptors. We show that a recombinant VKR is able to autophosphorylate on tyrosine residues, and report that it can be activated by L-arginine. This is in agreement with the high degree of conservation of the alpha amino acid binding residues found in many amino acid binding VFTs. The presence of high levels of vkr transcripts in larval forms and in female gonads indicates a putative function of VKR in reproduction and/or development. CONCLUSION: The identification of RTKs specific for parasites and insect vectors raises new perspectives for the control of human parasitic and infectious diseases.
author Ahier, Arnaud
Rondard, Philippe
Gouignard, Nadège
Khayath, Naji
Huang, Siluo
Trolet, Jacques
Donoghue, Daniel J.
Gauthier, Monique
Pin, Jean-Philippe
Dissous, Colette
author_facet Ahier, Arnaud
Rondard, Philippe
Gouignard, Nadège
Khayath, Naji
Huang, Siluo
Trolet, Jacques
Donoghue, Daniel J.
Gauthier, Monique
Pin, Jean-Philippe
Dissous, Colette
author_sort Ahier, Arnaud
title A New Family of Receptor Tyrosine Kinases with a Venus Flytrap Binding Domain in Insects and Other Invertebrates Activated by Aminoacids
title_short A New Family of Receptor Tyrosine Kinases with a Venus Flytrap Binding Domain in Insects and Other Invertebrates Activated by Aminoacids
title_full A New Family of Receptor Tyrosine Kinases with a Venus Flytrap Binding Domain in Insects and Other Invertebrates Activated by Aminoacids
title_fullStr A New Family of Receptor Tyrosine Kinases with a Venus Flytrap Binding Domain in Insects and Other Invertebrates Activated by Aminoacids
title_full_unstemmed A New Family of Receptor Tyrosine Kinases with a Venus Flytrap Binding Domain in Insects and Other Invertebrates Activated by Aminoacids
title_sort new family of receptor tyrosine kinases with a venus flytrap binding domain in insects and other invertebrates activated by aminoacids
publisher Public Library of Science
publisher_facet Public Library of Science
publishDate 2009
url https://ncbi.nlm.nih.gov/pmc/articles/PMC2680970/
https://ncbi.nlm.nih.gov/pubmed/19461966
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1371/journal.pone.0005651
_version_ 1760752152059314176

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