protist, Monosiga brevicollis, has a tyrosine kinase signaling network more elaborate and diverse than found in any known metazoan

Tyrosine kinase signaling has long been considered a hallmark of intercellular communication, unique to multicellular animals. Our genomic analysis of the unicellular choanoflagellate Monosiga brevicollis discovers a remarkable count of 128 tyrosine kinases, 38 tyrosine phosphatases, and 123 phospho...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2008-07, Vol.105 (28), p.9674-9679
Main Authors: Manning, Gerard, Young, Susan L, Miller, W. Todd, Zhai, Yufeng
Format: Article
Language:English
Subjects:
Animal cells
Animals
Binding sites
Biological Sciences
Cells
Convergent evolution
Drosophila
Eukaryota - enzymology
Eukaryota - genetics
Evolution
Evolution, Molecular
Genome, Protozoan
Genomes
Genomics
Kinases
Metazoa
Monosiga brevicollis
Phosphatases
Phosphorylation
Phylogeny
Protein-Tyrosine Kinases - genetics
Proteins
Receptors
Signal Transduction
Signaling proteins
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Summary:Tyrosine kinase signaling has long been considered a hallmark of intercellular communication, unique to multicellular animals. Our genomic analysis of the unicellular choanoflagellate Monosiga brevicollis discovers a remarkable count of 128 tyrosine kinases, 38 tyrosine phosphatases, and 123 phosphotyrosine (pTyr)-binding SH2 proteins, all higher counts than seen in any metazoan. This elaborate signaling network shows little orthology to metazoan counterparts yet displays many innovations reminiscent of metazoans. These include extracellular domains structurally related to those of metazoan receptor kinases, alternative methods for membrane anchoring and phosphotyrosine interaction in cytoplasmic kinases, and domain combinations that link kinases to small GTPase signaling and transcription. These proteins also display a wealth of combinations of known signaling domains. This uniquely divergent and elaborate signaling network illuminates the early evolution of pTyr signaling, explores innovative ways to traverse the cellular signaling circuitry, and shows extensive convergent evolution, highlighting pervasive constraints on pTyr signaling.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0801314105