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Molecular Biology and Evolution 18:312-321 (2001)
© 2001 Society for Molecular Biology and Evolution

ARTICLE

Coevolution of the Domains of Cytoplasmic Tyrosine Kinases

Martin Nars and Mauno Vihinen

*Department of Biochemistry and Food Chemistry, University of Turku, Turku, Finland;
{dagger}Institute of Medical Technology, University of Tampere, Tampere, Finland;
{ddagger}Tampere University Hospital, Tampere, Finland

Many signaling molecules are multidomain proteins that have other domains in addition to the catalytic kinase domain. Protein tyrosine kinases almost without exception contain Src homology 2 (SH2) and/or SH3 domains that can interact with other signaling proteins. Here, we studied evolution of the tyrosine kinases containing SH2 and/or SH3 and kinase domains. The three domains seem to have duplicated together, since the phylogenetic analysis using parsimony gave almost identical evolutionary trees for the separate domains and the multidomain complexes. The congruence analysis of the sequences for the separate domains also suggested that the domains have coevolved. There are several reasons for the domains to appear in a cluster. Kinases are regulated in many ways, and the presence of SH2 and SH3 domains at proper positions is crucial. Because all three domains can recognize different parts of ligands and substrates, their evolution has been interconnected. The reasons for the clustering and coevolution of the three domains in protein tyrosine kinases (PTKs) are discussed.


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