Coevolution of the domains of cytoplasmic tyrosine kinases
Author
Summary, in English
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.
Publishing year
2001
Language
English
Pages
312-321
Publication/Series
Molecular biology and evolution
Volume
18
Issue
3
Document type
Journal article
Publisher
Oxford University Press
Topic
- Medical Genetics
Keywords
- evolution
- phylogenetics
- SH2
- SH3
- protein kinase
- tyrosine kinase
- structural conservation
Status
Published
ISBN/ISSN/Other
- ISSN: 0737-4038