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Coevolution of the domains of cytoplasmic tyrosine kinases

Nars, M and Vihinen, Mauno LU (2001) In Molecular Biology and Evolution 18(3). p.312-321
Abstract
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... (More)
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. (Less)
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author
publishing date
type
Contribution to journal
publication status
published
subject
keywords
evolution, phylogenetics, SH2, SH3, protein kinase, tyrosine kinase, structural conservation
in
Molecular Biology and Evolution
volume
18
issue
3
pages
312 - 321
publisher
Oxford University Press
external identifiers
  • wos:000167286300004
  • scopus:0035107021
ISSN
0737-4038
language
English
LU publication?
no
id
63cc2b5f-a6ef-4d9f-83b8-18ac2586b4bb (old id 3851680)
date added to LUP
2013-06-28 15:25:28
date last changed
2018-05-29 12:23:10
@article{63cc2b5f-a6ef-4d9f-83b8-18ac2586b4bb,
  abstract     = {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.},
  author       = {Nars, M and Vihinen, Mauno},
  issn         = {0737-4038},
  keyword      = {evolution,phylogenetics,SH2,SH3,protein kinase,tyrosine kinase,structural conservation},
  language     = {eng},
  number       = {3},
  pages        = {312--321},
  publisher    = {Oxford University Press},
  series       = {Molecular Biology and Evolution},
  title        = {Coevolution of the domains of cytoplasmic tyrosine kinases},
  volume       = {18},
  year         = {2001},
}