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PNAS 105 (28): 9674-9679

Copyright © 2008 by the National Academy of Sciences.

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

Gerard Manning*,{dagger}, Susan L. Young{ddagger}, W. Todd Miller§, and Yufeng Zhai*

*Razavi Newman Center for Bioinformatics, Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, CA 92037; {ddagger}Department of Molecular and Cell Biology and Center for Integrative Genomics, University of California, Berkeley, CA 94720; and §Department of Physiology and Biophysics, Stony Brook University, Stony Brook, NY 11794


Figure 1
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  		Fig. 1. Phylogenetic tree of Monosiga tyrosine kinases, based on alignment of kinase domains, pairwise similarity, and conservation of key residues. Second kinase domains are prefixed by b-. Specific branching patterns between most families are relatively poorly supported.

 

Figure 2
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  		Fig. 2. Domain architecture of representative tyrosine kinases. Predicted inactive kinase domains indicated by lightning bolt, fragments or partial matches to domains indicated by shortened icons. SigP: signal peptide; Myr, myristoylation site; other names from Pfam, SMART, or Table S1. For fuller tyrosine kinome, see Fig. S1 and http://kinase.com/kinbase.

 

Figure 3
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  		Fig. 3. Monosiga Src1 kinase efficiently phosphorylates two RM2 motifs in the cytoplasmic tail of RTKB2 (MbRTK1). The higher efficiency relative to a site on a Monosiga STAT homolog or a consensus c-Src substrate suggests that these are specific Src1 phosphorylation sites.

 

Figure 4
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  		Fig. 4. Domain organization of selected PTP, PTB and SH2 domain-containing proteins. For fuller details, see Fig. S2 and http://kinase.com/kinbase.

 

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