Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0019296
Title: Ptb domain-directed substrate targeting in a tyrosine kinase from the unicellular choanoflagellate monosiga brevicollis
Authors: Prieto-Echagüe V.
Chan P.M.
Craddock B.P.
Manser E. 
Miller W.T.
Keywords: HM motif containing tyrosine kinase 1
protein tyrosine kinase
unclassified drug
ligand
peptide
protein tyrosine kinase
animal cell
article
binding affinity
controlled study
enzyme activity
enzyme phosphorylation
enzyme purification
enzyme substrate
molecular recognition
Monosiga brevicollis
nonhuman
nucleotide sequence
protein binding
protein domain
protein expression
protein function
protein protein interaction
sequence analysis
amino acid sequence
chemistry
choanoflagellate
cytology
enzyme specificity
enzymology
metabolism
molecular genetics
phosphorylation
protein tertiary structure
Choanoflagellida
Mammalia
Metazoa
Monosiga
Monosiga brevicollis
Amino Acid Sequence
Choanoflagellata
Ligands
Molecular Sequence Data
Peptides
Phosphorylation
Protein Binding
Protein Structure, Tertiary
Protein-Tyrosine Kinases
Substrate Specificity
Issue Date: 2011
Citation: Prieto-Echagüe V., Chan P.M., Craddock B.P., Manser E., Miller W.T. (2011). Ptb domain-directed substrate targeting in a tyrosine kinase from the unicellular choanoflagellate monosiga brevicollis. PLoS ONE 6 (4) : e19296. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0019296
Rights: Attribution 4.0 International
Abstract: Choanoflagellates are considered to be the closest living unicellular relatives of metazoans. The genome of the choanoflagellate Monosiga brevicollis contains a surprisingly high number and diversity of tyrosine kinases, tyrosine phosphatases, and phosphotyrosine-binding domains. Many of the tyrosine kinases possess combinations of domains that have not been observed in any multicellular organism. The role of these protein interaction domains in M. brevicollis kinase signaling is not clear. Here, we have carried out a biochemical characterization of Monosiga HMTK1, a protein containing a putative PTB domain linked to a tyrosine kinase catalytic domain. We cloned, expressed, and purified HMTK1, and we demonstrated that it possesses tyrosine kinase activity. We used immobilized peptide arrays to define a preferred ligand for the third PTB domain of HMTK1. Peptide sequences containing this ligand sequence are phosphorylated efficiently by recombinant HMTK1, suggesting that the PTB domain of HMTK1 has a role in substrate recognition analogous to the SH2 and SH3 domains of mammalian Src family kinases. We suggest that the substrate recruitment function of the noncatalytic domains of tyrosine kinases arose before their roles in autoinhibition. © 2011 Prieto-Echagüe et al.
Source Title: PLoS ONE
URI: https://scholarbank.nus.edu.sg/handle/10635/162051
ISSN: 19326203
DOI: 10.1371/journal.pone.0019296
Rights: Attribution 4.0 International
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