{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Suga H"],"funding":["NCI NIH HHS"],"pagination":["5362"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5876402"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8(1)"],"pubmed_abstract":["Creolimax fragrantissima is a member of the ichthyosporean clade, the earliest branching holozoan lineage. The kinome of Creolimax is markedly reduced as compared to those of metazoans. In particular, Creolimax possesses a single non-receptor tyrosine kinase: CfrSrc, the homolog of c-Src kinase. CfrSrc is an active tyrosine kinase, and it is expressed throughout the lifecycle of Creolimax. In animal cells, the regulatory mechanism for Src involves tyrosine phosphorylation at a C-terminal site by Csk kinase. The lack of Csk in Creolimax suggests that a different mode of negative regulation must exist for CfrSrc. We demonstrate that CfrPTP-3, one of the 7 tyrosine-specific phosphatases (PTPs) in Creolimax, suppresses CfrSrc activity in vitro and in vivo. Transcript levels of CfrPTP-3 and two"],"journal":["Scientific reports"],"pubmed_title":["Src signaling in a low-complexity unicellular kinome."],"pmcid":["PMC5876402"],"funding_grant_id":["R01 CA058530"],"pubmed_authors":["Miller WT","Suga H"],"additional_accession":[]},"is_claimable":false,"name":"Src signaling in a low-complexity unicellular kinome.","description":"Creolimax fragrantissima is a member of the ichthyosporean clade, the earliest branching holozoan lineage. The kinome of Creolimax is markedly reduced as compared to those of metazoans. In particular, Creolimax possesses a single non-receptor tyrosine kinase: CfrSrc, the homolog of c-Src kinase. CfrSrc is an active tyrosine kinase, and it is expressed throughout the lifecycle of Creolimax. In animal cells, the regulatory mechanism for Src involves tyrosine phosphorylation at a C-terminal site by Csk kinase. The lack of Csk in Creolimax suggests that a different mode of negative regulation must exist for CfrSrc. We demonstrate that CfrPTP-3, one of the 7 tyrosine-specific phosphatases (PTPs) in Creolimax, suppresses CfrSrc activity in vitro and in vivo. Transcript levels of CfrPTP-3 and two","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Mar","modification":"2025-04-04T09:05:38.559Z","creation":"2019-03-26T23:23:25Z"},"accession":"S-EPMC5876402","cross_references":{"pubmed":["29599515"],"doi":["10.1038/s41598-018-23721-8"]}}