Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/11990
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dc.contributor.authorBaldwin, Graham Sen
dc.contributor.authorLio, Daisy Sio-Sengen
dc.contributor.authorFerrand, Audreyen
dc.contributor.authorCatimel, Brunoen
dc.contributor.authorShehan, B Philipen
dc.contributor.authorNorton, Raymond Sen
dc.contributor.authorCheng, Heung-Chinen
dc.date.accessioned2015-05-16T01:37:32Z
dc.date.available2015-05-16T01:37:32Z
dc.date.issued2013-12-12en
dc.identifier.citationBiochimica Et Biophysica Acta 2013; 1844(3): 487-96en
dc.identifier.govdoc24334106en
dc.identifier.otherPUBMEDen
dc.identifier.urihttps://ahro.austin.org.au/austinjspui/handle/1/11990en
dc.description.abstractThe Src-family tyrosine kinases (SFKs) are oncogenic enzymes that contribute to the initiation and progression of many types of cancer. In normal cells, SFKs are kept in an inactive state mainly by phosphorylation of a consensus regulatory tyrosine near the C-terminus (Tyr(530) in the SFK c-Src). As recent data indicate that tyrosine modification enhances binding of metal ions, the hypothesis that SFKs might be regulated by metal ions was investigated. The c-Src C-terminal peptide bound two Fe(3+) ions with affinities at pH4.0 of 33 and 252μM, and phosphorylation increased the affinities at least 10-fold to 1.4 and 23μM, as measured by absorbance spectroscopy. The corresponding phosphorylated peptide from the SFK Lyn bound two Fe(3+) ions with much higher affinities (1.2pM and 160nM) than the Src C-terminal peptide. Furthermore, when Lyn or Hck kinases, which had been stabilised in the inactive state by phosphorylation of the C-terminal regulatory tyrosine, were incubated with Fe(3+) ions, a significant enhancement of kinase activity was observed. In contrast Lyn or Hck kinases in the unphosphorylated active state were significantly inhibited by Fe(3+) ions. These results suggest that Fe(3+) ions can regulate SFK activity by binding to the phosphorylated C-terminal regulatory tyrosine.en
dc.language.isoenen
dc.subject.otherCalciumen
dc.subject.otherFerricen
dc.subject.otherIronen
dc.subject.otherKinaseen
dc.subject.otherPhosphotyrosineen
dc.subject.otherAmino Acid Sequenceen
dc.subject.otherCationsen
dc.subject.otherEnzyme Activationen
dc.subject.otherFerric Compounds.metabolismen
dc.subject.otherMolecular Sequence Dataen
dc.subject.otherPhosphorylationen
dc.subject.otherProtein Bindingen
dc.subject.otherSurface Plasmon Resonanceen
dc.subject.othersrc-Family Kinases.chemistry.metabolismen
dc.titleActivation of Src family tyrosine kinases by ferric ions.en
dc.typeJournal Articleen
dc.identifier.journaltitleBiochimica et biophysica actaen
dc.identifier.affiliationThe Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australiaen
dc.identifier.affiliationThe University of Melbourne Department of Surgery, Austin Health, Heidelberg, Victoria, Australiaen
dc.identifier.affiliationDepartment of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria, Australiaen
dc.identifier.affiliationLudwig Institute for Cancer Research, Melbourne Branch, Austin Hospital, Heidelberg, Victoria, Australiaen
dc.identifier.doi10.1016/j.bbapap.2013.12.004en
dc.description.pages487-96en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/24334106en
dc.type.austinJournal Articleen
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.fulltextNo Fulltext-
item.grantfulltextnone-
item.languageiso639-1en-
item.openairetypeJournal Article-
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