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dc.contributor.authorHime, Gary R.en_US
dc.contributor.authorDhungat, Mukunda Paien_US
dc.contributor.authorNG, ASHLEYen_US
dc.contributor.authorBowtell, David D. L.en_US
dc.date.accessioned2014-05-22T09:35:39Z
dc.date.available2014-05-22T09:35:39Z
dc.date.issued1997en_US
dc.date.submitted2008-05-27en_US
dc.identifier.citationHime, G. R., Dhungat, M. P., Ng, A., & Bowtell, D. D. L. (1997). D-Cbl, the Drosophila homologue of the c-Cbl proto-oncogene, interacts with the Drosophila EGF receptor in vivo, despite lacking C-terminal adaptor binding sites. Oncogene, 14, 2709-2719.en_US
dc.identifier.urihttp://hdl.handle.net/11343/33606
dc.description© 1997 Nature Publishing Group. Publisher's version is restricted access in accordance with the Nature Publishing Group policy.en_US
dc.description.abstractThe c-Cbl proto-oncogene encodes a multidomain phosphoprotein that has been demonstrated to interact with a wide range of signalling proteins. The biochemical function of c-Cbl in these complexes is, however, unclear. Recent studies with the C. elegans Cbl homologue, sli-1, have suggested that Cbl proteins may act as negative regulators of EGF receptor (EGFR) signalling. As the EGFR and other protein tyrosine kinase receptor signalling pathways are highly conserved between insects and vertebrates, we sought a Drosophila homologue of c- Cbl for a detailed genetic analysis. We report here that Drosophila melanogaster has a single gene, D-cbl, that is homologous to c-cbl. We find that D-cbl encodes a 52 kDa protein that has a high degree of similarity to c- Cbl and SLI-1 across novel phosphotyrosine-binding (PTB) and RING finger domains. Surprisingly, however, D-Cbl is C-terminally truncated relative to c-Cbl and SLI-1 and consequently is unable to bind SH3-domain containing adaptor proteins, including the Drosophila Grb2 homologue, Drk. Although the D-Cbl protein lacks Drk binding sites it can nevertheless associate with a tyrosine phosphorylated protein, or is itself tyrosine phosphorylated in an DER dependent manner and associates with activated Drosophila EGF receptors (DER) in vivo. Consistent with a role for D-Cbl in DER dependent patterning in the embryo and adult, D- Cbl is expressed at a high level in early embryos and throughout the imaginal discs in third instar larvae. This study forms the basis for future genetic analysis of D- Cbl, aimed at gaining insights into the role of Cbl proteins in signal transduction.en_US
dc.formatapplication/pdfen_US
dc.languageengen_US
dc.publisherNature Publishing Groupen_US
dc.relation.isversionofhttp://web.ebscohost.com.ezproxy.lib.unimelb.edu.au/ehost/detail?vid=1&hid=114&sid=72bbedce-c163-4b9a-98d6-a330452127db%40sessionmgr109en_US
dc.subjectcblen_US
dc.subjectEGF receptoren_US
dc.subjectDrosophilaen_US
dc.subjectsignal transductionen_US
dc.titleD-Cbl, the Drosophila homologue of the c-Cbl proto-oncogene, interacts with the Drosophila EGF receptor in vivo, despite lacking C-terminal adaptor binding sitesen_US
dc.typeJournal (Paginated)en_US
melbourne.peerreviewPeer Revieweden_US
melbourne.affiliationThe University of Melbourneen_US
melbourne.affiliation.departmentSchool of Medicineen_US
melbourne.publication.statusPublisheden_US
melbourne.source.titleOncogeneen_US
melbourne.source.volume14en_US
melbourne.source.pages2709-2719en_US
melbourne.elementsidNA
melbourne.contributor.authorHime, Gary
melbourne.contributor.authorNg, Ashley
melbourne.accessrightsThis item is currently not available from this repository


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