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Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl.
Ludwiginstitutet för Cancerforskning.
Ludwiginstitutet för Cancerforskning.
Ludwiginstitutet för Cancerforskning.
Ludwiginstitutet för Cancerforskning.
2003 (English)In: Biochem J, ISSN 0264-6021, Vol. 370, no Pt 1, 29-34 p.Article in journal (Refereed) Published
Abstract [en]

The mechanisms leading to the ubiquitination and degradation of the activated c-Abl kinase have not yet been identified. We found that the multi-adaptor protein ArgBP2 links c-Abl to the ubiquitin ligase Cbl. Phosphorylation of Cbl and ArgBP2 by c-Abl resulted in the stabilization of their interactions, thus facilitating Cbl-induced ubiquitination and subsequent degradation of c-Abl and ArgBP2.

Place, publisher, year, edition, pages
2003. Vol. 370, no Pt 1, 29-34 p.
Keyword [en]
Animals, CHO Cells, Cricetinae, Homeodomain Proteins/*metabolism, Humans, Hydrolysis, Oncogene Protein v-cbl, Phosphorylation, Protein Binding, Proto-Oncogene Proteins c-abl/*metabolism, Retroviridae Proteins; Oncogenic/*metabolism, Two-Hybrid System Techniques, Ubiquitin/*metabolism
Identifiers
URN: urn:nbn:se:uu:diva-10805PubMedID: 12475393OAI: oai:DiVA.org:uu-10805DiVA: diva2:38573
Available from: 2007-04-25 Created: 2007-04-25 Last updated: 2011-01-13

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