Reference : The Pbx Interaction Motif of Hoxa1 Is Essential for Its Oncogenic Activity
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
The Pbx Interaction Motif of Hoxa1 Is Essential for Its Oncogenic Activity
Delval, Stéphanie [ > > ]
Taminiau, Arnaud [ > > ]
Lamy, Juliette [ > > ]
Lallemand, Cécile [ > > ]
Gilles, Christine mailto [Université de Liège - ULiège > Département des sciences cliniques > Labo de biologie des tumeurs et du développement >]
Noël, Agnès mailto [Université de Liège - ULiège > Département des sciences biomédicales et précliniques > Biologie cellulaire et moléculaire appliquée à l'homme >]
Rezsohazy, René [ > > ]
Public Library of Science
Yes (verified by ORBi)
San Franscisco
[en] Hoxa1 belongs to the Hox family of homeodomain transcription factors involved in patterning embryonic territories and governing organogenetic processes. In addition to its developmental functions, Hoxa1 has been shown to be an oncogene and to be overexpressed in the mammary gland in response to a deregulation of the autocrine growth hormone. It has therefore been suggested that Hoxa1 plays a pivotal role in the process linking autocrine growth hormone misregulation and mammary carcinogenesis. Like most Hox proteins, Hoxa1 can interact with Pbx proteins. This interaction relies on a Hox hexapeptidic sequence centred on conserved Tryptophan and Methionine residues. To address the importance of the Hox-Pbx interaction for the oncogenic activity of Hoxa1, we characterized here the properties of a Hoxa1 variant with substituted residues in the hexapeptide and demonstrate that the Hoxa1 mutant lost its ability to stimulate cell proliferation, anchorage-independent cell growth, and loss of contact inhibition. Therefore, the hexapeptide motif of Hoxa1 is required to confer its oncogenic activity, supporting the view that this activity relies on the ability of Hoxa1 to interact with Pbx.

File(s) associated to this reference

Fulltext file(s):

Open access
Delval S Plos one 2011.pdfPublisher postprint439.49 kBView/Open

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.