KPC2 relocalizes HOXA2 to the cytoplasm and decreases its transcriptional activity.

Animals; Cytoplasm/metabolism; Embryonic Development/genetics; Gene Expression Regulation, Developmental; Homeodomain Proteins/biosynthesis/genetics/metabolism; Intracellular Signaling Peptides and Proteins/genetics; Mice; Protein Binding; Transcriptional Activation/genetics; HOX; HOXA2; Interaction; KPC2; Mouse development

Abstract :

[en] Regulation of transcription factor activity relies on molecular interactions or enzymatic modifications which influence their interaction with DNA cis-regulatory sequences, their transcriptional activation or repression, and stability or intracellular distribution of these proteins. Regarding the well-conserved Hox protein family, a restricted number of activity regulators have been highlighted thus far. In the framework of a proteome-wide screening aiming at identifying proteins interacting with Hoxa2, KPC2, an adapter protein constitutive of the KPC ubiquitin-ligase complex, was identified. In this work, KPC2 was confirmed as being a genuine interactor of Hoxa2 by co-precipitation and bimolecular fluorescence complementation assays. At functional level, KPC2 diminishes the transcriptional activity and induces the nuclear exit of Hoxa2. Gene expression analyses revealed that Kpc2 is active in restricted areas of the developing mouse embryo which overlap with the Hoxa2 expression domain. Together, our data support that KPC2 regulates Hoxa2 by promoting its relocation to the cytoplasm.

Disciplines :

Biochemistry, biophysics & molecular biology

Author, co-author :

Bridoux, Laure

Bergiers, Isabelle

Draime, Amandine

Halbout, Mathias

Deneyer, Noemie

Twizere, Jean-Claude ; Université de Liège > Agronomie, Bio-ingénierie et Chimie (AgroBioChem) > Biologie cell. et moléc.

Rezsohazy, Rene

Language :

English

Title :

KPC2 relocalizes HOXA2 to the cytoplasm and decreases its transcriptional activity.

Publication date :

2015

Journal title :

Biochimica et Biophysica Acta

ISSN :

0006-3002

eISSN :

1878-2434

Publisher :

Elsevier, Amsterdam, Netherlands

Volume :

1849

Issue :

Pages :

1298-311

Peer reviewed :

Peer Reviewed verified by ORBi

Commentary :

Available on ORBi :

since 06 January 2016

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