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Protein interactions of the transcription factor Hoxa1

BACKGROUND: Hox proteins are transcription factors involved in crucial processes during animal development. Their mode of action remains scantily documented. While other families of transcription factors, like Smad or Stat, are known cell signaling transducers, such a function has never been squarel...

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Autores principales: Lambert, Barbara, Vandeputte, Julie, Remacle, Sophie, Bergiers, Isabelle, Simonis, Nicolas, Twizere, Jean-Claude, Vidal, Marc, Rezsohazy, René
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3514159/
https://www.ncbi.nlm.nih.gov/pubmed/23088713
http://dx.doi.org/10.1186/1471-213X-12-29
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author Lambert, Barbara
Vandeputte, Julie
Remacle, Sophie
Bergiers, Isabelle
Simonis, Nicolas
Twizere, Jean-Claude
Vidal, Marc
Rezsohazy, René
author_facet Lambert, Barbara
Vandeputte, Julie
Remacle, Sophie
Bergiers, Isabelle
Simonis, Nicolas
Twizere, Jean-Claude
Vidal, Marc
Rezsohazy, René
author_sort Lambert, Barbara
collection PubMed
description BACKGROUND: Hox proteins are transcription factors involved in crucial processes during animal development. Their mode of action remains scantily documented. While other families of transcription factors, like Smad or Stat, are known cell signaling transducers, such a function has never been squarely addressed for Hox proteins. RESULTS: To investigate the mode of action of mammalian Hoxa1, we characterized its interactome by a systematic yeast two-hybrid screening against ~12,200 ORF-derived polypeptides. Fifty nine interactors were identified of which 45 could be confirmed by affinity co-purification in animal cell lines. Many Hoxa1 interactors are proteins involved in cell-signaling transduction, cell adhesion and vesicular trafficking. Forty-one interactions were detectable in live cells by Bimolecular Fluorescence Complementation which revealed distinctive intracellular patterns for these interactions consistent with the selective recruitment of Hoxa1 by subgroups of partner proteins at vesicular, cytoplasmic or nuclear compartments. CONCLUSIONS: The characterization of the Hoxa1 interactome presented here suggests unexplored roles for Hox proteins in cell-to-cell communication and cell physiology.
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spelling pubmed-35141592012-12-05 Protein interactions of the transcription factor Hoxa1 Lambert, Barbara Vandeputte, Julie Remacle, Sophie Bergiers, Isabelle Simonis, Nicolas Twizere, Jean-Claude Vidal, Marc Rezsohazy, René BMC Dev Biol Research Article BACKGROUND: Hox proteins are transcription factors involved in crucial processes during animal development. Their mode of action remains scantily documented. While other families of transcription factors, like Smad or Stat, are known cell signaling transducers, such a function has never been squarely addressed for Hox proteins. RESULTS: To investigate the mode of action of mammalian Hoxa1, we characterized its interactome by a systematic yeast two-hybrid screening against ~12,200 ORF-derived polypeptides. Fifty nine interactors were identified of which 45 could be confirmed by affinity co-purification in animal cell lines. Many Hoxa1 interactors are proteins involved in cell-signaling transduction, cell adhesion and vesicular trafficking. Forty-one interactions were detectable in live cells by Bimolecular Fluorescence Complementation which revealed distinctive intracellular patterns for these interactions consistent with the selective recruitment of Hoxa1 by subgroups of partner proteins at vesicular, cytoplasmic or nuclear compartments. CONCLUSIONS: The characterization of the Hoxa1 interactome presented here suggests unexplored roles for Hox proteins in cell-to-cell communication and cell physiology. BioMed Central 2012-10-22 /pmc/articles/PMC3514159/ /pubmed/23088713 http://dx.doi.org/10.1186/1471-213X-12-29 Text en Copyright ©2012 Lambert et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Lambert, Barbara
Vandeputte, Julie
Remacle, Sophie
Bergiers, Isabelle
Simonis, Nicolas
Twizere, Jean-Claude
Vidal, Marc
Rezsohazy, René
Protein interactions of the transcription factor Hoxa1
title Protein interactions of the transcription factor Hoxa1
title_full Protein interactions of the transcription factor Hoxa1
title_fullStr Protein interactions of the transcription factor Hoxa1
title_full_unstemmed Protein interactions of the transcription factor Hoxa1
title_short Protein interactions of the transcription factor Hoxa1
title_sort protein interactions of the transcription factor hoxa1
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3514159/
https://www.ncbi.nlm.nih.gov/pubmed/23088713
http://dx.doi.org/10.1186/1471-213X-12-29
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