Alternative proteins are functional regulators in cell reprogramming by pka activation

Cardon, Tristan; Franck, Julien; Coyaud, Etienne-Marie; Laurent, Estelle; Damato, Marina; Maffia, Michele; Vergara, Daniele; FOURNIER, Isabelle; Salzet, Michel

Type de document :

Article dans une revue scientifique: Article original

DOI :

10.1093/nar/gkaa277

PMID :

32324228

URL permanente :

http://hdl.handle.net/20.500.12210/75007

Titre :

Alternative proteins are functional regulators in cell reprogramming by pka activation

Auteur(s) :

Cardon, Tristan [Auteur]

Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192
Franck, Julien [Auteur]

Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192
Coyaud, Etienne-Marie [Auteur]
Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192
Laurent, Estelle [Auteur]
Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192
Damato, Marina [Auteur]
Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U 1192 [PRISM]
Maffia, Michele [Auteur]
Università del Salento = University of Salento [Lecce]
Vergara, Daniele [Auteur]
Università del Salento = University of Salento [Lecce]
FOURNIER, Isabelle [Auteur]

Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192
Salzet, Michel [Auteur]

Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192

Titre de la revue :

Nucleic acids research

Nom court de la revue :

Nucleic Acids Res.

Numéro :

Pagination :

7864–7882

Éditeur :

Oxford Academic

Date de publication :

2020-04-23

ISSN :

1362-4962

Discipline(s) HAL :

Sciences du Vivant [q-bio]

Résumé en anglais : [en]

It has been recently shown that many proteins are lacking from reference databases used in mass spectrometry analysis, due to their translation templated on alternative open reading frames. This questions our current ...
Lire la suite >It has been recently shown that many proteins are lacking from reference databases used in mass spectrometry analysis, due to their translation templated on alternative open reading frames. This questions our current understanding of gene annotation and drastically expands the theoretical proteome complexity. The functions of these alternative proteins (AltProts) still remain largely unknown. We have developed a large-scale and unsupervised approach based on cross-linking mass spectrometry (XL-MS) followed by shotgun proteomics to gather information on the functional role of AltProts by mapping them back into known signalling pathways through the identification of their reference protein (RefProt) interactors. We have identified and profiled AltProts in a cancer cell reprogramming system: NCH82 human glioma cells after 0, 16, 24 and 48 h Forskolin stimulation. Forskolin is a protein kinase A activator inducing cell differentiation and epithelial-mesenchymal transition. Our data show that AltMAP2, AltTRNAU1AP and AltEPHA5 interactions with tropomyosin 4 are downregulated under Forskolin treatment. In a wider perspective, Gene Ontology and pathway enrichment analysis (STRING) revealed that RefProts associated with AltProts are enriched in cellular mobility and transfer RNA regulation. This study strongly suggests novel roles of AltProts in multiple essential cellular functions and supports the importance of considering them in future biological studies.Lire moins >

Langue :

Anglais

Audience :

Internationale

Vulgarisation :

Non

Établissement(s) :

INSERM
Université de Lille

Collections :

Protéomique, Réponse Inflammatoire, Spectrométrie de Masse (PRISM) - U1192

Date de dépôt :

2022-06-15T13:57:52Z
2023-03-08T10:37:22Z
2023-03-08T10:40:37Z

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2020-04-23-gkaa277.pdf
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Ce document est diffusé sous licence Attribution-NonCommercial 3.0 United States

Historique des modifications

Numéro de version	Lien	Date de modification
5	20.500.12210/75007	2023-03-08T10:44:16Z
4	20.500.12210/75007.4*	2023-03-08T10:40:02Z
3	20.500.12210/75007.3	2023-03-08T10:31:04Z
1	20.500.12210/75007.1	2022-06-15T13:57:52Z

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Alternative proteins are functional ...

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