Current trends in protein acetylation analysis.


Journal

Expert review of proteomics
ISSN: 1744-8387
Titre abrégé: Expert Rev Proteomics
Pays: England
ID NLM: 101223548

Informations de publication

Date de publication:
02 2019
Historique:
pubmed: 26 12 2018
medline: 14 8 2019
entrez: 25 12 2018
Statut: ppublish

Résumé

Acetylation is a widely occurring post-translational modification (PTM) of proteins that plays a crucial role in many cellular physiological and pathological processes. Over the last decade, acetylation analyses required the development of multiple methods to target individual acetylated proteins, as well as to cover a broader description of acetylated proteins that comprise the acetylome. Areas covered: This review discusses the different types of acetylation (N-ter/K-/O-acetylation) and then describes some major strategies that have been reported in the literature to detect, enrich, identify and quantify protein acetylation. The review highlights the advantages and limitations of these strategies, to guide researchers in designing their experimental investigations and analysis of protein acetylation. Finally, this review highlights the main applications of acetylomics (proteomics based on mass spectrometry) for understanding physiological and pathological conditions. Expert opinion: Recent advances in acetylomics have enhanced knowledge of the biological and pathological roles of protein acetylation and the acetylome. Besides, radiolabeling and western blotting remain also techniques-of-choice for targeted protein acetylation. Future challenges in acetylomics to analyze the N-ter and K-acetylome will most likely require enrichment/fractionation, MS instrumentation and bioinformatics. Challenges also remain to identify the potential biological roles of O-acetylation and cross-talk with other PTMs.

Identifiants

pubmed: 30580641
doi: 10.1080/14789450.2019.1559061
doi:

Substances chimiques

Proteome 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't Review

Langues

eng

Pagination

139-159

Auteurs

Issa Diallo (I)

a Universite Grenoble Alpes - LBFA and BEeSy, PROMETHEE, Proteomic Platform , Saint-Martin-d'Heres , France.
b Inserm, U1055, PROMETHEE Proteomic Platform , Saint-Martin-d'Heres , France.
c CHU de Grenoble, Institut de Biologie et de Pathologie, PROMETHEE Proteomic Platform , La Tronche , France.

Michel Seve (M)

a Universite Grenoble Alpes - LBFA and BEeSy, PROMETHEE, Proteomic Platform , Saint-Martin-d'Heres , France.
b Inserm, U1055, PROMETHEE Proteomic Platform , Saint-Martin-d'Heres , France.
c CHU de Grenoble, Institut de Biologie et de Pathologie, PROMETHEE Proteomic Platform , La Tronche , France.

Valérie Cunin (V)

a Universite Grenoble Alpes - LBFA and BEeSy, PROMETHEE, Proteomic Platform , Saint-Martin-d'Heres , France.
b Inserm, U1055, PROMETHEE Proteomic Platform , Saint-Martin-d'Heres , France.
c CHU de Grenoble, Institut de Biologie et de Pathologie, PROMETHEE Proteomic Platform , La Tronche , France.

Frédéric Minassian (F)

d Univ. Grenoble Alpes , CNRS, DCM , 38000 Grenoble , France.

Jean-François Poisson (JF)

d Univ. Grenoble Alpes , CNRS, DCM , 38000 Grenoble , France.

Sylvie Michelland (S)

a Universite Grenoble Alpes - LBFA and BEeSy, PROMETHEE, Proteomic Platform , Saint-Martin-d'Heres , France.
b Inserm, U1055, PROMETHEE Proteomic Platform , Saint-Martin-d'Heres , France.
c CHU de Grenoble, Institut de Biologie et de Pathologie, PROMETHEE Proteomic Platform , La Tronche , France.

Sandrine Bourgoin-Voillard (S)

a Universite Grenoble Alpes - LBFA and BEeSy, PROMETHEE, Proteomic Platform , Saint-Martin-d'Heres , France.
b Inserm, U1055, PROMETHEE Proteomic Platform , Saint-Martin-d'Heres , France.
c CHU de Grenoble, Institut de Biologie et de Pathologie, PROMETHEE Proteomic Platform , La Tronche , France.

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Classifications MeSH