Title :

Mapping of O-linked beta-N-acetylglucosamine modification sites in key contractile proteins of rat skeletal muscle.

Author(s) :

Hédou, Julie [Auteur]

Bastide, Bruno [Auteur]
Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369 - ULR 4488 [URePSSS]
Page, Adeline [Auteur]

Michalski, Jean-Claude [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Morelle, Willy [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]

Journal title :

Proteomics

Abbreviated title :

Proteomics

Volume number :

9

Pages :

2139-48

Publication date :

2009-04-01

ISSN :

1615-9861

English keyword(s) :

Acetylglucosamine
Actins
Animals
Glycosylation
Muscle Proteins
Muscle
Skeletal
Myosin Heavy Chains
Myosin Light Chains
Peptide Mapping
Protein Processing
Post-Translational
Rats
Serine
Tandem Mass Spectrometry

HAL domain(s) :

Sciences du Vivant [q-bio]

English abstract : [en]

O-linked beta-N-acetylglucosamine (O-GlcNAc) is a widespread modification of serine/threonine residues of nucleocytoplasmic proteins. Recently, several key contractile proteins in rat skeletal muscle (i.e., myosin heavy ...
Show more >O-linked beta-N-acetylglucosamine (O-GlcNAc) is a widespread modification of serine/threonine residues of nucleocytoplasmic proteins. Recently, several key contractile proteins in rat skeletal muscle (i.e., myosin heavy and light chains and actin) were identified as O-GlcNAc modified. Moreover, it was demonstrated that O-GlcNAc moieties involved in contractile protein interactions could modulate Ca(2+) activation parameters of contraction. In order to better understand how O-GlcNAc can modulate the contractile activity of muscle fibers, we decided to identify the sites of O-GlcNAc modification in purified contractile protein homogenates. Using an MS-based method that relies on mild beta-elimination followed by Michael addition of DTT (BEMAD), we determined the localization of one O-GlcNAc site in the subdomain four of actin and four O-GlcNAc sites in the light meromyosin region of myosin heavy chains (MHC). According to previous reports concerning the role of these regions, our data suggest that O-GlcNAc sites might modulate the actin-tropomyosin interaction, and be involved in MHC polymerization or interactions between MHC and other contractile proteins. Thus, the results suggest that this PTM might be involved in protein-protein interactions but could also modulate the contractile properties of skeletal muscle.Show less >

Language :

Anglais

Audience :

Non spécifiée

Administrative institution(s) :

Université de Lille
Univ. Artois
Univ. Littoral Côte d’Opale

Collections :

• Unité de Recherche Pluridisciplinaire Sport, Santé, Société (URePSSS) - ULR 7369

Research team(s) :

Activité Physique, Muscle, Santé (APMS)

Submission date :

2020-07-20T15:28:25Z
2020-08-18T12:02:44Z