α-Tubulin acetylation on lysine 40 controls cardiac glucose uptake

Author:

Renguet Edith1,De Loof Marine1,Fourny Natacha1,Ginion Audrey1,Bouzin Caroline2ORCID,Poüs Christian34,Horman Sandrine1,Beauloye Christophe15,Bultot Laurent1ORCID,Bertrand Luc1ORCID

Affiliation:

1. Institut de Recherche Expérimentale et Clinique, Pole of Cardiovascular Research, Université catholique de Louvain, Brussels, Belgium

2. Institut de Recherche Expérimentale et Clinique, IREC Imaging Platform (2IP), Université catholique de Louvain, Brussels, Belgium

3. INSERM UMR-S-1193, Université Paris-Saclay, Châtenay-Malabry, France

4. AP-HP, Biochimie-Hormonologie, Hôpital Antoine Béclère, Clamart, France

5. Division of Cardiology, Cliniques Universitaires Saint-Luc, Brussels, Belgium

Abstract

Acetylation level of α-tubulin on K40 is increased in the heart of a diet-induced mouse model of type 2 diabetes. Pharmacological stimulation of α-tubulin K40 acetylation lowers insulin-mediated GLUT4 vesicles translocation to the plasma membrane, reducing glucose transport. Expressing a nonacetylable dominant form of α-tubulin boosts glucose uptake in both insulin-sensitive and insulin-resistant cardiomyocytes.

Funder

Wallonia-Brussels Federation, French Community of Belgium

Astrazeneca Belgium

Fonds De La Recherche Scientifique - FNRS

Publisher

American Physiological Society

Subject

Physiology (medical),Cardiology and Cardiovascular Medicine,Physiology

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