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α-Tubulin acetylation on lysine 40 controls cardiac glucose uptake

Edith Renguet, Marine De Loof, Natacha Fourny, Audrey Ginion, Caroline Bouzin, Christian Poüs, Sandrine Horman, Christophe Beauloye, Laurent Bultot, Luc Bertrand

2022American Journal of Physiology-Heart and Circulatory Physiology12 citationsDOIOpen Access PDF

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.

Topics & Concepts

AcetylationGLUT4Glucose transporterTubulinBiologyGlucose uptakeInsulinBiochemistryMicrotubuleCell biologyEndocrinologyGeneMetabolism, Diabetes, and CancerProtein Tyrosine PhosphatasesAutophagy in Disease and Therapy
α-Tubulin acetylation on lysine 40 controls cardiac glucose uptake | Litcius