Rethinking tubulin acetylation: From regulation to cellular adaptation

Abstract

Ever since its discovery, acetylation of α-tubulin on lysine 40 (K40) has been associated with the presence of long-lived, stable microtubules. Indeed, later studies revealed that acetylation protects microtubules from mechanical breakage, yet the functional consequences of this modification at the cellular level are only beginning to emerge. Here, we outline novel insights into the mechanisms controlling tubulin acetylation, and its impact on microtubule properties and cellular functions. Finally, we highlight recent advances suggesting that tubulin acetylation can also occur as a dynamic modification in response to a variety of cellular stresses. These observations shed new light on the cell biological functions of tubulin acetylation and give rise to the notion that this modification could be a universal mechanism that allows cells to adapt to changes in their environment or intracellular state.