Structural highlights
Function
Q24BV4_TETTS
Publication Abstract from PubMed
Acetylation of alpha-tubulin at the lysine 40 residue (alphaK40) by alphaTAT1/MEC-17 acetyltransferase modulates microtubule properties and occurs in most eukaryotic cells. Previous literatures suggest that acetylated microtubules are more stable and damage resistant. alphaK40 acetylation is the only known microtubule luminal post-translational modification site. The luminal location suggests that the modification tunes the lateral interaction of protofilaments inside the microtubule. In this study, we examined the effect of tubulin acetylation on the doublet microtubule (DMT) in the cilia of Tetrahymena thermophila using a combination of cryo-electron microscopy, molecular dynamics, and mass spectrometry. We found that alphaK40 acetylation exerts a small-scale effect on the DMT structure and stability by influencing the lateral rotational angle. In addition, comparative mass spectrometry revealed a link between alphaK40 acetylation and phosphorylation in cilia.
Effect of alpha-tubulin acetylation on the doublet microtubule structure.,Yang SK, Kubo S, Black CS, Peri K, Dai D, Legal T, Valente-Paterno M, Gaertig J, Bui KH Elife. 2024 Apr 10;12:RP92219. doi: 10.7554/eLife.92219. PMID:38598282[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yang SK, Kubo S, Black CS, Peri K, Dai D, Legal T, Valente-Paterno M, Gaertig J, Bui KH. Effect of α-tubulin acetylation on the doublet microtubule structure. Elife. 2024 Apr 10;12:RP92219. PMID:38598282 doi:10.7554/eLife.92219
