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-Structure paper
Title | Effect of α-tubulin acetylation on the doublet microtubule structure. |
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Journal, issue, pages | Elife, Vol. 12, Year 2024 |
Publish date | Apr 10, 2024 |
Authors | Shun Kai Yang / Shintaroh Kubo / Corbin Steven Black / Katya Peri / Daniel Dai / Thibault Legal / Melissa Valente-Paterno / Jacek Gaertig / Khanh Huy Bui / |
PubMed Abstract | Acetylation of α-tubulin at the lysine 40 residue (αK40) by αTAT1/MEC-17 acetyltransferase modulates microtubule properties and occurs in most eukaryotic cells. Previous literatures suggest that ...Acetylation of α-tubulin at the lysine 40 residue (αK40) by αTAT1/MEC-17 acetyltransferase modulates microtubule properties and occurs in most eukaryotic cells. Previous literatures suggest that acetylated microtubules are more stable and damage resistant. αK40 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 using a combination of cryo-electron microscopy, molecular dynamics, and mass spectrometry. We found that αK40 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 αK40 acetylation and phosphorylation in cilia. |
External links | Elife / PubMed:38598282 / PubMed Central |
Methods | EM (single particle) |
Resolution | 4.1 Å |
Structure data | EMDB-40436, PDB-8sf7: |
Chemicals | ChemComp-GTP: ChemComp-MG: ChemComp-GDP: |
Source |
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Keywords | STRUCTURAL PROTEIN / Cilia / Axoneme / Doublet Microtubule / Microtubule Inner Protein |