The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.
Effects of α-tubulin acetylation on microtubule structure and stability
Open accessAbstract
Acetylation of K40 in α-tubulin is the sole posttranslational modification to mark the luminal surface of microtubules. It is still controversial whether its relationship with microtubule stabilization is correlative or causative. We have obtained high-resolution cryo-electron microscopy (cryo-EM) reconstructions of pure samples of αTAT1-acetylated and SIRT2-deacetylated microtubules to visualize the structural consequences of this modification and reveal its potential for influencing the larger assembly properties of microtubules. We modeled the conformational ensembles of the unmodified and acetylated states by using the experimental cryo-EM density as a structural restraint in molecular dynamics simulations. We found that acetylation alters the conformational landscape of the flexible loop that contains αK40. Modification of αK40 reduces the disorder of the loop and restricts the states that it samples. We propose that the change in conformational sampling that we describe, at a location very close to the lateral contacts site, is likely to affect microtubule stability and function.
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Cited by
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Modulation of cellular processes by histone and non-histone protein acetylation
Shvedunova, M., & Akhtar, A. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00441-y · Cited by 936
Structure of the Decorated Ciliary Doublet Microtubule
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Self-citationFerro, L. S., Fang, Q., Eshun-Wilson, L., Fernandes, J., Jack, A., Farrell, D. P., Golcuk, M., Huijben, T., Costa, K., Gur, M., et al. (2022) · Science · doi:10.1126/science.abf6154 · Cited by 112
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Metadata
- Authors
- Eshun-Wilson, L., Zhang, R., Portran, D., Nachury, M. V., Toso, D. B., Löhr, T., Vendruscolo, M., Bonomi, M., Fraser, J. S., & Nogales, E.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2019-05-09
- Volume
- 116
- Issue
- 21
- Pages
- 10366-10371
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2909456234
- Cited by
- 361
- References
- 62
- FWCI
- 18.84
- Type
- journal article
- Language
- en
- Open access
- hybrid
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