Effects of α-tubulin acetylation on microtubule structure and stability

Eshun-Wilson, Lisa; Zhang, Rui; Portran, Didier; Nachury, Maxence V.; Toso, Daniel B.; Löhr, Thomas; Vendruscolo, Michele; Bonomi, Massimiliano; Fraser, James S.; Nogales, Eva

doi:10.1073/pnas.1900441116

Effects of α-tubulin acetylation on microtubule structure and stability

Journal Article · Thu May 09 00:00:00 EDT 2019 · Proceedings of the National Academy of Sciences of the United States of America

DOI:https://doi.org/10.1073/pnas.1900441116· OSTI ID:1559217

Eshun-Wilson, Lisa ^[1]; Zhang, Rui ^[2]; Portran, Didier ^[3]; ^[4]; Toso, Daniel B. ^[1]; Löhr, Thomas ^[5]; Vendruscolo, Michele ^[5]; Bonomi, Massimiliano ^[6]; Fraser, James S. ^[7]; ^[8]

Univ. of California, Berkeley, CA (United States)
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States); Washington Univ., St. Louis, MO (United States)
Univ. of California, San Francisco, CA (United States); Univ. Montpellier, Montpellier (France)
Univ. of California, San Francisco, CA (United States)
Univ. of Cambridge, Cambridge (United Kingdom)
Univ. of Cambridge, Cambridge (United Kingdom); Inst. Pasteur, Paris (France)
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States); Univ. of California, San Francisco, CA (United States)
Univ. of California, Berkeley, CA (United States); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)

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.

View Accepted Manuscript (DOE)

Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: National Academy of Sciences National Research Council Ford Foundation; National Institute of General Medical Sciences (NIGMS); National Science Foundation (NSF); USDOE Office of Science (SC)

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1559217

Journal Information:: Proceedings of the National Academy of Sciences of the United States of America, Journal Name: Proceedings of the National Academy of Sciences of the United States of America Journal Issue: 21 Vol. 116; ISSN 0027-8424

Publisher:: National Academy of Sciences, Washington, DC (United States)Copyright Statement

Country of Publication:: United States

Language:: English

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