Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure
Abstract
Tubulin undergoes posttranslational modifications proposed to specify microtubule subpopulations for particular functions. Most of these modifications occur on the C-termini of tubulin and may directly affect the binding of microtubule-associated proteins (MAPs) or motors. Acetylation of Lys-40 on α-tubulin is unique in that it is located on the luminal surface of microtubules, away from the interaction sites of most MAPs and motors. We investigate whether acetylation alters the architecture of microtubules or the conformation of tubulin, using cryo–electron microscopy (cryo-EM). No significant changes are observed based on protofilament distributions or microtubule helical lattice parameters. Furthermore, no clear differences in tubulin structure are detected between cryo-EM reconstructions of maximally deacetylated or acetylated microtubules. Our results indicate that the effect of acetylation must be highly localized and affect interaction with proteins that bind directly to the lumen of the microtubule. We also investigate the interaction of the tubulin acetyltransferase, αTAT1, with microtubules and find that αTAT1 is able to interact with the outside of the microtubule, at least partly through the tubulin C-termini. Binding to the outside surface of the microtubule could facilitate access of αTAT1 to its luminal site of action if microtubules undergo lateral opening between protofilaments.
- Authors:
-
- Univ. of California, Berkeley, CA (United States). Biophysics Graduate Group
- Univ. of California, Berkeley, CA (United States).Howard Hughes Medical Inst. Dept. of Molecular and Cell Biology
- Stanford Univ., CA (United States). School of Medicine. Dept. of Molecular and Cellular Physiology
- Univ. of California, Berkeley, CA (United States).Howard Hughes Medical Inst. Dept. of Molecular and Cell Biology; Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Life Sciences Division
- Publication Date:
- Research Org.:
- Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States); Univ. of California, Berkeley, CA (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division
- OSTI Identifier:
- 1625232
- Grant/Contract Number:
- AC02-05CH11231
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Molecular Biology of the Cell
- Additional Journal Information:
- Journal Volume: 25; Journal Issue: 2; Journal ID: ISSN 1059-1524
- Publisher:
- American Society for Cell Biology
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; Cell Biology
Citation Formats
Howes, Stuart C., Alushin, Gregory M., Shida, Toshinobu, Nachury, Maxence V., and Nogales, Eva. Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure. United States: N. p., 2013.
Web. doi:10.1091/mbc.e13-07-0387.
Howes, Stuart C., Alushin, Gregory M., Shida, Toshinobu, Nachury, Maxence V., & Nogales, Eva. Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure. United States. https://doi.org/10.1091/mbc.e13-07-0387
Howes, Stuart C., Alushin, Gregory M., Shida, Toshinobu, Nachury, Maxence V., and Nogales, Eva. Wed .
"Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure". United States. https://doi.org/10.1091/mbc.e13-07-0387. https://www.osti.gov/servlets/purl/1625232.
@article{osti_1625232,
title = {Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure},
author = {Howes, Stuart C. and Alushin, Gregory M. and Shida, Toshinobu and Nachury, Maxence V. and Nogales, Eva},
abstractNote = {Tubulin undergoes posttranslational modifications proposed to specify microtubule subpopulations for particular functions. Most of these modifications occur on the C-termini of tubulin and may directly affect the binding of microtubule-associated proteins (MAPs) or motors. Acetylation of Lys-40 on α-tubulin is unique in that it is located on the luminal surface of microtubules, away from the interaction sites of most MAPs and motors. We investigate whether acetylation alters the architecture of microtubules or the conformation of tubulin, using cryo–electron microscopy (cryo-EM). No significant changes are observed based on protofilament distributions or microtubule helical lattice parameters. Furthermore, no clear differences in tubulin structure are detected between cryo-EM reconstructions of maximally deacetylated or acetylated microtubules. Our results indicate that the effect of acetylation must be highly localized and affect interaction with proteins that bind directly to the lumen of the microtubule. We also investigate the interaction of the tubulin acetyltransferase, αTAT1, with microtubules and find that αTAT1 is able to interact with the outside of the microtubule, at least partly through the tubulin C-termini. Binding to the outside surface of the microtubule could facilitate access of αTAT1 to its luminal site of action if microtubules undergo lateral opening between protofilaments.},
doi = {10.1091/mbc.e13-07-0387},
journal = {Molecular Biology of the Cell},
number = 2,
volume = 25,
place = {United States},
year = {Wed Nov 13 00:00:00 EST 2013},
month = {Wed Nov 13 00:00:00 EST 2013}
}
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