The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
The tubulin code: Molecular components, readout mechanisms, and functions
Open accessAbstract
Microtubules are cytoskeletal filaments that are dynamically assembled from α/β-tubulin heterodimers. The primary sequence and structure of the tubulin proteins and, consequently, the properties and architecture of microtubules are highly conserved in eukaryotes. Despite this conservation, tubulin is subject to heterogeneity that is generated in two ways: by the expression of different tubulin isotypes and by posttranslational modifications (PTMs). Identifying the mechanisms that generate and control tubulin heterogeneity and how this heterogeneity affects microtubule function are long-standing goals in the field. Recent work on tubulin PTMs has shed light on how these modifications could contribute to a “tubulin code” that coordinates the complex functions of microtubules in cells.
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Cites
HDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403
Microtubule Acetylation Promotes Kinesin-1 Binding and Transport
Reed, N. A., Cai, D., Blasius, T. L., Jih, G. T., Meyhofer, E., Gaertig, J., & Verhey, K. J. (2006) · Current Biology · doi:10.1016/j.cub.2006.09.014 · Cited by 919
Verhey, K. J., & Gaertig, J. (2007) · Cell Cycle · doi:10.4161/cc.6.17.4633 · Cited by 558
Molecular Basis for Age-Dependent Microtubule Acetylation by Tubulin Acetyltransferase
Szyk, A., Deaconescu, A. M., Spector, J., Goodman, B., Valenstein, M. L., Ziolkowska, N. E., Kormendi, V., Grigorieff, N., & Roll-Mecak, A. (2014) · Cell · doi:10.1016/j.cell.2014.03.061 · Cited by 218
Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure
Howes, S. C., Alushin, G. M., Shida, T., Nachury, M. V., & Nogales, E. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-07-0387 · Cited by 183
Cited by
Causes and Consequences of Microtubule Acetylation
Janke, C., & Montagnac, G. (2017) · Current Biology · doi:10.1016/j.cub.2017.10.044 · Cited by 312
Self-citationDifferentiation between oppositely oriented microtubules controls polarized neuronal transport
Tas, R. P., Chazeau, A., Cloin, B. M. C., Lambers, M. L. A., Hoogenraad, C. C., & Kapitein, L. C. (2017) · Neuron · doi:10.1016/j.neuron.2017.11.018 · Cited by 306
Wilson, C., & González-Billault, C. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00381 · Cited by 238
Tyrosination of α‐tubulin controls the initiation of processive dynein–dynactin motility
McKenney, R. J., Huynh, W., Vale, R. D., & Sirajuddin, M. (2016) · The EMBO Journal · doi:10.15252/embj.201593071 · Cited by 232
Posttranslational Modifications of Tubulin and Cilia
Wloga, D., Joachimiak, E., Louka, P., & Gaertig, J. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a028159 · Cited by 183
Metadata
- Authors
- Janke, C.
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2014-08-18
- Volume
- 206
- Issue
- 4
- Pages
- 461-472
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2123211763
- Cited by
- 532
- References
- 5
- FWCI
- 23.22
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
