The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
Stabilization and post‐translational modification of microtubules during cellular morphogenesis
Abstract
This review discusses the possible role of α‐tubulin detyrosination, a reversible post‐translational modification that occurs at the protein's C‐terminus, in cellular morphogenesis. Higher eukaryotic cells possess a cyclic post‐translational mechanism by which dynamic microtubules are differentiated from their more stable counterparts; a tubulin‐specific carboxypeptidase detyrosinates tubulin protomers within microtubules, while the reverse reaction, tyrosination, is performed on the soluble protomer by a second tubulin‐specific enzyme, tubulin tyrosine ligase. In general, the turnover of microtubules in undifferentiated, proliferating cells is so rapid that the microtubules accumulate very little detyrosinated tubulin; that is, they are enriched in tyrosinated tubulin. However, an early event common to at least three well‐studied morphogenetic events myogenesis, neuritogenesis, and directed cell motility is the elaboration of a polarized array of stable microtubules that become enriched in detyrosinated tubulin. The formation of this specialized array of microtubules in specific locations in cells undergoing morphogenesis suggests that it plays an important role in generating cellular asymmetries.
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Cites
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Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
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Conde, C., & Cáceres, A. (2009) · Nature Reviews Neuroscience · doi:10.1038/nrn2631 · Cited by 1,086
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Akhmanova, A., & Steinmetz, M. O. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2369 · Cited by 1,047
Verhey, K. J., & Gaertig, J. (2007) · Cell Cycle · doi:10.4161/cc.6.17.4633 · Cited by 558
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Metadata
- Authors
- Bulinski, J. C., & Gundersen, G. G.
- Venue
- BioEssays
- Publisher
- Wiley
- Published
- 1991-06
- Volume
- 13
- Issue
- 6
- Pages
- 285-293
- ISSN
- 0265-9247 (ISSN-L)
- 1521-1878
- OpenAlex
- W1966975951
- Cited by
- 274
- References
- 50
- FWCI
- 1.16
- Type
- journal article
- Language
- en
- Open access
- closed
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