Tubulin modifications and their cellular functions
Open accessAbstract
All microtubules are built from a basic alpha/beta-tubulin building block, yet subpopulations of microtubules can be differentially marked by a number of post-translational modifications. These modifications, conserved throughout evolution, are thought to act individually or in combination to control specific microtubule-based functions, analogous to how histone modifications regulate chromatin functions. Here we review recent studies demonstrating that tubulin modifications influence microtubule-associated proteins such as severing proteins, plus-end tracking proteins, and molecular motors. In this way, tubulin modifications play an important role in regulating microtubule properties, such as stability and structure, as well as microtubule-based functions, such as ciliary beating, cell division, and intracellular trafficking.
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Post-translational modifications of tubulin such as acetylation and tyrosination/detyrosination can act either singly or in concert with other modifications to control motor recruitment in a cargo-specific manner.
“Post-translational modifications of tubulin such as acetylation and tyrosination/detyrosination can act either singly or in concert with other modifications to control motor recruitment in a cargo-specific manner (Hammond et al., 2008; Mackeh et al., 2013).”
From The cell biology of the retinal pigment epithelium (2020) · cites this paper as Hammond et al., 2008
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- Authors
- Hammond, J. W., Cai, D., & Verhey, K. J.
- Affiliations
- University of Michigan (US)
- Corresponding author
- Verhey, Kristen J
- Venue
- Current Opinion in Cell Biology
- Publisher
- Elsevier BV
- Published
- 2008-02
- Volume
- 20
- Issue
- 1
- Pages
- 71-76
- ISSN
- 0955-0674 (ISSN-L)
- PMC
- PMC2274889
- OpenAlex
- W2033241989
- Cited by
- 509
- References
- 50
- Citations by year
- 2026: 7 · 2025: 17 · 2024: 9 · 2023: 22 · 2022: 21 · 2021: 14 · 2020: 16 · 2019: 24 · 2018: 26 · 2017: 25 · 2016: 26 · 2015: 33 · 2014: 33 · 2013: 34 · 2012: 41
- FWCI
- 4.34
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Current Opinion in Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (GM070862, R01GM070862)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Keywords
- tubulin modification, post-translational modification, microtubules, αβ-tubulin, microtubule stability, microtubule-associated proteins, plus-end tracking proteins, molecular motors, ciliary beating, cell division, intracellular trafficking
- MeSH terms
- Acetylation, Animals, Humans, Microtubules, Protein Processing, Post-Translational, Tubulin, Protein Structure, Secondary, Dimerization
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