ArticleNature communications2016
Reversal of axonal growth defects in an extraocular fibrosis model by engineering the kinesin-microtubule interface.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 37 citations in OpenAlex.
- Purification, Fluorescent Labeling, and Detyrosination of Mammalian Cell Tubulin for Biochemical Assays.Cytoskeleton (Hoboken, N.J.) · 2025Article
- Distinct Clinical Phenotypes in KIF1A-Associated Neurological Disorders Result from Different Amino Acid Substitutions at the Same Residue in KIF1A.Biomolecules · 2025Article
- Prevention and treatment of peri-implant fibrosis by functionally inhibiting skeletal cells expressing the leptin receptor.Nature biomedical engineering · 2024Article
- Clinical and genetic characteristics of Chinese patients with congenital fibrosis of the extraocular muscles.Orphanet journal of rare diseases · 2024Article
- Presynaptic perspective: Axonal transport defects in neurodevelopmental disorders.The Journal of cell biology · 2024Review
- Tubulin CFEOM mutations both inhibit or activate kinesin motor activity.Molecular biology of the cell · 2024Article
- Unraveling the interplay of kinesin-1, tau, and microtubules in neurodegeneration associated with Alzheimer's disease.Frontiers in cellular neuroscience · 2024Review
- TUBB3 and KIF21A in neurodevelopment and disease.Frontiers in neuroscience · 2023Review
- Clinical and genetic characteristics of Chinese patients with congenital cranial dysinnervation disorders.Orphanet journal of rare diseases · 2022Article
- Understanding molecular mechanisms and predicting phenotypic effects of pathogenic tubulin mutations.PLoS computational biology · 2022Article
- Plus and minus ends of microtubules respond asymmetrically to kinesin binding by a long-range directionally driven allosteric mechanism.Science advances · 2022Article
- Reconstituting Microtubules: A Decades-Long Effort From Building Block Identification to the Generation of Recombinant α/β-Tubulin.Frontiers in cell and developmental biology · 2022Review
- TUBB3 Arg262His causes a recognizable syndrome including CFEOM3, facial palsy, joint contractures, and early-onset peripheral neuropathy.Human genetics · 2021Article
- Axonal Growth Abnormalities Underlying Ocular Cranial Nerve Disorders.Annual review of vision science · 2021Review
- GTP-dependent formation of straight tubulin oligomers leads to microtubule nucleation.The Journal of cell biology · 2021Article
- TUBA1A mutations identified in lissencephaly patients dominantly disrupt neuronal migration and impair dynein activity.Human molecular genetics · 2019Article
- TAPping into the treasures of tubulin using novel protein production methods.Essays in biochemistry · 2018Review
- Neuronal-Specific TUBB3 Is Not Required for Normal Neuronal Function but Is Essential for Timely Axon Regeneration.Cell reports · 2018Article
- An allosteric propofol-binding site in kinesin disrupts kinesin-mediated processive movement on microtubules.The Journal of biological chemistry · 2018Article
- Ocular congenital cranial dysinnervation disorders (CCDDs): insights into axon growth and guidance.Human molecular genetics · 2017Review
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mutations in human β3-tubulin (TUBB3) cause an ocular motility disorder termed congenital fibrosis of the extraocular muscles type 3 (CFEOM3). In CFEOM3, the oculomotor nervous system develops abnormally due to impaired axon guidance and maintenance; however, the underlying mechanism linking TUBB3 mutations to axonal growth defects remains unclear. Here, we investigate microtubule (MT)-based motility in vitro using MTs formed with recombinant TUBB3. We find that the disease-associated TUBB3 mutations R262H and R262A impair the motility and ATPase activity of the kinesin motor. Engineering a mutation in the L12 loop of kinesin surprisingly restores a normal level of motility and ATPase activity on MTs carrying the R262A mutation. Moreover, in a CFEOM3 mouse model expressing the same mutation, overexpressing the suppressor mutant kinesin restores axonal growth in vivo. Collectively, these findings establish the critical role of the TUBB3-R262 residue for mediating kinesin interaction, which in turn is required for normal axonal growth and brain development.
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