STOP proteins are responsible for the high degree of microtubule stabilization observed in neuronal cells
Open accessAbstract
Neuronal differentiation and function require extensive stabilization of the microtubule cytoskeleton. Neurons contain a large proportion of microtubules that resist the cold and depolymerizing drugs and exhibit slow subunit turnover. The origin of this stabilization is unclear. Here we have examined the role of STOP, a calmodulin-regulated protein previously isolated from cold-stable brain microtubules. We find that neuronal cells express increasing levels of STOP and of STOP variants during differentiation. These STOP proteins are associated with a large proportion of microtubules in neuronal cells, and are concentrated on cold-stable, drug-resistant, and long-lived polymers. STOP inhibition abolishes microtubule cold and drug stability in established neurites and impairs neurite formation. Thus, STOP proteins are responsible for microtubule stabilization in neurons, and are apparently required for normal neurite formation.
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Dendritic-somatic MTs are capped by special MAPs that prevent de-polymerization, and are thus stable and suitable for long term information encoding and memory.
“Dendritic-somatic MTs are capped by special MAPs that prevent de-polymerization [63], and are thus stable and suitable for long term information encoding and memory (Fig. 4 [64]).”
From Consciousness in the universe (2014) · cites this paper as [63]
The Abstract reports that STOP proteins associate with neuronal microtubules and that inhibiting STOP abolishes their resistance to cold and depolymerizing drugs. But the Results section on DRG-cell axons describes STOP along axonal microtubules, not proteins capping dendritic-somatic microtubule ends. The separate claim about information encoding and memory is attached to [64], not this source. (LLM, conf=0.86)
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References 57 · Cited by 132
Research works printed but not linked: 1
- Cambray-Deakin, M.A. 1991. Cytoskeleton of the growing axon. In The Neuronal Cytoskeleton. R.D. Burgoyne, editor. Wiley-Liss, Inc. New York. 233–255.
- Authors
- Guillaud, L., Bosc, C., Fourest-Lieuvin, A., Denarier, E., Pirollet, F., Lafanechère, L., & Job, D.
- Affiliations
- Inserm (FR)
- CEA-Laboratoire du Cytosquelette, INSERM Unité 366, DBMS/CS, CEA-Grenoble, 38054 Grenoble Cedex 9, France
- Corresponding author
- Job, Didier
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 1998-07-13
- Volume
- 142
- Issue
- 1
- Pages
- 167-179
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2133033
- OpenAlex
- W1989901971
- Cited by
- 132
- References
- 57
- Citations by year
- 2026: 3 · 2025: 5 · 2023: 2 · 2022: 2 · 2021: 9 · 2020: 4 · 2019: 4 · 2018: 2 · 2017: 4 · 2016: 2 · 2015: 4 · 2014: 3 · 2013: 7 · 2012: 9
- FWCI
- 1.92
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Keywords
- microtubule stabilization, neuronal differentiation, neurite formation, calmodulin, microtubule cytoskeleton, brain microtubules
- MeSH terms
- Amino Acid Sequence, Animals, Axons, Cells, Cultured, Cold Temperature, Drug Resistance, Ganglia, Spinal, Microtubule-Associated Proteins, Microtubules, Molecular Sequence Data, Neurons, Rabbits, Tubulin, Tyrosine, Nocodazole, PC12 Cells, Rats
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