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Bundling of microtubules by glyceraldehyde‐3‐phosphate dehydrogenase and its modulation by ATP
Open accessAbstract
Glyceraldehyde‐3‐phosphate dehydrogenase from different origins (brain, muscle, erythrocytes) binds to microtubules polymerized from pure brain tubulin and causes bundle formation in vitro. ATP is shown to dissociate these bundles into individual microtubules, while the dehydrogenase is not displaced from the polymers by this nucleotide. ATP can be replaced by adenosine 5′‐(ß,γ‐imido]triphosphate, a nonhydrolyzable analog of ATP. These data are interpreted in terms of dissociation of the glyceraldehyde‐3‐phosphate dehydrogenase tetramer into dimers by ATP. The enzyme is also efficiently purified by a tubulin‐Sepharose affinity chromatography.
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Cited by
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Metadata
- Authors
- HUITOREL, P., & PANTALONI, D.
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1985-07
- Volume
- 150
- Issue
- 2
- Pages
- 265-269
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W1978774070
- Cited by
- 179
- References
- 0
- FWCI
- 1.67
- Type
- journal article
- Language
- en
- Open access
- bronze
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- HUITOREL, P., & PANTALONI, D. (1985). Bundling of microtubules by glyceraldehyde‐3‐phosphate dehydrogenase and its modulation by ATP. European Journal of Biochemistry. https://doi.org/10.1111/j.1432-1033.1985.tb09016.x
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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