Bundling of microtubules by glyceraldehyde‐3‐phosphate dehydrogenase and its modulation by ATP
Year: 1985
Type: article
Abstract: 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'-(beta, gamma-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.
Source: European Journal of Biochemistry
Authors: Philippe HUITOREL, Dominique PANTALONI
Institution: Centre National de la Recherche Scientifique
Language: English
Subfield: Cell Biology
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W1978774070