Literature DB >> 4018083

Bundling of microtubules by glyceraldehyde-3-phosphate dehydrogenase and its modulation by ATP.

P Huitorel, D Pantaloni.   

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.

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Year:  1985        PMID： 4018083     DOI： 10.1111/j.1432-1033.1985.tb09016.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN： 0014-2956


  35 in total

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