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

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  • Author(s): Huitorel P; Pantaloni D
  • Source:
    European journal of biochemistry [Eur J Biochem] 1985 Jul 15; Vol. 150 (2), pp. 265-9.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 0107600 Publication Model: Print Cited Medium: Print ISSN: 0014-2956 (Print) Linking ISSN: 00142956 NLM ISO Abbreviation: Eur J Biochem Subsets: MEDLINE
    • Publication Information:
      Publication: -2004: Oxford, UK : Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
      Original Publication: Berlin, New York, Springer.
    • Subject Terms:
      Adenosine Triphosphate/*pharmacology ; Glyceraldehyde-3-Phosphate Dehydrogenases/*metabolism ; Microtubules/*metabolism; Adenosine Triphosphate/analogs & derivatives ; Animals ; Brain/metabolism ; In Vitro Techniques ; Microtubules/drug effects ; Swine ; Tubulin/metabolism
    • 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.
    • Accession Number:
      0 (Tubulin)
      8L70Q75FXE (Adenosine Triphosphate)
      EC 1.2.1.- (Glyceraldehyde-3-Phosphate Dehydrogenases)
    • Publication Date:
      Date Created: 19850715 Date Completed: 19850905 Latest Revision: 20190620
    • Publication Date:
      20231215
    • Accession Number:
      10.1111/j.1432-1033.1985.tb09016.x
    • Accession Number:
      4018083