Abstract
AMPLE evidence now exists that, in addition to soluble, cytoplasmic tubulin, many tissues contain variable proportions of particulate tubulin as judged from colchicine-binding studies1–6. This colchicine-binding activity is not contamination from cytoplasmic microtubules, and is associated with a fraction enriched in plasma membrane markers6. The activity exhibits the ligand-binding properties of purified tubulin and reacts with antibodies against soluble brain tubulin. Finally, when the binding activity is solubilised from membranes it exhibits normal binding behaviour toward antimitotic agents, normal thermal lability, and normal interaction with antibody6. What was not clear was whether this tubulin could participate in polymerisation reactions to form microtubules. We report here that solubilised, labelled tubulin copolymerises with cytoplasmic tubulin through repeated cycles of polymerisation and depolymerisation.
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BHATTACHARYYA, B., WOLFF, J. Polymerisation of membrane tubulin. Nature 264, 576–577 (1976). https://doi.org/10.1038/264576a0
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DOI: https://doi.org/10.1038/264576a0
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