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Phosphorylation of tubulin enhances its interaction with membranes

Nature volume 323, pages 827–828 (1986)Cite this article

Abstract

Tubulin, the main component of intracellular microtubules, is also a major protein in subcellular membrane preparations1–4 and can interact with biological5–7 and artificial8–12 membranes in vitro. Of particular interest is the association of tubulin with postsynaptic junctional lattices enriched in a polypeptide of relative molecular mass (Mr) 50,000 (50K)13, recently identified as the major subunit of the calmodulin-dependent protein kinase14. Phosphorylation of tubulin with a calmodulin-dependent protein kinase similar to that found in postsynaptic densities inhibits its ability to self-assemble into microtubules in a reversible fashion15. This involves the phosphorylation of residues in its 4K carboxy-terminal region, a domain that seems to regulate its self-assembly16–18. The results presented here suggest that the phosphorylation of tubulin with this kinase enhances its ability to interact with membranes. This effect is reversible.

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Authors and Affiliations

  1. Centre de Biologia Molecular (CSIC-UAM), Universidad Autónoma, Canto Blanco, 28049, Madrid, Spain

    Alan J. Hargreaves, Francisco Wandosell & Jesús Avila

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  1. Alan J. Hargreaves
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  2. Francisco Wandosell
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  3. Jesús Avila
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Hargreaves, A., Wandosell, F. & Avila, J. Phosphorylation of tubulin enhances its interaction with membranes. Nature 323, 827–828 (1986). https://doi.org/10.1038/323827a0

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