The C terminus of tubulin, a versatile partner for cationic molecules: binding of Tau, polyamines, and calcium.

ABSTRACT: The C-terminal region of tubulin is involved in multiple aspects of the regulation of microtubule assembly. To elucidate the molecular mechanisms of this regulation, we study here, using different approaches, the interaction of Tau, spermine, and calcium, three representative partners of the tubulin C-terminal region, with a peptide composed of the last 42 residues of α1a-tubulin. The results show that their binding involves overlapping amino acid stretches in the C-terminal tubulin region: amino acid residues 421-441 for Tau, 430-432 and 444-451 for spermine, and 421-443 for calcium. Isothermal titration calorimetry, NMR, and cosedimentation experiments show that Tau and spermine have similar micromolar binding affinities, whereas their binding stoichiometry differs (C-terminal tubulin pe

SUBMITTER: Lefevre J 

PROVIDER: S-EPMC3024800 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature