Polymorphism of tubulin oligomers in the presence of microtubule-associated proteins. Implications in microtubule assembly.

The interaction between tubulin and microtubule-associated proteins (MAPs) in solutions of cycled microtubule protein has been studied by using radioactively labeled MAPs. Kinetic data of MAP association to microtubules in the polymerization process indicate that an oligomer P of tubulin and MAPs is the polymerizing species. Analysis of MAP binding to microtubules formed from solutions in which the ratio MAPs/tubulin was varied shows evidence for a polymorphism of tubulin-MAP oligomers. When the ratio MAPs/tubulin is decreased by addition of dimeric tubulin to 3 times cycled microtubule protein, an oligomer P' less rich in MAPs than P and unable to incorporate in microtubules is formed. The data further show that while tau, MAP1, and MAP2 can bind to oligomer P, only MAP1 and MAP2 can bind to oligomer P'. Therefore, the interactions of tau factor and of MAP1 and MAP2 with tubulin follow different patterns.