Structure and phosphorylation of microtubule-associated protein 2 (MAP 2).

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Abstract
Chymotryptic fragments of [calf brain] microtubule-associated protein 2 (MAP2) containing the portion of the molecule responsible for promoting microtubule assembly were identified. These assembly-promoting fragments displaced intact MAP 2, but not MAP 1, from assembled microtubules. This indicates that the association of MAP 2 with the microtubule surface is reversible. Both the assembly-promoting fragments and fragments representing the portion of the MAP 2 molecule observed as a projection on the microtubule surface contained sites for endogenous cyclic AMP-dependent phosphorylation. The projection fragments were capable of endogenous phosphorylation even after their physical separation from microtubules. This suggests an intimate association of a kinase activity with the projections. Detailed analysis of the properties of the chymotryptic fragments of MAP 2 led to a map of the molecule showing the major sites of proteolytic attack and the sites of phosphorylation.
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