Biochemical and cell biological characterizations of microtubule-associated proteins

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Microtubule is a ubiquitous structure in eukaryotic cytoplasm, playing a variety of important roles. Since the structure of microtubules is rather simple, accessory proteins that bind to microtubules are important in investing microtubules with diverse functions. I have been working on some of the accessory proteins called microtubule-associated proteins (MAPs), such as the 190-kDa MAP (MAP4) and the 250-kDa MAP (ferritin), to name a few. In this article, my accomplishments on MAP4 are summarized. MAP4 has a polar structure made of a projection domain and a microtubule-binding domain. The latter is further dividedinto a Pro-rich region, a Repeat region, and a Tail region. The Pro-rich region enhancesthe binding of MAP4 to microtubules, while the Repeat region ensures the promotion of ordered microtubule assembly. MAP4 has several isoforms produced by alternative splicing of a single gene. Isoforms with deletions in the Repeat region may modulate the microtubule surface property, which in turn may regulate the interaction between microtubules and other cytoplasmic structures. An isoform with a deletion in the Pro-rich region is neuron-specific.Since this isoform is rapidly exchanging between microtubule-bound and unbound states in the living cells, it may serve the dynamic reorganization of neural cytoskeletons.
2009-10-20