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Science 11 November 1988:
Vol. 242. no. 4880, pp. 936 - 939
DOI: 10.1126/science.3142041
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Articles

Science, Vol 242, Issue 4880, 936-939
Copyright © 1988 by American Association for the Advancement of Science

articles

Microtubule-associated protein MAP2 shares a microtubule binding motif with tau protein

SA Lewis, DH Wang, and NJ Cowan

Department of Biochemistry, New York University Medical Center, NY 10016.

The microtubule-associated protein MAP2 is a prominent large-sized component of purified brain microtubules that, like the 36- to 38-kilodalton tau proteins, bears antigenic determinants found in association with the neurofibrillary tangles of Alzheimer's disease. The complete sequence of mouse brain MAP2 was determined from a series of overlapping cloned complementary DNAs. The sequence of the carboxyl-terminal 185 amino acids is very similar (67 percent) to a corresponding region of tau protein, and includes a series of three imperfect repeats, each 18 amino acids long and separated by 13 or 14 amino acids. A subcloned fragment spanning the first two of the 18-amino acid repeats was expressed as a polypeptide by translation in vitro. This polypeptide copurified with microtubules through two successive cycles of polymerization and depolymerization, whereas a control polypeptide derived from the amino-terminal region of MAP2 completely failed to copurify. These data imply that the carboxyl-terminal domain containing the 18-amino acid repeats constitutes the microtubule binding site in MAP2. The occurrence of these repeats in tau protein suggests that these may be a general feature of microtubule binding proteins.


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