دورية
In VitroPolymerization of Embryonic MAP-2c and Fragments of the MAP-2 Microtubule Binding Region into Structures Resembling Paired Helical Filaments*
العنوان: | In VitroPolymerization of Embryonic MAP-2c and Fragments of the MAP-2 Microtubule Binding Region into Structures Resembling Paired Helical Filaments* |
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المؤلفون: | DeTure, Michael A., Yi Zhang, Edith, Bubb, Michael R., Purich, Daniel L. |
المصدر: | Journal of Biological Chemistry; December 1996, Vol. 271 Issue: 51 p32702-32706, 5p |
مستخلص: | The microtubule-associated protein Tau is widely regarded as the principal component of paired helical filaments comprising Alzheimer neurofibrillary tangles. Tau fragments containing the non-identical repeat region formed structures resembling paired helical filaments (Schweers, O., Mandelkow, M., Biernat, J., and Mandelkow, E. (1995) Proc. Natl. Acad. Sci. U. S. A.92, 8463-8467). MAP-2, the other structurally related neuronal microtubule-associated protein, has not been implicated in paired helical filament formation. We now describe the assembly of paired helical filament-like structures from MAP-2 polypeptides containing only 100 residues. A dimeric species, stabilized by an interchain disulfide, appears to be involved in the assembly reaction. We also investigated the polymerization of embryonic MAP-2c, which, except for its microtubule binding region, is structurally distinct from Tau. Full-length MAP-2c formed paired helical filament-like polymers. Polymerized MAP-2c and the microtubule binding region fragment readily bound thioflavin-S, a dye that stains paired helical filaments in the histochemical diagnosis of Alzheimer's disease. Our unprecedented finding that a small MAP-2 microtubule binding region fragment and MAP-2c can form structures resembling straight filaments or Pronase-treated paired helical filaments raises fundamental questions concerning the role of MAP-2 in the pathobiology of Alzheimer disease. |
قاعدة البيانات: | Supplemental Index |
تدمد: | 00219258 1083351X |
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DOI: | 10.1074/jbc.271.51.32702 |