In vitro polymerization of embryonic MAP-2c and fragments of the MAP-2 microtubule binding region into structures resembling paired helical filaments.

The Journal of Biological Chemistry
M A DeTureDaniel L Purich

Abstract

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 MA...Continue Reading

References

Feb 1, 1976·Journal of the Neurological Sciences·H M WiśniewskiR D Terry
Jun 1, 1986·Proceedings of the National Academy of Sciences of the United States of America·J G WoodL I Binder
Dec 1, 1989·Journal of Neuroscience Research·M DammermanB Shafit-Zagardo
Jun 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·C M WischikA Klug
Dec 1, 1984·Proceedings of the National Academy of Sciences of the United States of America·K S KosikD J Selkoe
Oct 13, 1995·The Journal of Biological Chemistry·D M Wilson, L I Binder
Aug 29, 1995·Proceedings of the National Academy of Sciences of the United States of America·O SchweersE Mandelkow
Jan 10, 1994·FEBS Letters·R A CrowtherM Goedert
Oct 1, 1963·Journal of Neuropathology and Experimental Neurology·R D TERRY

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Citations

Nov 10, 2009·Journal of Chemical Biology·Megan H WrightEdward W Tate
Sep 11, 1998·Neurobiology of Aging·I VincentP Davies
Nov 29, 2002·Eukaryotic Cell·Brian D ShawMichelle Momany
May 11, 2000·Proceedings of the National Academy of Sciences of the United States of America·M von BergenE Mandelkow
Mar 19, 2004·Current Biology : CB·Benoit RogerShelley Halpain
Nov 5, 2003·Journal of Neurobiology·Leif Dehmelt, Shelley Halpain
Nov 30, 1999·Molecular Cell Biology Research Communications : MCBRC·L Di NotoD L Purich

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