Oláh Judit, Tokési Natália, Vincze Orsolya, Horváth István, Lehotzky Attila, Erdei Anna, Szájli Emília, Medzihradszky Katalin F, Orosz Ferenc, Kovács Gábor G, Ovádi Judit
Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Karolina út 29, H-1113 Budapest, Hungary.
FEBS Lett. 2006 Oct 30;580(25):5807-14. doi: 10.1016/j.febslet.2006.09.037. Epub 2006 Sep 27.
TPPP/p25, a flexible unstructured protein, binds to tubulin and induces aberrant microtubule assemblies. We identified hereby glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as a new interacting partner of TPPP/p25. The immunoprecipitation and affinity chromatographic experiments with bovine brain cell-free extract revealed that the interaction was salt and NAD(+) sensitive while ELISA showed resistant and firm association of the two isolated proteins. In transfected HeLa cells at low expression level of EGFP-TPPP/p25, while the green fusion protein aligned at the microtubular network, GAPDH distributed uniformly in the cytosol. However, at high expression level, GAPDH co-localized with TPPP/p25 in the aggresome-like aggregate. Immunohistochemistry showed enrichment of TPPP/p25 and GAPDH within the alpha-synuclein positive Lewy body.
