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Interaction of TPPP/p25 protein with glyceraldehyde‐3‐phosphate dehydrogenase and their co‐localization in Lewy bodies
Author(s) -
Oláh Judit,
Tőkési Natália,
Vincze Orsolya,
Horváth István,
Lehotzky Attila,
Erdei Anna,
Szájli Emília,
Medzihradszky Katalin F.,
Orosz Ferenc,
Kovács Gábor G.,
Ovádi Judit
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.09.037
Subject(s) - glyceraldehyde 3 phosphate dehydrogenase , immunoprecipitation , cytosol , aggresome , chemistry , microbiology and biotechnology , fusion protein , biochemistry , dehydrogenase , biology , enzyme , recombinant dna , apoptosis , autophagy , gene
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 α‐synuclein positive Lewy body.