期刊
FEBS LETTERS
卷 580, 期 25, 页码 5807-5814出版社
WILEY
DOI: 10.1016/j.febslet.2006.09.037
关键词
glyceraldehyde-3-phosphate dehydrogenase; TPPP/p25; microtubule; Parkinson's disease; Lewy body
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 a-synuclein positive Lewy body. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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