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All rights reserved. http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RAO7291DekbGegk7YEuUcD1tM06wGfTa_aKr9UKHKkC4c#_5 http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/pav/version 20131211 http://www.tkuhn.ch/bel2nanopub/RAO7291DekbGegk7YEuUcD1tM06wGfTa_aKr9UKHKkC4c#_4 http://www.w3.org/ns/prov#value To evaluate whether Mdg1 actually accumulated within the nucleoli, HeLa cells were transfected with pEGFP-Mdg1, heat shocked, and immunostained with a nucleolus-specific antibody. Red-fluorescence, due to cy3-conjugated secondary antibody, clearly stained the nucleoli within the nucleus. Green fluorescence, due to expression of the transfected fusion construct, exhibited a strict colocalization in heat-shocked cells providing evidence for the nucleolus being the compartment for Mdg1 accumulation during stress (Fig. 7). We then studied whether nucleolar-associated Mdg1 protein could be reexported into the cytosol under recovery conditions. To test this, heat-shocked transfected HeLa cells were allowed to recover at 37 degrees C for 1 and 3 h. The stress-induced translocation of Mdg1 into the nucleoli proved to be reversible within 3 h (Fig. 8), indicating that the localization and transport of Mdg1 is actively controlled by the cell. 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