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. 2010 Aug 23;190(4):637–650. doi: 10.1083/jcb.200908092

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© 2010 Minami et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 4. — BAG-6 is involved in the metabolism of puromycin-induced nascent chain polypeptides. (A) BAG-6 bound to truncated puromycin-labeled proteins. After treatment with 5 µg/ml puromycin for the indicated times, HeLa cells were harvested, the puromycin-labeled polypeptides were immunoprecipitated from cell extracts with antibody against puromycin, and the precipitates were probed with antibody against BAG-6. (B and C) BAG-6 localized on cytoplasmic dots after puromycin treatment. HeLa cells were treated with 5 µg/ml puromycin for 2 h and extracted with 1% Triton X-100. Fixed cells were stained with antibodies against BAG-6, puromycin (B), and ubiquitin (C). Note that a part of BAG-6 also localized in the nucleus. (D–F) BAG-6 controlled the dynamics of puromycin-induced aggregate formation. Puromycin-treated HeLa cells with BAG-6 siRNA contained enlarged but reduced numbers of ubiquitin-positive cytoplasmic aggregates. Error bars represent SD calculated from three experiments. (G) 48 h after siRNA treatment, cells were treated with puromycin for 24 h and cell viability was analyzed with a cell counting kit. The percent viability was normalized to the cells without puromycin treatment.