AI Article Synopsis
- The study investigates the role of HS1-binding protein 3 (HS1BP3) in essential tremor and lymphocyte activation, finding it partially located in mitochondria and the endoplasmic reticulum.
- Overexpression of HS1BP3 led to apoptosis in HEK293T and HeLa cells, indicated by nuclear DNA condensation and PS externalization.
- HS1BP3 was found to enhance AP-1-mediated transcription in a dose-dependent manner and its effects were modulated by HS1 and HS1BP3 suppression.
Article Abstract
In the present study, we characterized the function of HS1-binding protein 3 (HS1BP3), which is mutated in essential tremor and may be involved in lymphocyte activation. We found that HS1BP3 localized to the mitochondria and endoplasmic reticulum partially. Overexpression of HS1BP3 induced apoptosis in HEK293T and HeLa cell lines. When these cell lines were transfected with HS1BP3, they exhibited nuclear DNA condensation, externalization of phosphatidylserine (PS), and cleavage of poly ADP ribose polymerase (PARP). Furthermore, suppression of HS1BP3 or HS1 expression attenuates HS1BP3 induced apoptosis. In addition, HS1BP3 enhanced activator protein 1 (AP-1)-mediated transcription in a dose-dependent manner. Therefore, we conclude that HS1BP3 regulates apoptosis via HS1 and stimulates AP-1-mediated transcription.
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| http://dx.doi.org/10.5483/BMBRep.2011.44.6.381 | DOI Listing |
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