HSP70 protects BCL2L12 and BCL2L12A from N‐terminal ubiquitination‐mediated proteasomal degradation

@article{Yang2009HSP70PB,
  title={HSP70 protects BCL2L12 and BCL2L12A from N‐terminal ubiquitination‐mediated proteasomal degradation},
  author={Jun-wu Yang and Yi Hong and Wenzong Wang and Weibing Wu and Yayun Chi and Hongliang Zong and Xiangfei Kong and Yuanyan Wei and Xiao-jing Yun and Chunming Cheng and Kangli Chen and Jianxin Gu},
  journal={FEBS Letters},
  year={2009},
  volume={583}
}

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It is observed that ARF can be degraded in vitro by the 20S proteasome, in the absence of ubiquitination and this effect can be counteracted by TBP-1, and observations seem relevant in the comprehension of the regulation of ARF metabolism.

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This chapter describes methods that will enable researchers to identify this novel mode of ubiquitination and the identity of the set of proteins in the proteome that undergoes N-terminal Ubiquitination.