CHIP: A new modulator of human malignant disorders
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Zhe Cao1,*, Guanqiao Li1,*, Qianqian Shao1, Gang Yang1, Lianfang Zheng2, Taiping Zhang1 and Yupei Zhao1
1, Department of General Surgery, Peking Union Medical College Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China
2, Department of Nuclear Medicine, Peking Union Medical Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China
* These authors have contributed equally to this work
Taiping Zhang, email:
Yupei Zhao, email:
Keywords: CHIP; cancer; co-chaperon; ubiquitination
Received: October 25, 2015 Accepted: February 05, 2016 Published: March 20, 2016
Carboxyl terminus of Hsc70-interacting protein (CHIP) is known as a chaperone-associated E3 for a variety of protein substrates. It acts as a link between molecular chaperones and ubiquitin–proteasome system. Involved in the process of protein clearance, CHIP plays a critical role in maintaining protein homeostasis in diverse conditions. Here, we provide a comprehensive review of our current understanding of CHIP and summarize recent advances in CHIP biology, with a focus on CHIP in the setting of malignancies.
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