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- HAX1 regulates E3 ubiquitin ligase activity of cIAPs by promoting their dimerization = HAX1의 이합체화로 인한 cIAPs의 유비퀴틴 ligase 활성 조절
- Jin Sun Choi; Byoung Chul Park; Seung-Wook Chi; Kwang-Hee Bae; Sun Hong Kim; S Cho; W C Son; P K Myung; Jeong Hoon Kim; Sung Goo Park
- Bibliographic Citation
- Oncotarget, vol. 5, no. 20, pp. 10084-10099
- Publication Year
- HS-1-associated protein X-1 (HAX1) is a multi-functional protein which was first identified as a Hematopoietic cell specific Lyn Substrate 1 (HS1)-binding protein. Although the roles of HAX1 in apoptosis have been unraveled and HAX1 has been proposed to be involved in several diseases, additional roles of HAX1 are still being identified. Here, we demonstrated that HAX1 directly interacted with cellular Inhibitor of Apoptosis Proteins (cIAPs), ubiquitin E3 ligases which regulate the abundance of cellular proteins, via ubiquitin-dependent proteasomal degradation. We showed that HAX1 promotes auto-ubiquitination and degradation of cIAPs by facilitating the intermolecular homodimerization of RING finger domain. Moreover, HAX1 regulates the non-canonical Nuclear Factor-κB (NF-κB) signaling pathway by modulating the stability of NF-κB-Inducing Kinase (NIK), which is one of the substrates of cIAPs. Taken together, these results unveil a novel role of HAX1 in the non-canonical NF-κB pathway, and provide an important clue that HAX1 is a potential therapeutic target for the treatment of cancer.
- Impact Journals
- Appears in Collections:
- Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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