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Identification of the ring Finger protein 6 (RNF6)-interacting proteins

ABSTRACT: In this project, RNF6-interacting proteins were precipitated and purified by an anti-body purification strategy followed by HPLC-coupled tandem mass spectrometry (LC/MS/MS).

ORGANISM(S): Homo Sapiens

SUBMITTER: Xinliang Mao

PROVIDER: PXD032990 | iProX | Wed Apr 06 00:00:00 BST 2022

REPOSITORIES: iProX

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Induction of zinc finger protein RNF6 auto-ubiquitination for the treatment of myeloma and chronic myeloid leukemia.

Zhuang Haixia H Ren Ying Y Mao Chenyu C Zhong Yueya Y Zhang Zubin Z Cao Biyin B Zhang Yuming Y Huang Jinqi J Xu Guoqiang G Huang Zhenqian Z Xu Yujia Y Mao Xinliang X

The Journal of biological chemistry 20220801 9

The zinc finger ubiquitin ligase RNF6 has been proposed as a potential therapeutic target in several cancers, but understanding its molecular mechanism of degradation has been elusive. In the present study, we find that RNF6 is degraded via auto-ubiquitination in a manner dependent on its Really Interesting New Gene (RING) domain. We determine that when the RING domain is deleted (ΔRING) or the core cysteine residues in the zinc finger are mutated (C632S/C635S), the WT protein, but not the ΔRING ...[more]

PMID: 35926709

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