NIR is degraded by the anaphase-promoting complex proteasome pathway | Zendy

Ho Joong Jeong | Zendy; Kuk Kang | Zendy; Yang Hee Kim | Zendy; Jin Han | Zendy

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NIR is degraded by the anaphase-promoting complex proteasome pathway

Author(s) -

Ho Joong Jeong,

Kuk Kang,

Yang Hee Kim,

Jin Han

Publication year - 2014

Publication title -

archives of biological sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.217

H-Index - 25

eISSN - 1821-4339

pISSN - 0354-4664

DOI - 10.2298/abs1404493j

Subject(s) - nucleolus , mg132 , microbiology and biotechnology , proteasome , chemistry , cytoplasm , ribonucleoprotein , ubiquitin , histone , repressor , anaphase , acetylation , rna , biochemistry , proteasome inhibitor , biology , gene , cell cycle , transcription factor

Novel INHAT Repressor (NIR) is a histone acetylation inhibitor that can directly bind histone complexes and the tumor suppressors p53 and p63. Because NIR is mainly localized in the nucleolus and disappears from the nucleolus upon RNase treatment, it is thought to bind RNA or ribonucleoproteins. When NIR moves to the cytoplasm, it is immediately degraded; this degradation was blocked by MG132, a proteasome inhibitor. Furthermore, the central domain of NIR specifically bound APC-CCdh1. These data show that the stability of NIR is governed by the ubiquitin/proteasome pathway

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