Open AccessThe Deubiquitinating Enzyme USP14 Regulates Leukemic Chemotherapy Drugs-Induced Cell Apoptosis by Suppressing Ubiquitination of Aurora Kinase B
Author(s) -
Chunge Song,
Ruojin Ma,
Xiaoyu Yang,
Sulei Pang
Publication year - 2017
Publication title -
cellular physiology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.486
H-Index - 87
eISSN - 1421-9778
pISSN - 1015-8987
DOI - 10.1159/000478679
Subject(s) - aurora inhibitor , deubiquitinating enzyme , mitosis , apoptosis , aurora b kinase , jurkat cells , leukemia , cancer research , biology , ubiquitin , aurora a kinase , aurora kinase , microbiology and biotechnology , cytokinesis , cell , cell cycle , immunology , cell division , biochemistry , immune system , t cell , gene
Aurora kinase B is a mitotic checkpoint kinase that plays a pivotal role in mitosis by ensuring correct chromosome segregation and normal progression through mitosis. Aurora B has been found to be amplified and overexpressed in several types of leukemia. The deubiquitinating enzyme USP14 is one of three proteasome-associated deubiquitinating enzymes and plays critical roles in diverse biological processes including cancer. However, whether USP14 has a role in leukemia cells remains elusive.