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Nuclear protein isoforms: Implications for cancer diagnosis and therapy
Author(s) -
Shen Fei,
Kirmani Kashif Z.,
Xiao Zhimin,
Thirlby Benjamin H.,
Hickey Robert J.,
Malkas Linda H.
Publication year - 2011
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.23002
Subject(s) - sumo protein , nuclear protein , gene isoform , histone , acetylation , proliferating cell nuclear antigen , biology , signal transduction , nuclear localization sequence , transcription factor , nuclear export signal , nuclear transport , microbiology and biotechnology , retinoblastoma , epigenetics , methylation , cancer research , cell nucleus , ubiquitin , gene , cell growth , genetics
Post‐translational modifications (PTMs) of nuclear proteins play essential roles in the regulation of gene transcription and signal transduction pathways. Numerous studies have demonstrated a correlation between specific nuclear protein isoforms and cellular malignant process. This communication reviews the impact of major PTM events such as phosphorylation, acetylation, methylation, ubiquitination, and sumoylation on several important nuclear proteins including p53, histones, proliferating cellular nuclear antigen (PCNA), and retinoblastoma protein (Rb) in the process. In addition, the implications of the PTMs as cancer biomarkers and therapeutic targets are considered. J. Cell. Biochem. 112: 756–760, 2011. © 2010 Wiley‐Liss, Inc.