Work

Regulation of p53 function by lysine methylation

Year: 2011

Type: article

Abstract: The reversible and dynamic methylation of proteins on lysine residues can greatly increase the signaling potential of the modified factor. In addition to histones, several other nuclear factors such as the tumor suppressor and transcription factor p53 undergo lysine methylation, suggesting that this modification may be a common mechanism for modulating protein–protein interactions and key cellular signaling pathways. This article focuses on how lysine methylation events on the C-terminal tail of p53 are generated, sensed and transduced to modulate p53 functions.

Source: Epigenomics

DOI: 10.2217/epi.11.21

Authors: Lisandra E West, Or Gozani

Institution: Stanford University

Language: English

Topic: Cancer-related gene regulation

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Institute of General Medical Sciences

Award: Function of PHD Domain Proteins in Chromatin Regulation