Rapid Detection of p53 Acetylation Status in Response to Cellular Stress Signaling.
Publication/Presentation Date
1-1-2019
Abstract
The posttranslational lysine acetylation of proteins is increasingly appreciated as a key regulatory mechanism in fundamental cellular process such as transcription, cytoskeleton dynamics, metabolic flux, and cell survival/death signaling. As empirical studies are undertaken to dissect the functional importance of specific acetylation events, methods for rapid detection of this modification on individual proteins, in different cellular contexts, is essential. Much like nucleosomal histones, the tumor suppressor protein p53 is acetylated on a number of distinct lysine residues, often with distinct functional consequences. We discuss here a number of technical considerations that facilitate the use of protein-specific antibodies to interrogate these key acetylation events.
Volume
1983
First Page
255
Last Page
262
ISSN
1940-6029
Published In/Presented At
Farkas, M., & McMahon, S. B. (2019). Rapid Detection of p53 Acetylation Status in Response to Cellular Stress Signaling. Methods in molecular biology (Clifton, N.J.), 1983, 255–262. https://doi.org/10.1007/978-1-4939-9434-2_15
Disciplines
Business Administration, Management, and Operations | Health and Medical Administration | Management Sciences and Quantitative Methods
PubMedID
31087303
Department(s)
Administration and Leadership
Document Type
Article