NDLI: Discovery of a novel ligand that modulates the protein–protein interactions of the AAA+ superfamily oncoprotein reptin

Content Provider	Royal Society of Chemistry (RSC)
Author	Huart, Anne-Sophie Blackburn, Elizabeth A. Houston, Douglas R. Muller, Petr Brychtova, Veronika Hupp, Ted R. Healy, Alan R. Krejci, Adam Vojtesek, Borek Remnant, Lucy Maslon, Magda M. Meers, Olivia Hernychova, Lenka Westwood, Nicholas J. Walkinshaw, Malcolm D.
Copyright Year	2015
Abstract	Developing approaches to discover protein–protein interactions (PPIs) remains a fundamental challenge. A chemical biology platform is applied here to identify novel PPIs for the AAA+ superfamily oncoprotein reptin. An in silico screen coupled with chemical optimization provided Liddean, a nucleotide-mimetic which modulates reptin's oligomerization status, protein-binding activity and global conformation. Combinatorial peptide phage library screening of Liddean-bound reptin with next generation sequencing identified interaction motifs including a novel reptin docking site on the p53 tumor suppressor protein. Proximity ligation assays demonstrated that endogenous reptin forms a predominantly cytoplasmic complex with its paralog pontin in cancer cells and Liddean promotes a shift of this complex to the nucleus. An emerging view of PPIs in higher eukaryotes is that they occur through a striking diversity of linear peptide motifs. The discovery of a compound that alters reptin's protein interaction landscape potentially leads to novel avenues for therapeutic development.
Starting Page	3109
Ending Page	3116
Page Count	8
File Format	HTM / HTML PDF
ISSN	20416520
Volume Number	6
Issue Number	5
Journal	Chemical Science
DOI	10.1039/c4sc03885a
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Subscribed
Subject Keyword	DNA ligase Liddean Homology (biology) Oncogene Bacteriophage Protein P53 Library Molecular biology Mathematical optimization Protein structure Peptide Cancer
Content Type	Text
Resource Type	Article
Subject	Chemistry

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