Sign on

SAO/NASA ADS General Science Abstract Service

· Find Similar Abstracts (with default settings below)
· Electronic Refereed Journal Article (HTML)
· References in the article
· Citations to the Article (6) (Citation History)
· Refereed Citations to the Article
· Also-Read Articles (Reads History)
·
· Translate This Page
Title:
A quantitative protein interaction network for the ErbB receptors using protein microarrays
Authors:
Jones, Richard B.; Gordus, Andrew; Krall, Jordan A.; MacBeath, Gavin
Affiliation:
AA(Department of Chemistry and Chemical Biology, and), AB(Department of Chemistry and Chemical Biology, and), AC(Department of Chemistry and Chemical Biology, and), AD(Department of Chemistry and Chemical Biology, and)
Publication:
Nature, Volume 439, Issue 7073, pp. 168-174 (2006). (Nature Homepage)
Publication Date:
01/2006
Origin:
NATURE
Abstract Copyright:
(c) 2006: Nature
DOI:
10.1038/nature04177
Bibliographic Code:
2006Natur.439..168J

Abstract

Although epidermal growth factor receptor (EGFR; also called ErbB1) and its relatives initiate one of the most well-studied signalling networks, there is not yet a genome-wide view of even the earliest step in this pathway: recruitment of proteins to the activated receptors. Here we use protein microarrays comprising virtually every Src homology 2 (SH2) and phosphotyrosine binding (PTB) domain encoded in the human genome to measure the equilibrium dissociation constant of each domain for 61 peptides representing physiological sites of tyrosine phosphorylation on the four ErbB receptors. This involved 77,592 independent biochemical measurements and provided a quantitative protein interaction network that reveals many new interactions, including ones that fall outside of our current view of domain selectivity. By slicing through the network at different affinity thresholds, we found surprising differences between the receptors. Most notably, EGFR and ErbB2 become markedly more promiscuous as the threshold is lowered, whereas ErbB3 does not. Because EGFR and ErbB2 are overexpressed in many human cancers, our results suggest that the extent to which promiscuity changes with protein concentration may contribute to the oncogenic potential of receptor tyrosine kinases, and perhaps other signalling proteins as well.
Bibtex entry for this abstract   Preferred format for this abstract (see Preferences)
   

Find Similar Abstracts:

Use: Authors
Title
Abstract Text
Return: Query Results Return    items starting with number
Query Form
Database: Astronomy
Physics
arXiv e-prints