English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Significance EGFR is a transmembrane cell-surface receptor tyrosine kinase crucial for regulating diverse physiological and pathological responses, but how protein function is turned on has remained elusive. Our results indicated that EGF stimulation recruits a key scaffold protein called TRAF4, which in turn recognizes the C-terminal half of the juxtamembrane segment of EGFR and promotes EGFR activation. Specific mutations in the TRAF4 binding site of EGFR resulted in significant attenuation of EGF-induced EGFR activation. These findings provide important insight into the mechanism of EGFR activation, and implicate TRAF4 as a potential therapeutic target for treating EGF/EGFR-driven cancers.

TRAF4 binds to the juxtamembrane region of EGFR directly and promotes kinase activation