Effects of N361 Glycosylation on Epidermal Growth Factor Receptor Biological Function.

ABSTRACT:

Background

Epidermal growth factor receptor (EGFR) is a transmembrane tyrosine kinase that is frequently post-translationally modified by glycosylation. In cancer, EGFR amplifications and hotspot mutations such as L858R that promote proliferation have been detected in a significant fraction of non-small cell lung carcinomas and breast adenocarcinomas. Analyses of disruptions to glycosylation pathways in cancer cells identified EGFR glycosylation at residue N361 as one of the most heavily impacted sites.

Methods

We stably expressed a glycosylation-deficient mutant EGFR, N361A, with or without the oncogenic EGFR mutation L858R in cells. Proximity ligation assays were employed to study the effects of the glycosylation mutant on the co-localization of EGFR and HER2. The effects

SUBMITTER: Lam D 

PROVIDER: S-EPMC12896819 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature