The Epidermal Growth Factor Receptor Forms Location-Dependent Complexes in Resting Cells.

ABSTRACT: The epidermal growth factor receptor (EGFR) is a prototypical receptor tyrosine kinase involved in cell growth and proliferation and associated with various cancers. It is commonly assumed that after activation by binding of epidermal growth factor to the extracellular domain it dimerizes, followed by autophosphorylation of tyrosine residues at the intracellular domain. However, its oligomerization state before activation is controversial. In the absence of ligands, EGFR has been found in various, inconsistent amounts of monomeric, inactive dimeric, and oligomeric forms. In addition, evidence suggests that the active conformation is not a simple dimer but contains higher oligomers. As experiments in the past have been conducted at different conditions, we investigate here the influence of

SUBMITTER: Yavas S 

PROVIDER: S-EPMC5112932 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature