10.1371/journal.pone.0139971.g006
Malgorzata Kluba
Malgorzata
Kluba
Yves Engelborghs
Yves
Engelborghs
Johan Hofkens
Johan
Hofkens
Hideaki Mizuno
Hideaki
Mizuno
Proposed mechanism of EGFR feedback monomerization upon EGF stimulation.
Public Library of Science
2015
EGFR dimer formation
receptor monomerization
monomeric state
feedback loop
pkd
epidermal growth factor receptor
protein kinase D
EGFR Signaling Dimerization
feedback mechanism
juxtamembrane threonine residues
raster image correlation spectroscopy
Signal transduction
dimerization state
oscillatory behavior
Receptor Dimerization
2.5 min
2015-10-14 04:12:03
Figure
https://plos.figshare.com/articles/figure/_Proposed_mechanism_of_EGFR_feedback_monomerization_upon_EGF_stimulation_/1575196
<p>After EGF challenging, two EGFR monomers associate on the plasma membrane to form an asymmetric dimer. The asymmetric dimer formation activates the kinase domain which transphosphorylates tyrosine residues at the C-termini of the receptor, three of which (pY1173, pY1148, pY992) recruit PLCγ1. EGFR phosphorylates PLCγ1 on Y783 for activation. PLCγ1 hydrolyses PIP<sub>2</sub> forming DAG. DAG activates nPKCs, which phosphorylates PKD at S744 and S748 for activation. PKD causes EGFR phosphorylation at T654 and/or T669 to shift the monomer-dimer equilibrium of liganded EGFR back towards the monomer. The insets show the close-up of the JM part. The two PDB files (2M20, 3GOP) were superimposed and aligned in the JM-A region to obtain presented images.</p>