scholarly journals Human Epidermal Growth Factor Receptor (EGFR) Aligned on the Plasma Membrane Adopts Key Features of Drosophila EGFR Asymmetry

2011 ◽  
Vol 31 (11) ◽  
pp. 2241-2252 ◽  
Author(s):  
C. J. Tynan ◽  
S. K. Roberts ◽  
D. J. Rolfe ◽  
D. T. Clarke ◽  
H. H. Loeffler ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Plasma Membrane ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Human Epidermal Growth Factor ◽  
Epidermal Growth ◽  
Key Features

scholarly journals O-GlcNAcylation of the human epidermal growth factor receptor

2015 ◽  
Vol 13 (30) ◽  
pp. 8196-8204 ◽  
Author(s):  
Silviya R. Stateva ◽  
Antonio Villalobo
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Plasma Membrane ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Protein Kinases ◽  
Protein Phosphatases ◽  
Growth Factor Receptor ◽  
Human Epidermal Growth Factor ◽  
Epidermal Growth ◽  
Acetylglucosamine Transferase

The cartoon represents the EGFR at the plasma membrane where serine/threonine residues could be subjected to phosphorylation/dephosphorylation events by protein kinases (PK) and phospho-protein phosphatases (PPP) and to O-GlcNAcylation/deGlcNAcylation events by O-linked β-N-acetylglucosamine transferase (OGT) and O-linked β-N-acetylglucosaminidase (OGA).

Human epidermal growth factor receptor (HER1) aligned on the plasma membrane adopts key features of Drosophila EGFR asymmetry

2012 ◽  
Vol 40 (1) ◽  
pp. 184-188 ◽  
Author(s):  
Marisa L. Martin-Fernandez
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Plasma Membrane ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Ligand Binding ◽  
Growth Factor Receptor ◽  
Structural Basis ◽  
Extracellular Region ◽  
Epidermal Growth ◽  
Key Features

Current models suggest that ligand-binding heterogeneity in HER1 [human EGFR (epidermal growth factor receptor] arises from negative co-operativity in signalling HER1 dimers, for which the asymmetry of the extracellular region of the Drosophila EGFR has recently provided a structural basis. However, no asymmetry is apparent in the current crystal structure of the isolated extracellular region of HER1. This receptor also differs from the Drosophila EGFR in that negative co-operativity is found only in full-length receptors in cells. Structural insights into HER1 in epithelial cells, derived from FLIM (fluorescence lifetime imaging microscopy) and two-dimensional FRET (Förster resonance energy transfer) combined with Monte Carlo and molecular dynamics simulations, have demonstrated a high-affinity ligand-binding HER1 conformation consistent with the extracellular region aligned flat on the plasma membrane. This conformation shares key features with that of the Drosophila EGFR, suggesting that the structural basis for negative co-operativity is conserved from invertebrates to humans, but that, in HER1, the extracellular region asymmetry requires interactions with the plasma membrane.

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