Replacement of a labile aspartyl residue increases the stability of human epidermal growth factor

Biochemistry ◽  
1990 ◽  
Vol 29 (41) ◽  
pp. 9584-9591 ◽  
Author(s):  
Carlos George-Nascimento ◽  
Jonathan Lowenson ◽  
Michael Borissenko ◽  
Maria Calderon ◽  
Angelica Medina-Selby ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Human Epidermal Growth Factor ◽  
Epidermal Growth ◽  
The Stability ◽  
Aspartyl Residue

Effect of excipients on the stability and transport of recombinant human epidermal growth factor (rhEGF) across CACO-2 cell monolayers

2003 ◽  
Vol 26 (4) ◽  
pp. 330-337 ◽  
Author(s):  
In-Wha Kim ◽  
Ho-Jung Yoo ◽  
Im-Sook Song ◽  
Youn-Bok Chung ◽  
Dong-Cheul Moon ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Cell Monolayers ◽  
Human Epidermal Growth Factor ◽  
Epidermal Growth ◽  
The Stability

scholarly journals EGFR forms ligand-independent oligomers that are distinct from the active state

2020 ◽  
Vol 295 (38) ◽  
pp. 13353-13362 ◽  
Author(s):  
Patrick O. Byrne ◽  
Kalina Hristova ◽  
Daniel J. Leahy
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Fluorescent Protein ◽  
Growth Factor Receptor ◽  
Physiological Role ◽  
Active State ◽  
Human Epidermal Growth Factor ◽  
Epidermal Growth ◽  
The Stability

The human epidermal growth factor receptor (EGFR/ERBB1) is a receptor tyrosine kinase (RTK) that forms activated oligomers in response to ligand. Much evidence indicates that EGFR/ERBB1 also forms oligomers in the absence of ligand, but the structure and physiological role of these ligand-independent oligomers remain unclear. To examine these features, we use fluorescence microscopy to measure the oligomer stability and FRET efficiency for homo- and hetero-oligomers of fluorescent protein-labeled forms of EGFR and its paralog, human epidermal growth factor receptor 2 (HER2/ERBB2) in vesicles derived from mammalian cell membranes. We observe that both receptors form ligand-independent oligomers at physiological plasma membrane concentrations. Mutations introduced in the kinase region at the active state asymmetric kinase dimer interface do not affect the stability of ligand-independent EGFR oligomers. These results indicate that ligand-independent EGFR oligomers form using interactions that are distinct from the EGFR active state.

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