Spontaneous dimerization of ligand-responsive EGFR mutants

Stable Identifier
R-HSA-1220614
Type
Reaction [binding]
Species
Homo sapiens
Compartment
cytosol, plasma membrane
ReviewStatus
5/5
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Spontaneous dimerization of ligand-responsive EGFR mutants
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EGFR ligand-responsive mutants dimerize spontaneously, without ligand binding, although ligand binding ability is preserved. This was experimentally demonstrated for EFGR L858R mutant and is presumed to happen in other constitutively active EGFR kinase domain mutants and EGFR extracellular domain point mutants.
Literature References
PubMed ID Title Journal Year
16187797 Oncogenic transformation by inhibitor-sensitive and -resistant EGFR mutants

Feng, WL, Hahn, WC, Chen, TH, Meyerson, M, Frank, DA, Sellers, WR, Jänne, PA, Alvarez, JV, Greulich, H, Bulmer, SE, Zappaterra, M

PLoS Med 2005
17349580 Structures of lung cancer-derived EGFR mutants and inhibitor complexes: mechanism of activation and insights into differential inhibitor sensitivity

Li, Y, Meyerson, M, Woo, MS, Boggon, TJ, Greulich, H, Eck, MJ, Yun, CH

Cancer Cell 2007
19560417 The juxtamembrane region of the EGF receptor functions as an activation domain

Alvarado, D, Red Brewer, M, Pozzi, A, Choi, SH, Lemmon, MA, Moravcevic, K, Carpenter, G

Mol Cell 2009
16777603 An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor

Zhang, X, Kuriyan, J, Shen, K, Cole, PA, Gureasko, J

Cell 2006
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Functional status

Gain of function of Ligand-responsive EGFR mutants:HSP90:CDC37 [plasma membrane]

Normal Entity
Disease Entity
Status
Disease
Name Identifier Synonyms
cancer DOID:162 malignant tumor, malignant neoplasm, primary cancer
Authored
Orlic-Milacic, M  (2011-11-04)
Reviewed
Greulich, H  (2011-11-15)
Savas, S  (2011-11-15)
Created
Orlic-Milacic, M  (2011-02-23)
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