Binding of SHC1 to p-5Y-EGFRvIII

Stable Identifier
R-HSA-5637766
Type
Reaction [binding]
Species
Homo sapiens
Compartment
cytosol, extracellular region, plasma membrane
ReviewStatus
5/5
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Binding of SHC1 to p-5Y-EGFRvIII
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SHC1 (Src homology 2 domain-containing transforming protein) is known to bind two phosphorylated tyrosine docking sites of EGFR: Y1148 and Y1173 (corresponding to Y1172 and Y1197 when counting from the first amino acid of EGFR precursor, before the cleavage of the 24-amino acid signal peptide at the N-terminus takes place). Phosphorylation of Y1173 tyrosine residue was directly demonstrated in EGFRvIII mutant (Han et al. 2006, Grandal et al. 2007) as well as the phosphorylation of Y1148 (Huang et al. 2007).
Binding of SHC1 to EGFRvIII cancer mutant has not been tested but SHC1 is assumed to bind EGFRvIII in the same way it binds wild-type EGFR.
Literature References
PubMed ID Title Journal Year
16969069 Hypophosphorylation of residue Y1045 leads to defective downregulation of EGFRvIII

Han, W, Zhang, T, Yu, H, Foulke, JG, Tang, CK

Cancer Biol Ther 2006
17372273 EGFRvIII escapes down-regulation due to impaired internalization and sorting to lysosomes

Grandal, MV, Zandi, R, Pedersen, MW, Willumsen, BM, van Deurs, B, Poulsen, HS

Carcinogenesis 2007
17646646 Quantitative analysis of EGFRvIII cellular signaling networks reveals a combinatorial therapeutic strategy for glioblastoma

Huang, PH, Mukasa, A, Bonavia, R, Flynn, RA, Brewer, ZE, Cavenee, WK, Furnari, FB, White, FM

Proc Natl Acad Sci U S A 2007
Participants
Input
Output
Participates
as an event of
Normal reaction
SHC1 binds to the phosphorylated EGF receptor:ligand complex (Homo sapiens)
Functional status

Gain of function of p-5Y-EGFRvIII mutant dimer [plasma membrane]

Normal Entity
Disease Entity
Status
Disease
Name Identifier Synonyms
cancer DOID:162 malignant tumor, malignant neoplasm, primary cancer
Cross References
Mondo
Authored
Orlic-Milacic, M  (2011-11-04)
Reviewed
Greulich, H  (2011-11-15)
Savas, S  (2011-11-15)
Created
Orlic-Milacic, M  (2014-11-13)
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