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. Author manuscript; available in PMC: 2015 Jan 1.
Published in final edited form as: Wiley Interdiscip Rev Syst Biol Med. 2013 Sep 30;6(1):13–36. doi: 10.1002/wsbm.1245

Table 1.

Description of interactions considered in figures.

Index Description
1 EGF binds EGFR201.
2 EGF-induced dimerization of EGFR via EGFR-EGFR interaction201
3 EGFR autophosphorylation at Y1016204
4 EGFR autophosphorylation at Y1092205
5 EGFR autophosphorylation at Y1110206
6 EGFR autophosphorylation at Y1172205
7 EGFR autophosphorylation at Y1197205
8 EGFR-mediated phosphorylation of Y317 in SHC1 (isoform p52Shc)207
9 EGFR-mediated phosphorylation of Y627 in GAB1208
10 EGFR-mediated phosphorylation of Y659 in GAB1208
11 PTPN11 binds pY1016 in EGFR209.
12 The SH2 domains in RASA1 mediate interaction with pY1016 in EGFR78, 210.
13 The SH2 domain in GRB2 binds pY1092 in EGFR121, 211, 212.
14 The SH2 domain in GRB2 binds pY1110 in EGFR121, 211, 212.
15 The PTB domain in SHC1 binds pY1172 in EGFR122, 212.
16 The PTB domain in SHC1 binds pY1197 in EGFR122, 212.
17 PTPN11-mediated dephosphorylation of pY1016 in EGFR210
18 The SH2 domain in GRB2 binds pY317 in SHC1 (isoform p52Shc)207.
19 The N-terminal SH2 domain in PTPN11 binds pY627 in GAB1213.
20 The C-terminal SH2 domain in PTPN11 binds pY659 in GAB1213.
21 PTPN11-mediated dephosphorylation of pY627 in GAB1213
22 PTPN11-mediated dephosphorylation of pY659 in GAB1213
23 The GAP domain in RASA1 binds KRAS causing an increase in GTPase activity that favors the GDP-loaded form of KRAS214.
24 The N-terminal SH3 domain in GRB2 interacts with several C-terminal proline-rich sequences (PRS) in SOS1215, 216.
25 The C-terminal SH3 domain in GRB2 interacts with two central proline-rich sequences (PRS) in GAB1217.
26 GTP-loaded KRAS binds the REM domain in SOS1, which increases the GEF activity of SOS1218, 219.
27 The GEF domain in SOS1 binds KRAS causing a release of guanine nucleotide that favors the GTP-loaded form of KRAS220.