Table 1.

Theraputic peptides targeting protiens required for EGFR retrograde trafficking

Name	Peptide mimetic	Mechanism of action	Reference
PMIP	MUC1 c-tail	EGFR-Muc1 binding	Bitler et al. [77]
GO-201	MUC1 c-tail	Binds Muc1 c-tail	Raina et al. [78]
GO-202	MUC1 c-tail	Binds Muc1 c-tail	Raina et al. [78]
GO-203	MUC1 c-tail	EGFR-Muc1 binding	Kharbanda et al. [79]
GO-203-NP	MUC1 c-tail nano particle	Increased cellular uptake of GO-203 peptide	Hasegawa et al. [82]
EJ-1	EGFR JXM domain	EGFR dimerization, nuclear localization, calmodulin binding, basolateral targeting, mitochondrial localization	Hart et al. [84]
SAH5	Hydrocarbon stapled EGFR JXM domain	EGFR dimerization, nuclear localization, calmodulin binding, basolateral targeting, mitochondrial localization	Maisel et al. [85]
cSNX1.3	SNX1 Bar domain	EGFR-SNX1 binding	Atwell et al. [86]

Peptides derived from MUC1 cytoplasmic tail, EGFR juxtamembrane (JXM) domain, and SNX1 have demonstrated anti-tumor effects in models of breast, prostate, glioblastoma, and lung cancer. PMIP, EGFR JXM-1 (EJ-1), stapled aromatic hydrocarbon EJ1-5 (SAH5), and cSNX1.3 have all been shown to directly inhibit the retrograde trafficking of EGFR. The GO peptides have been shown to inhibit the nuclear accumulation of MUC1 and inhibit the retrograde trafficking of EGFR