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CD82 — EGFR

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: CD82 — EGFR (physical association, affinity chromatography technology) Odintsova et al., Curr Biol 2000*
• IRef Hprd Interaction: CD82 — EGFR (in vitro) Odintsova et al., Curr Biol 2000*
• IRef Hprd Interaction: CD82 — EGFR (in vivo) Odintsova et al., Curr Biol 2000*
• IRef Ophid Interaction: CD82 — EGFR (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Odintsova et al., J Cell Sci 2003 : Expression of CD82 causes a significant increase in the amount of EGFR and ErbB2 in the light fractions of the sucrose gradient
Wang et al., Cancer Res 2007 (Carcinoma, Squamous Cell) : Suppression of epidermal growth factor receptor signaling by protein kinase C-alpha activation requires CD82 , caveolin-1, and ganglioside ... GM3- and CD82 induced inhibition of EGFR signaling requires PKC-alpha translocation and serine/threonine phosphorylation, which eventually triggers EGFR Thr654 phosphorylation and receptor internalization ... Within this ordered complex of signaling molecules, the ability of CD82 to associate with PKC-alpha requires the presence of caveolin-1, whereas the interaction of caveolin-1 or PKC-alpha with EGFR requires the presence of CD82 and ganglioside GM3
Danglot et al., J Cell Sci 2010 : Role of TI-VAMP and CD82 in EGFR cell-surface dynamics and signaling
Park et al., Biochem Pharmacol 2012 (Colonic Neoplasms) : An examination of the effect of sialylation on epidermal growth factor receptor (EGFR) activity and downstream signaling, which are highly correlated with cell proliferation, showed that the loss of ST6Gal-I augmented EGF induced EGFR phosphorylation and activation of extracellular signal regulated kinase ( ERK ) in colon cancer cells