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MEMO1-ERα interaction may occur independent of Y537 phosphorylation which differs from MEMO1-ErbB2 binding
Paxton Mills1, Haley Salus1, Khanh Vu1
1Chemistry Department, University of Richmond, Richmond, VA USA.
Abstract:
MEMO1 is a protein implicated in cancer-associated signaling through interactions with other proteins, including estrogen receptor α (ERα). We used fluorescence polarization, molecular dynamics simulations, and protein pull-down assays to characterize the interaction between MEMO1 and ERα. MEMO1 bound to an ERα peptide containing phosphorylated Y537 but unexpectedly showed comparable affinity for the non-phosphorylated peptide. Computational modeling identified distinct binding modes and suggested contributions from MEMO1 residues. Pull-down experiments confirmed interaction between MEMO1 and the ERα ligand-binding domain. These findings suggest that MEMO1 interacts with ERα in a phosphorylation-independent manner, highlighting diverse binding modes that may support its scaffolding functions.
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