Title : Estrogen receptor α/β-cofactor motif interactions; interplay of tyrosine 537/488 phosphorylation and LXXLL motifs.

Pub. Date : 2012 Oct 30

PMID : 22930062






1 Functional Relationships(s)
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1 These findings not only show regulation of the ERbeta-cofactor interaction via tyrosine phosphorylation, but also suggest that ERbeta and its tyrosine 488 phosphorylation play crucial roles in modulating interactions of coactivators to ERalpha since the natural Steroid Receptor Coactivators (SRCs) feature LXXLL motifs with acidic C-termini, while the repressor protein RIP140 features LXXLL motifs with basic C-termini. Tyrosine nuclear receptor interacting protein 1 Homo sapiens