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Identification of three distinct calmodulin‐binding domains in the G Protein‐coupled Estrogen Receptor
Author(s) -
TRAN KIM,
VerMeer Mark
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.lb548
Subject(s) - gper , calmodulin , g protein coupled receptor , estrogen receptor , receptor , chemistry , microbiology and biotechnology , biochemistry , biology , genetics , cancer , breast cancer , enzyme
The novel G protein‐coupled estrogen receptor (GPER/GPR30) is being increasingly identified as an important GPCR in many organ system. Calmodulin (CaM) is a ubiquitous Ca 2+ transducer that is required for the activities of numerous cellular proteins. Here we show that CaM coimmunoprecipitates with GPER in primary vascular endothelial cells upon stimulation with 17β‐estradiol or Ca 2+ ‐elevating ionophore. To identify the CaM‐binding sites in GPER/GPR30, we have developed a series of novel FRET‐based biosensors whose responses allow identification and highly quantitative characterization of CaM‐binding properties of CaM‐binding domains in GPER/GPR30. Three separate CaM‐binding domains with distinct dissociation constants and Ca 2+ sensitivities for complex formation with CaM were found. The functional implications of CaM‐GPER interactions are explored.