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The chaperone heat shock protein 90 (Hsp90) participates in the endothelial store operated calcium entry heterocomplex
Author(s) -
Kadeba Pierre I,
Scammell Jonathan G,
Cioffi Donna L
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.724.4
Subject(s) - hsp90 , geldanamycin , heat shock protein , microbiology and biotechnology , fkbp , chaperone (clinical) , chemistry , calcium , biology , biochemistry , medicine , organic chemistry , pathology , gene
Heat shock protein 90 (Hsp90) is a molecular chaperone involved in protein complexes that participate in various cellular signaling events. FK506‐binding proteins (FKBPs) are regulators of store operated calcium (SOC) entry. The association of Hsp90 with FKBPs has been shown to be responsible for many of their effects. However, it is not known whether Hsp90 participates in FKBP action on SOC entry. Here we show that membrane‐cytoskeleton preparations of pulmonary endothelial cells resolve Hsp90 in plasma membrane fractions where the calcium‐selective Isoc subunits, TRPC1/4, are found. Hsp90 co‐immunoprecipitates with TRPC4. Endothelial cells treated with the Hsp90 inhibitor geldanamycin show decreased global SOC entry compared to untreated controls. Collectively, these data reveal the participation of Hsp90 in the endothelial SOC entry heterocomplex. Supported by 5R00HL089361.