USP2-45 Represses Aldosterone Mediated Responses by Decreasing Mineralocorticoid Receptor Availability | Zendy

Nourdine Faresse | Zendy; Anne Debonneville | Zendy; Olivier Staub | Zendy

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USP2-45 Represses Aldosterone Mediated Responses by Decreasing Mineralocorticoid Receptor Availability

Author(s) -

Nourdine Faresse,

Anne Debonneville,

Olivier Staub

Publication year - 2013

Publication title -

cellular physiology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.486

H-Index - 87

eISSN - 1421-9778

pISSN - 1015-8987

DOI - 10.1159/000343382

Subject(s) - mineralocorticoid receptor , ubiquitin , aldosterone , tsg101 , receptor , immunoprecipitation , hek 293 cells , chemistry , downregulation and upregulation , transfection , proteasome , microbiology and biotechnology , cancer research , medicine , endocrinology , biology , biochemistry , gene , microrna , microvesicles

Ligand activation of the mineralocorticoid receptor (MR) induces several post-translational modifications (PTMs). Among the different PTMs, MR is known to be dynamically ubiquitylated with impact on its stability and transcriptional activity. Previously, we have shown that MR is monoubiquitylated at the basal state and that aldosterone stimulation induces monoubiquitylation removal prompting polyubiquitin-dependent destabilization of the receptor and proteasomal degradation. This study investigated the role of the aldosterone induced ubiquitin-specific protease USP2-45 on the ubiquitylation state of MR.

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