The phosphatase calcineurin PP2BAβ mediates part of mineralocorticoid receptor transcriptional activity

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
Anja SeiferthClaudia Grossmann

Abstract

Recently it was shown that the mineralocorticoid receptor (MR) may exert part of its transcriptional activity by mediation of calcineurin (PP2B). Here we investigated the mechanism of interaction of MR with calcineurin and provide a new MR signaling pathway with potential physiological and pathophysiological relevance. MR → calcineurin crosstalk was assessed in a heterologous expression system (human embryonic kidney cells), which provides the opportunity for detailed mechanistic investigation. SiRNA knockdown experiments show that activated MR, but not GR, reduces CREB- and enhances NFaT-mediated transcriptional activation via the catalytic calcineurin subunit PP2BAβ but not via PP2BAα. Altered PP2BAβ expression, elevated cytosolic Ca(2+), activation of mitogen-activated kinase [p38, extracellular signal-regulated kinase (ERK) 1/2], or protein kinase C do not seem to be involved, whereas inhibition of the chaperone heat-shock protein 90 (HSP90) abrogated the effect of MR. Coimmunoprecipitation indicates the existence of protein complexes harboring MR and PP2BAβ independent of MR activation but dependent on HSP90. Activated MR alters the subcellular distribution of PP2BAβ, enhancing its nuclear fraction, and reduces mRNA expres...Continue Reading

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Citations

Jul 4, 2012·Free Radical Biology & Medicine·Stefanie RuhsClaudia Grossmann
Mar 20, 2012·American Journal of Physiology. Heart and Circulatory Physiology·J S SchulteF U Müller
Nov 12, 2017·Scientific Reports·Stefanie RuhsClaudia Grossmann

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