StAR Protein Stability in Y1 and Kin-8 Mouse Adrenocortical Cells

Biology
Barbara J Clark, Elizabeth A Hudson

Abstract

The steroidogenic acute regulatory protein (STAR) protein expression is required for cholesterol transport into mitochondria to initiate steroidogenesis in the adrenal and gonads. STAR is synthesized as a 37 kDa precursor protein which is targeted to the mitochondria and imported and processed to an intra-mitochondrial 30 kDa protein. Tropic hormone stimulation of the cAMP-dependent protein kinase A (PKA) signaling pathway is the major contributor to the transcriptional and post-transcriptional regulation of STAR synthesis. Many studies have focused on the mechanisms of cAMP-PKA mediated control of STAR synthesis while there are few reports on STAR degradation pathways. The objective of this study was to determine the effect of cAMP-PKA-dependent signaling on STAR protein stability. We have used the cAMP-PKA responsive Y1 mouse adrenocortical cells and the PKA-deficient Kin-8 cells to measure STAR phosphorylation and protein half-life. Western blot analysis and standard radiolabeled pulse-chase experiments were used to determine STAR phosphorylation status and protein half-life, respectively. Our data demonstrate that PKA-dependent STAR phosphorylation does not contribute to 30 kDa STAR protein stability in the mitochondria. We...Continue Reading

References

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May 23, 2014·Molecular Endocrinology·Goro SasakiRichard J Auchus

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Citations

Dec 22, 2016·Frontiers in Neuroscience·Barbara J Clark
Jan 14, 2020·Molecular and Cellular Endocrinology·Barbara J Clark

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Methods Mentioned

BETA
Immunoprecipitation

Software Mentioned

GraphPad
Un
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ImageQuant
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