| http://purl.uniprot.org/citations/17050526 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17050526 | http://www.w3.org/2000/01/rdf-schema#comment | "Transport of cholesterol into the mitochondria is the rate-determining, hormone-sensitive step in steroid biosynthesis. Here we report that the mechanism underlying mitochondrial cholesterol transport involves the formation of a macromolecular signaling complex composed of the outer mitochondrial membrane translocator protein (TSPO), previously known as peripheral-type benzodiazepine receptor; the TSPO-associated protein PAP7, which binds and brings to mitochondria the regulatory subunit RIalpha of the cAMP-dependent protein kinase (PKARIalpha); and the hormone-induced PKA substrate, steroidogenic acute regulatory protein (StAR). Hormone treatment of MA-10 Leydig cells induced the co-localization of TSPO, PAP7, PKARIalpha, and StAR in mitochondria, visualized by confocal microscopy, and the formation in living cells of a high molecular weight multimeric complex identified using photoactivable amino acids. The hormone-induced recruitment of exogenous TSPO in this complex was found to parallel the increased presence of 7-azi-5alpha-cholestan-3beta-ol in the samples. Co-expression of Tspo, Pap7, PkarIalpha, and Star genes resulted in the stimulation of steroid formation in both steroidogenic MA-10 and non-steroidogenic COS-F2-130 cells that were engineered to metabolize cholesterol. Disruption of these protein-protein interactions and specifically the PKARIalpha-PAP7 and PAP7-TSPO interactions, using PAP7 mutants where the N0 area homologous to dual A-kinase-anchoring protein-1 or the acyl-CoA signature motif were deleted or using the peptide Ht31 known to disrupt the anchoring of PKA, inhibited both basal and hormone-induced steroidogenesis. These results suggest that the initiation of cAMP-induced protein-protein interactions results in the formation of a multivalent scaffold in the outer mitochondrial membrane that mediates the effect of hormones on mitochondrial cholesterol transport and steroidogenesis."xsd:string |
| http://purl.uniprot.org/citations/17050526 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m608820200"xsd:string |
| http://purl.uniprot.org/citations/17050526 | http://purl.uniprot.org/core/author | "Liu J."xsd:string |
| http://purl.uniprot.org/citations/17050526 | http://purl.uniprot.org/core/author | "Papadopoulos V."xsd:string |
| http://purl.uniprot.org/citations/17050526 | http://purl.uniprot.org/core/author | "Rone M.B."xsd:string |
| http://purl.uniprot.org/citations/17050526 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/17050526 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/17050526 | http://purl.uniprot.org/core/pages | "38879-38893"xsd:string |
| http://purl.uniprot.org/citations/17050526 | http://purl.uniprot.org/core/title | "Protein-protein interactions mediate mitochondrial cholesterol transport and steroid biosynthesis."xsd:string |
| http://purl.uniprot.org/citations/17050526 | http://purl.uniprot.org/core/volume | "281"xsd:string |
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