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ATP-binding cassette transporters and sterol O-acyltransferases interact at membrane microdomains to modulate sterol uptake and esterification.
Gulati, Sonia; Balderes, Dina; Kim, Christine; Guo, Zhongmin A; Wilcox, Lisa; Area-Gomez, Estela; Snider, Jamie; Wolinski, Heimo; Stagljar, Igor; Granato, Juliana T; Ruggles, Kelly V; DeGiorgis, Joseph A; Kohlwein, Sepp D; Schon, Eric A; Sturley, Stephen L.
Afiliación
  • Gulati S; *Institute of Human Nutrition, Department of Neurology, **Department of Genetics and Development, and Department of Pediatrics, Columbia University Medical Center, New York, New York, USA; Department of Biological Sciences and Department of Chemistry, Columbia University, New York, New York, USA; Do
  • Balderes D; *Institute of Human Nutrition, Department of Neurology, **Department of Genetics and Development, and Department of Pediatrics, Columbia University Medical Center, New York, New York, USA; Department of Biological Sciences and Department of Chemistry, Columbia University, New York, New York, USA; Do
  • Kim C; *Institute of Human Nutrition, Department of Neurology, **Department of Genetics and Development, and Department of Pediatrics, Columbia University Medical Center, New York, New York, USA; Department of Biological Sciences and Department of Chemistry, Columbia University, New York, New York, USA; Do
  • Guo ZA; *Institute of Human Nutrition, Department of Neurology, **Department of Genetics and Development, and Department of Pediatrics, Columbia University Medical Center, New York, New York, USA; Department of Biological Sciences and Department of Chemistry, Columbia University, New York, New York, USA; Do
  • Wilcox L; *Institute of Human Nutrition, Department of Neurology, **Department of Genetics and Development, and Department of Pediatrics, Columbia University Medical Center, New York, New York, USA; Department of Biological Sciences and Department of Chemistry, Columbia University, New York, New York, USA; Do
  • Area-Gomez E; *Institute of Human Nutrition, Department of Neurology, **Department of Genetics and Development, and Department of Pediatrics, Columbia University Medical Center, New York, New York, USA; Department of Biological Sciences and Department of Chemistry, Columbia University, New York, New York, USA; Do
  • Snider J; *Institute of Human Nutrition, Department of Neurology, **Department of Genetics and Development, and Department of Pediatrics, Columbia University Medical Center, New York, New York, USA; Department of Biological Sciences and Department of Chemistry, Columbia University, New York, New York, USA; Do
  • Wolinski H; *Institute of Human Nutrition, Department of Neurology, **Department of Genetics and Development, and Department of Pediatrics, Columbia University Medical Center, New York, New York, USA; Department of Biological Sciences and Department of Chemistry, Columbia University, New York, New York, USA; Do
  • Stagljar I; *Institute of Human Nutrition, Department of Neurology, **Department of Genetics and Development, and Department of Pediatrics, Columbia University Medical Center, New York, New York, USA; Department of Biological Sciences and Department of Chemistry, Columbia University, New York, New York, USA; Do
  • Granato JT; *Institute of Human Nutrition, Department of Neurology, **Department of Genetics and Development, and Department of Pediatrics, Columbia University Medical Center, New York, New York, USA; Department of Biological Sciences and Department of Chemistry, Columbia University, New York, New York, USA; Do
  • Ruggles KV; *Institute of Human Nutrition, Department of Neurology, **Department of Genetics and Development, and Department of Pediatrics, Columbia University Medical Center, New York, New York, USA; Department of Biological Sciences and Department of Chemistry, Columbia University, New York, New York, USA; Do
  • DeGiorgis JA; *Institute of Human Nutrition, Department of Neurology, **Department of Genetics and Development, and Department of Pediatrics, Columbia University Medical Center, New York, New York, USA; Department of Biological Sciences and Department of Chemistry, Columbia University, New York, New York, USA; Do
  • Kohlwein SD; *Institute of Human Nutrition, Department of Neurology, **Department of Genetics and Development, and Department of Pediatrics, Columbia University Medical Center, New York, New York, USA; Department of Biological Sciences and Department of Chemistry, Columbia University, New York, New York, USA; Do
  • Schon EA; *Institute of Human Nutrition, Department of Neurology, **Department of Genetics and Development, and Department of Pediatrics, Columbia University Medical Center, New York, New York, USA; Department of Biological Sciences and Department of Chemistry, Columbia University, New York, New York, USA; Do
  • Sturley SL; *Institute of Human Nutrition, Department of Neurology, **Department of Genetics and Development, and Department of Pediatrics, Columbia University Medical Center, New York, New York, USA; Department of Biological Sciences and Department of Chemistry, Columbia University, New York, New York, USA; Do
FASEB J ; 29(11): 4682-94, 2015 Nov.
Article en En | MEDLINE | ID: mdl-26220175
ABSTRACT
A key component of eukaryotic lipid homeostasis is the esterification of sterols with fatty acids by sterol O-acyltransferases (SOATs). The esterification reactions are allosterically activated by their sterol substrates, the majority of which accumulate at the plasma membrane. We demonstrate that in yeast, sterol transport from the plasma membrane to the site of esterification is associated with the physical interaction of the major SOAT, acyl-coenzyme Acholesterol acyltransferase (ACAT)-related enzyme (Are)2p, with 2 plasma membrane ATP-binding cassette (ABC) transporters Aus1p and Pdr11p. Are2p, Aus1p, and Pdr11p, unlike the minor acyltransferase, Are1p, colocalize to sterol and sphingolipid-enriched, detergent-resistant microdomains (DRMs). Deletion of either ABC transporter results in Are2p relocalization to detergent-soluble membrane domains and a significant decrease (53-36%) in esterification of exogenous sterol. Similarly, in murine tissues, the SOAT1/Acat1 enzyme and activity localize to DRMs. This subcellular localization is diminished upon deletion of murine ABC transporters, such as Abcg1, which itself is DRM associated. We propose that the close proximity of sterol esterification and transport proteins to each other combined with their residence in lipid-enriched membrane microdomains facilitates rapid, high-capacity sterol transport and esterification, obviating any requirement for soluble intermediary proteins.
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Esteroles / Esterol O-Aciltransferasa / Transportadoras de Casetes de Unión a ATP / Microdominios de Membrana / Proteínas de Saccharomyces cerevisiae Límite: Animals Idioma: En Revista: FASEB J Asunto de la revista: BIOLOGIA / FISIOLOGIA Año: 2015 Tipo del documento: Article
Texto completo
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Esteroles / Esterol O-Aciltransferasa / Transportadoras de Casetes de Unión a ATP / Microdominios de Membrana / Proteínas de Saccharomyces cerevisiae Límite: Animals Idioma: En Revista: FASEB J Asunto de la revista: BIOLOGIA / FISIOLOGIA Año: 2015 Tipo del documento: Article