StarD5: an ER stress protein regulates plasma membrane and intracellular cholesterol homeostasis.


Journal

Journal of lipid research
ISSN: 1539-7262
Titre abrégé: J Lipid Res
Pays: United States
ID NLM: 0376606

Informations de publication

Date de publication:
06 2019
Historique:
received: 20 12 2018
revised: 08 04 2019
pubmed: 25 4 2019
medline: 14 7 2020
entrez: 25 4 2019
Statut: ppublish

Résumé

How plasma membrane (PM) cholesterol is controlled is poorly understood. Ablation of the gene encoding the ER stress steroidogenic acute regulatory-related lipid transfer domain (StarD)5 leads to a decrease in PM cholesterol content, a decrease in cholesterol efflux, and an increase in intracellular neutral lipid accumulation in macrophages, the major cell type that expresses StarD5. ER stress increases StarD5 expression in mouse hepatocytes, which results in an increase in accessible PM cholesterol in WT but not in StarD5

Identifiants

pubmed: 31015253
pii: S0022-2275(20)32249-5
doi: 10.1194/jlr.M091967
pmc: PMC6547630
doi:

Substances chimiques

Adaptor Proteins, Vesicular Transport 0
RNA, Messenger 0
Stard5 protein, mouse 0
Triglycerides 0
Cholesterol 97C5T2UQ7J

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

1087-1098

Subventions

Organisme : NCATS NIH HHS
ID : UL1 TR002649
Pays : United States
Organisme : NCATS NIH HHS
ID : UL1 TR000058
Pays : United States
Organisme : NIGMS NIH HHS
ID : P50 GM076516
Pays : United States
Organisme : BLRD VA
ID : I01 BX000197
Pays : United States
Organisme : NIGMS NIH HHS
ID : P41 GM103540
Pays : United States
Organisme : NCI NIH HHS
ID : P30 CA016059
Pays : United States

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Auteurs

Daniel Rodriguez-Agudo (D)

Departments of Medicine, Virginia Commonwealth University School of Medicine, Richmond, VA 23298.
McGuire Veterans Affairs Medical Center, Richmond, VA 23248.

Leonel Malacrida (L)

Laboratory for Fluorescence Dynamics, Department of Biomedical Engineering, University of California at Irvine, Irvine, CA 92697.
Area de Investigación Respiratoria, Departamento de Fisiopatologia, Hospital de Clinicas, Facultad de Medicina, Universidad de la Republica, Montevideo, Uruguay.

Genta Kakiyama (G)

Departments of Medicine, Virginia Commonwealth University School of Medicine, Richmond, VA 23298.
McGuire Veterans Affairs Medical Center, Richmond, VA 23248.

Tavis Sparrer (T)

Biochemistry and Molecular Biology, Virginia Commonwealth University School of Medicine, Richmond, VA 23298.

Carolina Fortes (C)

Departments of Medicine, Virginia Commonwealth University School of Medicine, Richmond, VA 23298.
Departmento de Biologia Molecular y Bioquimica, Universidad de Malaga, Malaga, Spain.

Michael Maceyka (M)

Biochemistry and Molecular Biology, Virginia Commonwealth University School of Medicine, Richmond, VA 23298.
Massey Cancer Center, Virginia Commonwealth University School of Medicine, Richmond, VA 23298.

Mark A Subler (MA)

Human and Molecular Genetics, Virginia Commonwealth University School of Medicine, Richmond, VA 23298.

Jolene J Windle (JJ)

Massey Cancer Center, Virginia Commonwealth University School of Medicine, Richmond, VA 23298.
Human and Molecular Genetics, Virginia Commonwealth University School of Medicine, Richmond, VA 23298.

Enrico Gratton (E)

Laboratory for Fluorescence Dynamics, Department of Biomedical Engineering, University of California at Irvine, Irvine, CA 92697.

William M Pandak (WM)

Departments of Medicine, Virginia Commonwealth University School of Medicine, Richmond, VA 23298 gregorio.gil@vcuhealth.org William.pandakjr@vcuhealth.org.
McGuire Veterans Affairs Medical Center, Richmond, VA 23248.

Gregorio Gil (G)

Biochemistry and Molecular Biology, Virginia Commonwealth University School of Medicine, Richmond, VA 23298 gregorio.gil@vcuhealth.org William.pandakjr@vcuhealth.org.
Massey Cancer Center, Virginia Commonwealth University School of Medicine, Richmond, VA 23298.

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Classifications MeSH