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A peroxisome biogenesis deficiency prevents the binding of alpha-synuclein to lipid droplets in lipid-loaded yeast.

ABSTRACT: Using a yeast model of Parkinson's disease, we found that alpha-synuclein (?S) binds to lipid droplets in lipid-loaded, wild-type yeast cells but not to lipid droplets in lipid-loaded, peroxisome-deficient cells (pex3?). Our analysis revealed that pex3? cells have both fewer lipid droplets and smaller lipid droplets than wild-type cells, and that the acyl chains of the phospholipids on the surface of the lipid droplets from pex3? cells are on average shorter (C16) than those (C18) on the surface of lipid droplets from wild-type cells. We propose that the shift to shorter (C18?C16) acyl chains contributes to the reduced binding of ?S to lipid droplets in pex3? cells.

SUBMITTER: Wang S

PROVIDER: S-EPMC3770730 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature

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A peroxisome biogenesis deficiency prevents the binding of alpha-synuclein to lipid droplets in lipid-loaded yeast.

Wang Shaoxiao S Horn Patrick J PJ Liou Liang-Chun LC Muggeridge Martin I MI Zhang Zhaojie Z Chapman Kent D KD Witt Stephan N SN

Biochemical and biophysical research communications 20130731 2

Using a yeast model of Parkinson's disease, we found that alpha-synuclein (αS) binds to lipid droplets in lipid-loaded, wild-type yeast cells but not to lipid droplets in lipid-loaded, peroxisome-deficient cells (pex3Δ). Our analysis revealed that pex3Δ cells have both fewer lipid droplets and smaller lipid droplets than wild-type cells, and that the acyl chains of the phospholipids on the surface of the lipid droplets from pex3Δ cells are on average shorter (C16) than those (C18) on the surface ...[more]

PMID: 23916615

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