Sphingomyelin synthase 2 is palmitoylated at the COOH-terminal tail, which is involved in its localization in plasma membranes

研究成果: ジャーナルへの寄稿学術誌査読

28 被引用数 (Scopus)

抄録

Sphingomyelin synthase (SMS) is an enzyme that catalyzes the transfer of phosphocholine from phosphatidylcholine to ceramide for sphingomyelin synthesis. Here, we show that SMS2 is palmitoylated at cysteine residues via thioester bonds in the COOH-terminal cytoplasmic tail. [3H]palmitic acid labeling of SMS1 or SMS2-overexpressing HEK293 cells revealed that SMS2, but not SMS1, is palmitoylated. Site-directed mutagenesis of cysteine residues to alanine ones indicated that the COOH-terminal cysteine cluster of the enzyme is palmitoylated. Mutation of all potential palmitoylation sites resulted in a dramatic reduction in the plasma membrane distribution of SMS2, whereas it did not affect the in vitro enzyme activity. These results suggested that this posttranslational modification is important for determination of the subcellular localization of SMS2.

本文言語英語
ページ(範囲)328-332
ページ数5
ジャーナルBiochemical and Biophysical Research Communications
381
3
DOI
出版ステータス出版済み - 4月 10 2009

!!!All Science Journal Classification (ASJC) codes

  • 生化学
  • 生物理学
  • 細胞生物学
  • 分子生物学

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