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

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)328-332
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume381
Issue number3
DOIs
Publication statusPublished - Apr 10 2009

Fingerprint

Cell membranes
Cysteine
Cell Membrane
Enzymes
Lipoylation
Mutagenesis
Phosphorylcholine
Sphingomyelins
Palmitic Acid
Ceramides
HEK293 Cells
Enzyme activity
Post Translational Protein Processing
Site-Directed Mutagenesis
Phosphatidylcholines
Alanine
Labeling
Mutation
phosphatidylcholine-ceramide phosphocholine transferase

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

Cite this

@article{a774c424e2b44339aa0be4e27f159e9d,
title = "Sphingomyelin synthase 2 is palmitoylated at the COOH-terminal tail, which is involved in its localization in plasma membranes",
abstract = "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.",
author = "Motohiro Tani and Osamu Kuge",
year = "2009",
month = "4",
day = "10",
doi = "10.1016/j.bbrc.2009.02.063",
language = "English",
volume = "381",
pages = "328--332",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "3",

}

TY - JOUR

T1 - Sphingomyelin synthase 2 is palmitoylated at the COOH-terminal tail, which is involved in its localization in plasma membranes

AU - Tani, Motohiro

AU - Kuge, Osamu

PY - 2009/4/10

Y1 - 2009/4/10

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=62049085281&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=62049085281&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2009.02.063

DO - 10.1016/j.bbrc.2009.02.063

M3 - Article

C2 - 19233134

AN - SCOPUS:62049085281

VL - 381

SP - 328

EP - 332

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

ER -