Loss of hydroxyl groups from the ceramide moiety can modify the lateral diffusion of membrane proteins in S. cerevisiae

Satoshi Uemura, Fumi Shishido, Motohiro Tani, Takahiro Mochizuki, Fumiyoshi Abe, Jin Ichi Inokuchi

研究成果: ジャーナルへの寄稿記事

12 引用 (Scopus)

抄録

In the yeast Saccharomyces cerevisiae , structural diversities of complex sphingolipids [inositol phosphorylceramide (IPC), mannosylinositol phosphorylceramide, and mannosyldiinositol phosphorylceramide] are often observed in the presence or absence of hydroxyl groups on the C-4 position of long-chain base (C4-OH) and the C-2 position of very long-chain fatty acids (C2-OH), but the biological signifi - cance of these groups remains unclear. Here, we evaluated cellular membrane fl uidity in hydroxyl group-defective yeast mutants by fl uorescence recovery after photobleaching. The lateral diffusion of enhanced green fl uorescent proteintagged hexose transporter 1 (Hxt1-EGFP) was infl uenced by the absence of C4-OH and/or C2-OH. Notably, the fl uorescence recovery of Hxt1-EGFP was dramatically decreased in the sur2 - mutant (absence of C4-OH) under the csg1 - csh1 - background, in which mannosylation of IPC is blocked leading to IPC accumulation, while the recovery in the scs7 - mutant (absence of C2-OH) under the same background was modestly decreased. In addition, the amount of low affi nity tryptophan transporter 1 (Tat1)-EGFP was markedly decreased in the sur2 - csg1 - csh1 - mutant and accumulated in intracellular membranes in the scs7 - csg1 - csh1 - mutant without altering its protein expression. These results suggest that C4-OH and C2-OH are most probably critical factors for maintaining membrane fl uidity and proper turnover of membrane molecules in yeast containing complex sphingolipids with only one hydrophilic head group. -Uemura, S., F. Shishido, M. Tani, T. Mochizuki, F. Abe, and J-i. Inokuchi. Loss of hydroxyl groups from the ceramide moiety can modify the lateral diffusion of membrane proteins in S. cerevisiae . J. Lipid Res. 2014. 55: 1343 - 1356 .

元の言語英語
ページ(範囲)1343-1356
ページ数14
ジャーナルJournal of Lipid Research
55
発行部数7
DOI
出版物ステータス出版済み - 1 1 2014

Fingerprint

Ceramides
Protein S
Inositol
Hydroxyl Radical
Yeast
Saccharomyces cerevisiae
Membrane Proteins
Sphingolipids
Yeasts
Membranes
Monosaccharide Transport Proteins
Photobleaching
Intracellular Membranes
Recovery
Tryptophan
Fatty Acids
Lipids
Proteins
Molecules

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Endocrinology
  • Cell Biology

これを引用

Loss of hydroxyl groups from the ceramide moiety can modify the lateral diffusion of membrane proteins in S. cerevisiae. / Uemura, Satoshi; Shishido, Fumi; Tani, Motohiro; Mochizuki, Takahiro; Abe, Fumiyoshi; Inokuchi, Jin Ichi.

:: Journal of Lipid Research, 巻 55, 番号 7, 01.01.2014, p. 1343-1356.

研究成果: ジャーナルへの寄稿記事

Uemura, Satoshi ; Shishido, Fumi ; Tani, Motohiro ; Mochizuki, Takahiro ; Abe, Fumiyoshi ; Inokuchi, Jin Ichi. / Loss of hydroxyl groups from the ceramide moiety can modify the lateral diffusion of membrane proteins in S. cerevisiae. :: Journal of Lipid Research. 2014 ; 巻 55, 番号 7. pp. 1343-1356.
@article{fb3d70e454a541dfa51ef1918fbf49f6,
title = "Loss of hydroxyl groups from the ceramide moiety can modify the lateral diffusion of membrane proteins in S. cerevisiae",
abstract = "In the yeast Saccharomyces cerevisiae , structural diversities of complex sphingolipids [inositol phosphorylceramide (IPC), mannosylinositol phosphorylceramide, and mannosyldiinositol phosphorylceramide] are often observed in the presence or absence of hydroxyl groups on the C-4 position of long-chain base (C4-OH) and the C-2 position of very long-chain fatty acids (C2-OH), but the biological signifi - cance of these groups remains unclear. Here, we evaluated cellular membrane fl uidity in hydroxyl group-defective yeast mutants by fl uorescence recovery after photobleaching. The lateral diffusion of enhanced green fl uorescent proteintagged hexose transporter 1 (Hxt1-EGFP) was infl uenced by the absence of C4-OH and/or C2-OH. Notably, the fl uorescence recovery of Hxt1-EGFP was dramatically decreased in the sur2 - mutant (absence of C4-OH) under the csg1 - csh1 - background, in which mannosylation of IPC is blocked leading to IPC accumulation, while the recovery in the scs7 - mutant (absence of C2-OH) under the same background was modestly decreased. In addition, the amount of low affi nity tryptophan transporter 1 (Tat1)-EGFP was markedly decreased in the sur2 - csg1 - csh1 - mutant and accumulated in intracellular membranes in the scs7 - csg1 - csh1 - mutant without altering its protein expression. These results suggest that C4-OH and C2-OH are most probably critical factors for maintaining membrane fl uidity and proper turnover of membrane molecules in yeast containing complex sphingolipids with only one hydrophilic head group. -Uemura, S., F. Shishido, M. Tani, T. Mochizuki, F. Abe, and J-i. Inokuchi. Loss of hydroxyl groups from the ceramide moiety can modify the lateral diffusion of membrane proteins in S. cerevisiae . J. Lipid Res. 2014. 55: 1343 - 1356 .",
author = "Satoshi Uemura and Fumi Shishido and Motohiro Tani and Takahiro Mochizuki and Fumiyoshi Abe and Inokuchi, {Jin Ichi}",
year = "2014",
month = "1",
day = "1",
doi = "10.1194/jlr.M048637",
language = "English",
volume = "55",
pages = "1343--1356",
journal = "Journal of Lipid Research",
issn = "0022-2275",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "7",

}

TY - JOUR

T1 - Loss of hydroxyl groups from the ceramide moiety can modify the lateral diffusion of membrane proteins in S. cerevisiae

AU - Uemura, Satoshi

AU - Shishido, Fumi

AU - Tani, Motohiro

AU - Mochizuki, Takahiro

AU - Abe, Fumiyoshi

AU - Inokuchi, Jin Ichi

PY - 2014/1/1

Y1 - 2014/1/1

N2 - In the yeast Saccharomyces cerevisiae , structural diversities of complex sphingolipids [inositol phosphorylceramide (IPC), mannosylinositol phosphorylceramide, and mannosyldiinositol phosphorylceramide] are often observed in the presence or absence of hydroxyl groups on the C-4 position of long-chain base (C4-OH) and the C-2 position of very long-chain fatty acids (C2-OH), but the biological signifi - cance of these groups remains unclear. Here, we evaluated cellular membrane fl uidity in hydroxyl group-defective yeast mutants by fl uorescence recovery after photobleaching. The lateral diffusion of enhanced green fl uorescent proteintagged hexose transporter 1 (Hxt1-EGFP) was infl uenced by the absence of C4-OH and/or C2-OH. Notably, the fl uorescence recovery of Hxt1-EGFP was dramatically decreased in the sur2 - mutant (absence of C4-OH) under the csg1 - csh1 - background, in which mannosylation of IPC is blocked leading to IPC accumulation, while the recovery in the scs7 - mutant (absence of C2-OH) under the same background was modestly decreased. In addition, the amount of low affi nity tryptophan transporter 1 (Tat1)-EGFP was markedly decreased in the sur2 - csg1 - csh1 - mutant and accumulated in intracellular membranes in the scs7 - csg1 - csh1 - mutant without altering its protein expression. These results suggest that C4-OH and C2-OH are most probably critical factors for maintaining membrane fl uidity and proper turnover of membrane molecules in yeast containing complex sphingolipids with only one hydrophilic head group. -Uemura, S., F. Shishido, M. Tani, T. Mochizuki, F. Abe, and J-i. Inokuchi. Loss of hydroxyl groups from the ceramide moiety can modify the lateral diffusion of membrane proteins in S. cerevisiae . J. Lipid Res. 2014. 55: 1343 - 1356 .

AB - In the yeast Saccharomyces cerevisiae , structural diversities of complex sphingolipids [inositol phosphorylceramide (IPC), mannosylinositol phosphorylceramide, and mannosyldiinositol phosphorylceramide] are often observed in the presence or absence of hydroxyl groups on the C-4 position of long-chain base (C4-OH) and the C-2 position of very long-chain fatty acids (C2-OH), but the biological signifi - cance of these groups remains unclear. Here, we evaluated cellular membrane fl uidity in hydroxyl group-defective yeast mutants by fl uorescence recovery after photobleaching. The lateral diffusion of enhanced green fl uorescent proteintagged hexose transporter 1 (Hxt1-EGFP) was infl uenced by the absence of C4-OH and/or C2-OH. Notably, the fl uorescence recovery of Hxt1-EGFP was dramatically decreased in the sur2 - mutant (absence of C4-OH) under the csg1 - csh1 - background, in which mannosylation of IPC is blocked leading to IPC accumulation, while the recovery in the scs7 - mutant (absence of C2-OH) under the same background was modestly decreased. In addition, the amount of low affi nity tryptophan transporter 1 (Tat1)-EGFP was markedly decreased in the sur2 - csg1 - csh1 - mutant and accumulated in intracellular membranes in the scs7 - csg1 - csh1 - mutant without altering its protein expression. These results suggest that C4-OH and C2-OH are most probably critical factors for maintaining membrane fl uidity and proper turnover of membrane molecules in yeast containing complex sphingolipids with only one hydrophilic head group. -Uemura, S., F. Shishido, M. Tani, T. Mochizuki, F. Abe, and J-i. Inokuchi. Loss of hydroxyl groups from the ceramide moiety can modify the lateral diffusion of membrane proteins in S. cerevisiae . J. Lipid Res. 2014. 55: 1343 - 1356 .

UR - http://www.scopus.com/inward/record.url?scp=84904015439&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84904015439&partnerID=8YFLogxK

U2 - 10.1194/jlr.M048637

DO - 10.1194/jlr.M048637

M3 - Article

VL - 55

SP - 1343

EP - 1356

JO - Journal of Lipid Research

JF - Journal of Lipid Research

SN - 0022-2275

IS - 7

ER -