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Title: GLUCOSAMINE INOSITOLPHOSPHORYLCERAMIDE TRANSFERASE1 (GINT1) Is a GlcNAc-Containing Glycosylinositol Phosphorylceramide Glycosyltransferase

Abstract

Glycosylinositol phosphorylceramides (GIPCs), which have a ceramide core linked to a glycan headgroup of varying structure, are the major sphingolipids in the plant plasma membrane. Recently, we identified the major biosynthetic genes for GIPC glycosylation in Arabidopsis thaliana, and demonstrated that the glycan headgroup is essential for plant viability. However, the function of GIPCs and the significance of their structural variation are poorly understood. Here, we characterized the Arabidopsis glycosyltransferase GLUCOSAMINE INOSITOLPHOSPHORYLCERAMIDE TRANSFERASE1 (GINT1) and showed that it is responsible for the glycosylation of a subgroup of GIPCs found in seeds and pollen that contain N-acetylglucosamine (GlcNAc) and glucosamine (GlcN; collectively GlcN(Ac)). In Arabidopsis gint1 plants, loss of the GlcN(Ac) GIPCs did not affect vegetative growth, although seed germination was less sensitive to abiotic stress than in wild-type plants. However, in rice, where GlcN(Ac) containing GIPCs are the major GIPC subgroup in vegetative tissue, loss of GINT1 was seedling lethal. Furthermore, we could produce, de novo, "rice-like" GlcN(Ac) GIPCs in Arabidopsis leaves, which allowed us to test the function of different sugars in the GIPC headgroup. Lastly, this study describes a monocot GIPC biosynthetic enzyme and shows that its Arabidopsis homolog has the same biochemical function. We also identify amore » possible role for GIPCs in maintaining cell-cell adhesion.« less

Authors:
ORCiD logo [1]; ORCiD logo [2]; ORCiD logo [3]; ORCiD logo [2]; ORCiD logo [2]; ORCiD logo [2]; ORCiD logo [4]; ORCiD logo [5]; ORCiD logo [4]; ORCiD logo [1]; ORCiD logo [2]
  1. Graduate School of Science and Engineering, Saitama University, Saitama 338-8570, Japan
  2. Joint BioEnergy Institute, Emeryville, California 94608, Biosciences Area, Lawrence Berkeley National Laboratory, Berkeley, California 94720
  3. Biosciences Area, Lawrence Berkeley National Laboratory, Berkeley, California 94720, Department of Plant and Molecular Biology, University of California, Berkeley, California 94720, Center for Plant Science Innovation and Department of Biochemistry, University of Nebraska-Lincoln, Lincoln, Nebraska 68588
  4. Joint BioEnergy Institute, Emeryville, California 94608, Biosciences Area, Lawrence Berkeley National Laboratory, Berkeley, California 94720, Department of Plant and Molecular Biology, University of California, Berkeley, California 94720
  5. Center for Plant Science Innovation and Department of Biochemistry, University of Nebraska-Lincoln, Lincoln, Nebraska 68588
Publication Date:
Research Org.:
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23); National Science Foundation (NSF)
OSTI Identifier:
1437090
Alternate Identifier(s):
OSTI ID: 1457008
Grant/Contract Number:  
AC02-05CH11231; 17K15411; 26292190; 1158500
Resource Type:
Published Article
Journal Name:
Plant Physiology (Bethesda)
Additional Journal Information:
Journal Name: Plant Physiology (Bethesda) Journal Volume: 177 Journal Issue: 3; Journal ID: ISSN 0032-0889
Publisher:
American Society of Plant Biologists (ASPB)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Ishikawa, Toshiki, Fang, Lin, Rennie, Emilie A., Sechet, Julien, Yan, Jingwei, Jing, Beibei, Moore, William, Cahoon, Edgar B., Scheller, Henrik V., Kawai-Yamada, Maki, and Mortimer, Jenny C. GLUCOSAMINE INOSITOLPHOSPHORYLCERAMIDE TRANSFERASE1 (GINT1) Is a GlcNAc-Containing Glycosylinositol Phosphorylceramide Glycosyltransferase. United States: N. p., 2018. Web. doi:10.1104/pp.18.00396.
Ishikawa, Toshiki, Fang, Lin, Rennie, Emilie A., Sechet, Julien, Yan, Jingwei, Jing, Beibei, Moore, William, Cahoon, Edgar B., Scheller, Henrik V., Kawai-Yamada, Maki, & Mortimer, Jenny C. GLUCOSAMINE INOSITOLPHOSPHORYLCERAMIDE TRANSFERASE1 (GINT1) Is a GlcNAc-Containing Glycosylinositol Phosphorylceramide Glycosyltransferase. United States. doi:10.1104/pp.18.00396.
Ishikawa, Toshiki, Fang, Lin, Rennie, Emilie A., Sechet, Julien, Yan, Jingwei, Jing, Beibei, Moore, William, Cahoon, Edgar B., Scheller, Henrik V., Kawai-Yamada, Maki, and Mortimer, Jenny C. Mon . "GLUCOSAMINE INOSITOLPHOSPHORYLCERAMIDE TRANSFERASE1 (GINT1) Is a GlcNAc-Containing Glycosylinositol Phosphorylceramide Glycosyltransferase". United States. doi:10.1104/pp.18.00396.
@article{osti_1437090,
title = {GLUCOSAMINE INOSITOLPHOSPHORYLCERAMIDE TRANSFERASE1 (GINT1) Is a GlcNAc-Containing Glycosylinositol Phosphorylceramide Glycosyltransferase},
author = {Ishikawa, Toshiki and Fang, Lin and Rennie, Emilie A. and Sechet, Julien and Yan, Jingwei and Jing, Beibei and Moore, William and Cahoon, Edgar B. and Scheller, Henrik V. and Kawai-Yamada, Maki and Mortimer, Jenny C.},
abstractNote = {Glycosylinositol phosphorylceramides (GIPCs), which have a ceramide core linked to a glycan headgroup of varying structure, are the major sphingolipids in the plant plasma membrane. Recently, we identified the major biosynthetic genes for GIPC glycosylation in Arabidopsis thaliana, and demonstrated that the glycan headgroup is essential for plant viability. However, the function of GIPCs and the significance of their structural variation are poorly understood. Here, we characterized the Arabidopsis glycosyltransferase GLUCOSAMINE INOSITOLPHOSPHORYLCERAMIDE TRANSFERASE1 (GINT1) and showed that it is responsible for the glycosylation of a subgroup of GIPCs found in seeds and pollen that contain N-acetylglucosamine (GlcNAc) and glucosamine (GlcN; collectively GlcN(Ac)). In Arabidopsis gint1 plants, loss of the GlcN(Ac) GIPCs did not affect vegetative growth, although seed germination was less sensitive to abiotic stress than in wild-type plants. However, in rice, where GlcN(Ac) containing GIPCs are the major GIPC subgroup in vegetative tissue, loss of GINT1 was seedling lethal. Furthermore, we could produce, de novo, "rice-like" GlcN(Ac) GIPCs in Arabidopsis leaves, which allowed us to test the function of different sugars in the GIPC headgroup. Lastly, this study describes a monocot GIPC biosynthetic enzyme and shows that its Arabidopsis homolog has the same biochemical function. We also identify a possible role for GIPCs in maintaining cell-cell adhesion.},
doi = {10.1104/pp.18.00396},
journal = {Plant Physiology (Bethesda)},
number = 3,
volume = 177,
place = {United States},
year = {2018},
month = {5}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
DOI: 10.1104/pp.18.00396

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Cited by: 4 works
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