Loss of Inositol Phosphorylceramide Sphingolipid Mannosylation Induces Plant Immune Responses and Reduces Cellulose Content in Arabidopsis. Issue 12 (28th November 2016)
- Record Type:
- Journal Article
- Title:
- Loss of Inositol Phosphorylceramide Sphingolipid Mannosylation Induces Plant Immune Responses and Reduces Cellulose Content in Arabidopsis. Issue 12 (28th November 2016)
- Main Title:
- Loss of Inositol Phosphorylceramide Sphingolipid Mannosylation Induces Plant Immune Responses and Reduces Cellulose Content in Arabidopsis
- Authors:
- Fang, Lin
Ishikawa, Toshiki
Rennie, Emilie A.
Murawska, Gosia M.
Lao, Jeemeng
Yan, Jingwei
Tsai, Alex Yi-Lin
Baidoo, Edward E.K.
Xu, Jun
Keasling, Jay D.
Demura, Taku
Kawai-Yamada, Maki
Scheller, Henrik V.
Mortimer, Jenny C. - Abstract:
- Abstract : Identification and characterization of a putative Arabidopsis sphingolipid glycosyltranferase suggests that glycosylation of these crucial lipids affects cellulose content and plant defense signaling. Abstract: Glycosylinositol phosphorylceramides (GIPCs) are a class of glycosylated sphingolipids found in plants, fungi, and protozoa. These lipids are abundant in the plant plasma membrane, forming ∼25% of total plasma membrane lipids. Little is known about the function of the glycosylated headgroup, but two recent studies have indicated that they play a key role in plant signaling and defense. Here, we show that a member of glycosyltransferase family 64, previously named ECTOPICALLY PARTING CELLS1, is likely a Golgi-localized GIPC -specific mannosyl-transferase, which we renamed GIPC MANNOSYL-TRANSFERASE1 (GMT1). Sphingolipid analysis revealed that the Arabidopsis thaliana gmt1 mutant almost completely lacks mannose-carrying GIPCs. Heterologous expression of GMT1 in Saccharomyces cerevisiae and tobacco ( Nicotiana tabacum ) cv Bright Yellow 2 resulted in the production of non-native mannosylated GIPCs. gmt1 displays a severe dwarfed phenotype and a constitutive hypersensitive response characterized by elevated salicylic acid and hydrogen peroxide levels, similar to that we previously reported for the Golgi-localized, GIPC -specific, GDP-Man transporter GONST1 (Mortimer et al., 2013 ). Unexpectedly, we show that gmt1 cell walls have a reduction in celluloseAbstract : Identification and characterization of a putative Arabidopsis sphingolipid glycosyltranferase suggests that glycosylation of these crucial lipids affects cellulose content and plant defense signaling. Abstract: Glycosylinositol phosphorylceramides (GIPCs) are a class of glycosylated sphingolipids found in plants, fungi, and protozoa. These lipids are abundant in the plant plasma membrane, forming ∼25% of total plasma membrane lipids. Little is known about the function of the glycosylated headgroup, but two recent studies have indicated that they play a key role in plant signaling and defense. Here, we show that a member of glycosyltransferase family 64, previously named ECTOPICALLY PARTING CELLS1, is likely a Golgi-localized GIPC -specific mannosyl-transferase, which we renamed GIPC MANNOSYL-TRANSFERASE1 (GMT1). Sphingolipid analysis revealed that the Arabidopsis thaliana gmt1 mutant almost completely lacks mannose-carrying GIPCs. Heterologous expression of GMT1 in Saccharomyces cerevisiae and tobacco ( Nicotiana tabacum ) cv Bright Yellow 2 resulted in the production of non-native mannosylated GIPCs. gmt1 displays a severe dwarfed phenotype and a constitutive hypersensitive response characterized by elevated salicylic acid and hydrogen peroxide levels, similar to that we previously reported for the Golgi-localized, GIPC -specific, GDP-Man transporter GONST1 (Mortimer et al., 2013 ). Unexpectedly, we show that gmt1 cell walls have a reduction in cellulose content, although other matrix polysaccharides are unchanged. … (more)
- Is Part Of:
- The Plant Cell. Volume 28:Issue 12(2016)
- Journal:
- The Plant Cell
- Issue:
- Volume 28:Issue 12(2016)
- Issue Display:
- Volume 28, Issue 12 (2016)
- Year:
- 2016
- Volume:
- 28
- Issue:
- 12
- Issue Sort Value:
- 2016-0028-0012-0000
- Page Start:
- 2991
- Page End:
- 3004
- Publication Date:
- 2016-11-28
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.16.00186 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16361.xml