Characterization of the GPI-anchored lipid transfer proteins in the moss Physcomitrella patens

Edstam, Monika M.; Laurila, Maiju; Höglund, Andrey; Raman, Amitha; Dahlström, Käthe M.; Salminen, Tiina A.; Edqvist, Johan; Blomqvist, Kristina

doi:10.1016/j.plaphy.2013.12.001

Cited by 42 publications

(35 citation statements)

References 92 publications

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“…Evolutionary studies of chimeric AGPs, many of which are predicted to be GPI‐anchored, could also be identified in the genomes of 47 plant species (Ma et al ). In addition, studies of GPI‐LTPs, proposed to function in the synthesis and/or deposition of cutin and cuticular waxes, in the moss Physcomitrella suggest they share similar features and function to GPI‐LTPs found in flowering plants (Edstam and Edqvist ; Edstam et al ).…”

Section: The Plant Gpi‐anchored Proteomementioning

confidence: 95%

Plant glycosylphosphatidylinositol anchored proteins at the plasma membrane‐cell wall nexus

Yeats

Bacic

Johnson

2018

JIPB

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Approximately 1% of plant proteins are predicted to be post-translationally modified with a glycosylphosphatidylinositol (GPI) anchor that tethers the polypeptide to the outer leaflet of the plasma membrane. Whereas the synthesis and structure of GPI anchors is largely conserved across eukaryotes, the repertoire of functional domains present in the GPI-anchored proteome has diverged substantially. In plants, this includes a large fraction of the GPI-anchored proteome being further modified with plant-specific arabinogalactan (AG) O-glycans. The importance of the GPI-anchored proteome to plant development is underscored by the fact that GPI biosynthetic null mutants exhibit embryo lethality. Mutations in genes encoding specific GPI-anchored proteins (GAPs) further supports their contribution to diverse biological processes, occurring at the interface of the plasma membrane and cell wall, including signaling, cell wall metabolism, cell wall polymer cross-linking, and plasmodesmatal transport. Here, we review the literature concerning plant GPI-anchored proteins, in the context of their potential to act as molecular hubs that mediate interactions between the plasma membrane and the cell wall, and their potential to transduce the signal into the protoplast and, thereby, activate signal transduction pathways.

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Section: The Plant Gpi‐anchored Proteomementioning

confidence: 95%

Plant glycosylphosphatidylinositol anchored proteins at the plasma membrane‐cell wall nexus

Yeats

Bacic

Johnson

2018

JIPB

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“…Recently we reported a critical role of OsABCG26 (ortholog of AtABCG11) in facilitating the formation of anther cuticle and pollen exine via its collaboration with OsABCG15 in rice (Zhao et al ., ). LTPs are able to carry lipid molecules and move into the extracellular space (Huang et al ., ; Liu et al ., , ; Wei and Zhong, ), and their functions in exine transportation have been confirmed in Arabidopsis and rice, such as Arabidopsis type III LTPs (Huang et al ., ), GPI‐anchored non‐specific LTPs (LTPGs; Edstam et al ., ), and rice OsC6 (Zhang et al ., ). In addition, Ubisch bodies or orbicules present on the inner surface of tapetal cells in rice and other secretory tapetum plants, which bear electron‐dense materials and display spinous or rod‐like protrusions resembling those of the pollen exine, are proposed as translocators of sporopollenin precursors onto the surface of microspores (Huysmans et al ., ; Wang et al ., ).…”

Section: Introductionmentioning

confidence: 99%

Rice No Pollen 1 (NP1) is required for anther cuticle formation and pollen exine patterning

et al. 2017

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Angiosperm male reproductive organs (anthers and pollen grains) have complex and interesting morphological features, but mechanisms that underlie their patterning are poorly understood. Here we report the isolation and characterization of a male sterile mutant of No Pollen 1 (NP1) in rice (Oryza sativa). The np1-4 mutant exhibited smaller anthers with a smooth cuticle surface, abnormal Ubisch bodies, and aborted pollen grains covered with irregular exine. Wild-type exine has two continuous layers; but np1-4 exine showed a discontinuous structure with large granules of varying size. Chemical analysis revealed reduction in most of the cutin monomers in np1-4 anthers, and less cuticular wax. Map-based cloning suggested that NP1 encodes a putative glucose-methanol-choline oxidoreductase; and expression analyses found NP1 preferentially expressed in the tapetal layer from stage 8 to stage 10 of anther development. Additionally, the expression of several genes involved in biosynthesis and in the transport of lipid monomers of sporopollenin and cutin was decreased in np1-4 mutant anthers. Taken together, these observations suggest that NP1 is required for anther cuticle formation, and for patterning of Ubisch bodies and the exine. We propose that products of NP1 are likely important metabolites in the development of Ubisch bodies and pollen exine, necessary for polymerization, assembly, or both.

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“…The locations of the LTPs are varied. LTPs occur in the plasma membrane (Debono et al, 2009; Kim et al, 2012), cell wall (Thoma et al, 1993), or cytoplasm (Guo et al, 2013; Edstam et al, 2014). LTPs are reported to probable participated in cutin synthesis (Pyee et al, 1994; Han et al, 2001; Debono et al, 2009; Kim et al, 2012), pathogen defense responses (Maldonado et al, 2002; Silverstein et al, 2007; Guo et al, 2013; Yu et al, 2013), reproductive development (Chae et al, 2009; Zhang D. et al, 2010; Zhang Y. et al, 2010), and adaption to abiotic stresses (Guo et al, 2013; Pitzschke et al, 2014), even though their functions remain unclear.…”

Section: Introductionmentioning

confidence: 99%

A Non-specific Setaria italica Lipid Transfer Protein Gene Plays a Critical Role under Abiotic Stress

Pan

Jiao

et al. 2016

Front. Plant Sci.

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Lipid transfer proteins (LTPs) are a class of cysteine-rich soluble proteins having small molecular weights. LTPs participate in flower and seed development, cuticular wax deposition, also play important roles in pathogen and abiotic stress responses. A non-specific LTP gene (SiLTP) was isolated from a foxtail millet (Setaria italica) suppression subtractive hybridization library enriched for differentially expressed genes after abiotic stress treatments. A semi-quantitative reverse transcriptase PCR analysis showed that SiLTP was expressed in all foxtail millet tissues. Additionally, the SiLTP promoter drove GUS expression in root tips, stems, leaves, flowers, and siliques of transgenic Arabidopsis. Quantitative real-time PCR indicated that the SiLTP expression was induced by NaCl, polyethylene glycol, and abscisic acid (ABA). SiLTP was localized in the cytoplasm of tobacco leaf epidermal cells and maize protoplasts. The ectopic expression of SiLTP in tobacco resulted in higher levels of salt and drought tolerance than in the wild type (WT). To further assess the function of SiLTP, SiLTP overexpression (OE) and RNA interference (RNAi)-based transgenic foxtail millet were obtained. SiLTP-OE lines performed better under salt and drought stresses compared with WT plants. In contrast, the RNAi lines were much more sensitive to salt and drought compared than WT. Electrophoretic mobility shift assays and yeast one-hybrids indicated that the transcription factor ABA-responsive DRE-binding protein (SiARDP) could bind to the dehydration-responsive element of SiLTP promoter in vitro and in vivo, respectively. Moreover, the SiLTP expression levels were higher in SiARDP-OE plants compared than the WT. These results confirmed that SiLTP plays important roles in improving salt and drought stress tolerance of foxtail millet, and may partly be upregulated by SiARDP. SiLTP may provide an effective genetic resource for molecular breeding in crops to enhance salt and drought tolerance levels.

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Characterization of the GPI-anchored lipid transfer proteins in the moss Physcomitrella patens

Cited by 42 publications

References 92 publications

Plant glycosylphosphatidylinositol anchored proteins at the plasma membrane‐cell wall nexus

Plant glycosylphosphatidylinositol anchored proteins at the plasma membrane‐cell wall nexus

Rice No Pollen 1 (NP1) is required for anther cuticle formation and pollen exine patterning

A Non-specific Setaria italica Lipid Transfer Protein Gene Plays a Critical Role under Abiotic Stress

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