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  4. Monthly Traffic Estimate
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We began analyzing https://www.molbiolcell.org/doi/10.1091/mbc.E16-04-0221, but it redirected us to https://www.molbiolcell.org/doi/10.1091/mbc.E16-04-0221. The analysis below is for the second page.

Title[redir]:
Two-ligand priming mechanism for potentiated phosphoinositide synthesis is an evolutionarily conserved feature of Sec14-like phosphatidylinositol and phosphatidylcholine exchange proteins | Molecular Biology of the Cell
Description:
Lipid signaling, particularly phosphoinositide signaling, plays a key role in regulating the extreme polarized membrane growth that drives root hair development in plants. The Arabidopsis AtSFH1 gene encodes a two-domain protein with an amino-terminal Sec14-like phosphatidylinositol transfer protein (PITP) domain linked to a carboxy-terminal nodulin domain. AtSfh1 is critical for promoting the spatially highly organized phosphatidylinositol-4,5-bisphosphate signaling program required for establishment and maintenance of polarized root hair growth. Here we demonstrate that, like the yeast Sec14, the AtSfh1 PITP domain requires both its phosphatidylinositol (PtdIns)- and phosphatidylcholine (PtdCho)-binding properties to stimulate PtdIns-4-phosphate [PtdIns(4)P] synthesis. Moreover, we show that both phospholipid-binding activities are essential for AtSfh1 activity in supporting polarized root hair growth. Finally, we report genetic and biochemical evidence that the two-ligand mechanism for potentiation of PtdIns 4-OH kinase activity is a broadly conserved feature of plant Sec14-nodulin proteins, and that this strategy appeared only late in plant evolution. Taken together, the data indicate that the PtdIns/PtdCho-exchange mechanism for stimulated PtdIns(4)P synthesis either arose independently during evolution in yeast and in higher plants, or a suitable genetic module was introduced to higher plants from a fungal source and subsequently exploited by them.

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Content Management System {📝}

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🚄 Respectable Traffic: 10k - 20k visitors per month


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Keywords {🔍}

atsfh, ptdins, proteins, sec, root, yeast, google, scholar, protein, transfer, figure, ptdinsp, plant, medline, plants, crossref, ptdcho, ptdchobinding, secnodulin, lbd, mutant, seclike, activity, phosphoinositide, synthesis, hair, arabidopsis, activities, domain, hairs, cell, bankaitis, lipid, relative, residues, expression, phosphatidylinositol, signaling, growth, schaaf, domains, membrane, functional, binding, conserved, mechanism, lbds, seedlings, tip, barcodes,

Topics {✒️}

1-palmitoyl-2-decapyrenyl-sn-glycero-3-phosphoinositol 1-palmitoyl-2-decapyrenyl-sn-glycero-3-phosphocholine 1-palmitoyl-2-hydroxy-sn-glycero-3-phosphocholine high-performance liquid chromatography age-matched wild-type seedlings attribution–noncommercial–share alike 3 atsfh1-lbd phospholipid-binding motifs perform site-directed mutagenesis triple-tip-growing root hairs post–md simulation analyses specific phospholipid-binding/transfer defects confocal spinning-disk microscope stranded β-sheet capped ligand ptdins/ptdcho-exchange strategy ligand ptdins/ptdcho-exchange mechanism ptdins/ptdcho-binding/exchange activities uk/tools/msa/clustalo/ atsfh1-ptdins/ptdcho homology models called “pinch-close” mutants agrobacterium tumefaciens–mediated transformation sec14-1ts sac1 strain uk/tools/phylogeny/clustalw2_phylogeny/ l-α-phosphatidic acid octahistidine-tagged recombinant proteins ptdcho head-group binding phospholipid-binding pocket floor phospholipid-binding pocket comprises free-standing nodulin domain �front-end” sensing mechanism atsfh1-lbd residues r96 mutant versions atsfh1-lbdr96a carboxy-terminal nodulin domain quantify tip-directed ptdins ptdcho head-group phosphate ptdcho-exchange activities afforded recognizable ptdcho-binding barcode atsfh1-mediated lateral organization atsfh1-lbd structural element chimeric sec14-nodulin protein pairwise t-test analyses plcδ1-ph domain tagged heterotypic ptdcho/ptdins exchange specific lipid-regulated arfgaps strong tip-focused ptdins hydrophobic phospholipid-binding pocket ptdins-binding-defective mutants reconstituted atsfh1-null plants cognate phospholipid-binding barcodes site-directed mutagenesis ptdcho-binding barcode residues

Questions {❓}

  • , 2004, 2006)?
  • One possibility is that bulk membrane PtdCho is not generally accessible to (is sequestered from?

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External Links {🔗}(281)

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  • mx.zoho.eu
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