ArticleMolecular biology of the cell2016
Two-ligand priming mechanism for potentiated phosphoinositide synthesis is an evolutionarily conserved feature of Sec14-like phosphatidylinositol and phosphatidylcholine exchange proteins.
Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
17 citing papers in PubMed, 32 citations in OpenAlex.
- Genome-wide identification of the peanut PITP gene family and functional verification of AhSFH8 in resistance to Aspergillus flavus infection.BMC plant biology · 2025Article
- A brief history of phosphatidylinositol transfer proteins: from the backwaters of cell biology to prime time in lipid signaling.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2025Review
- OsSNDP4, a Sec14-nodulin Domain Protein, is Required for Pollen Development in Rice.Rice (New York, N.Y.) · 2024Article
- SF-1 Induces Nuclear PIP2.Biomolecules · 2023Article
- SEC14-GOLD protein PATELLIN2 binds IRON-REGULATED TRANSPORTER1 linking root iron uptake to vitamin E.Plant physiology · 2023Article
- Role of SEC14-like phosphatidylinositol transfer proteins in membrane identity and dynamics.Frontiers in plant science · 2023Review
- OsSNDP3 Functions for the Polar Tip Growth in Rice Pollen Together with OsSNDP2, a Paralog of OsSNDP3.Rice (New York, N.Y.) · 2022Article
- Emerging Prospects for Combating Fungal Infections by Targeting Phosphatidylinositol Transfer Proteins.International journal of molecular sciences · 2021Review
- Anionic phospholipid gradients: an uncharacterized frontier of the plant endomembrane network.Plant physiology · 2021Article
- A Sec14-like phosphatidylinositol transfer protein paralog defines a novel class of heme-binding proteins.eLife · 2020Article
- Noncanonical regulation of phosphatidylserine metabolism by a Sec14-like protein and a lipid kinase.The Journal of cell biology · 2020Article
- Functional diversification of the chemical landscapes of yeast Sec14-like phosphatidylinositol transfer protein lipid-binding cavities.The Journal of biological chemistry · 2019Article
- Genome-wide identification, phylogeny, and expression analysis of Sec14-like PITP gene family in sugarcane.Plant cell reports · 2019Article
- Lipid transfer proteins: the lipid commute via shuttles, bridges and tubes.Nature reviews. Molecular cell biology · 2019Review
- The interface between phosphatidylinositol transfer protein function and phosphoinositide signaling in higher eukaryotes.Journal of lipid research · 2019Review
- A Golgi Lipid Signaling Pathway Controls Apical Golgi Distribution and Cell Polarity during Neurogenesis.Developmental cell · 2018Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
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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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.