ArticleNature communications2014
Molecular insights into the membrane-associated phosphatidylinositol 4-kinase IIα.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Phosphatidylinositol 4-kinase as a target of pathogens-friend or foe?FEBS letters · 2026Review
- Phosphatidylinositol 4-phosphate; A minor lipid with multiple personalities.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2025Review
- Specific sialylation of N-glycans and its novel regulatory mechanism.Glycoconjugate journal · 2024Review
- Reconstitution of ORP-mediated lipid exchange coupled to PI4P metabolism.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Review
- Reconstitution of ORP-mediated lipid exchange process coupled to PI(4)P metabolism.bioRxiv : the preprint server for biology · 2023Article
- Loss of the batten disease protein CLN3 leads to mis-trafficking of M6PR and defective autophagic-lysosomal reformation.Nature communications · 2023Article
- A Plethora of Functions Condensed into Tiny Phospholipids: The Story of PI4P and PI(4,5)PCells · 2023Review
- Tex2 is required for lysosomal functions at TMEM55-dependent ER membrane contact sites.The Journal of cell biology · 2023Article
- Chemoproteomic profiling of kinases in live cells using electrophilic sulfonyl triazole probes.Chemical science · 2021Article
- Transport Pathways That Contribute to the Cellular Distribution of Phosphatidylserine.Frontiers in cell and developmental biology · 2021Review
- Putative Role of Protein Palmitoylation in Cardiac Lipid-Induced Insulin Resistance.International journal of molecular sciences · 2020Review
- Novel defect in phosphatidylinositol 4-kinase type 2-alpha (PI4K2A) at the membrane-enzyme interface is associated with metabolic cutis laxa.Journal of inherited metabolic disease · 2020Article
- Palmitoylation: A Fatty Regulator of Myocardial Electrophysiology.Frontiers in physiology · 2020Review
- Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.Chemical reviews · 2019Review
- A complex between phosphatidylinositol 4-kinase IIα and integrin α3β1 is required forThe Journal of biological chemistry · 2019Article
- Lipopolysaccharide Upregulates Palmitoylated Enzymes of the Phosphatidylinositol Cycle: An Insight from Proteomic Studies.Molecular & cellular proteomics : MCP · 2018Article
- Protein post-translational modifications:Computational and structural biotechnology journal · 2017Review
- Diverse mechanisms of metaeffector activity in an intracellular bacterial pathogen, Legionella pneumophila.Molecular systems biology · 2016Article
- Can I solve my structure by SAD phasing? Planning an experiment, scaling data and evaluating the useful anomalous correlation and anomalous signal.Acta crystallographica. Section D, Structural biology · 2016Article
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Phosphatidylinositol 4-kinase IIα (PI4KIIα), a membrane-associated PI kinase, plays a central role in cell signalling and trafficking. Its kinase activity critically depends on palmitoylation of its cysteine-rich motif (-CCPCC-) and is modulated by the membrane environment. Lack of atomic structure impairs our understanding of the mechanism regulating kinase activity. Here we present the crystal structure of human PI4KIIα in ADP-bound form. The structure identifies the nucleotide-binding pocket that differs notably from that found in PI3Ks. Two structural insertions, a palmitoylation insertion and an RK-rich insertion, endow PI4KIIα with the 'integral' membrane-binding feature. Molecular dynamics simulations, biochemical and mutagenesis studies reveal that the palmitoylation insertion, containing an amphipathic helix, contributes to the PI-binding pocket and anchors PI4KIIα to the membrane, suggesting that fluctuation of the palmitoylation insertion affects PI4KIIα's activity. We conclude from our results that PI4KIIα's activity is regulated indirectly through changes in the membrane environment.
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