ArticleMolecular biology of the cell2006
Specific and nonspecific membrane-binding determinants cooperate in targeting phosphatidylinositol transfer protein beta-isoform to the mammalian trans-Golgi network.
Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 47 citations in OpenAlex.
- Leaflet-specific phospholipid imaging using genetically encoded proximity sensors.Nature chemical biology · 2026Article
- Mammalian START-like phosphatidylinositol transfer proteins - Physiological perspectives and roles in cancer biology.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2024Review
- Non-vesicular phosphatidylinositol transfer plays critical roles in defining organelle lipid composition.The EMBO journal · 2024Article
- Individual phosphatidylinositol transfer proteins have distinct functions that do not involve lipid transfer activity.Blood advances · 2023Article
- Courier service for phosphatidylinositol: PITPs deliver on demand.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2021Review
- Lipid synthesis and transport are coupled to regulate membrane lipid dynamics in the endoplasmic reticulum.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020Review
- Lipid Exchangers: Cellular Functions and Mechanistic Links With Phosphoinositide Metabolism.Frontiers in cell and developmental biology · 2020Review
- GOLPH3: a Golgi phosphatidylinositol(4)phosphate effector that directs vesicle trafficking and drives cancer.Journal of lipid research · 2019Review
- The interface between phosphatidylinositol transfer protein function and phosphoinositide signaling in higher eukaryotes.Journal of lipid research · 2019Review
- Polyphosphoinositide-Binding Domains: Insights from Peripheral Membrane and Lipid-Transfer Proteins.Advances in experimental medicine and biology · 2019Review
- A Golgi Lipid Signaling Pathway Controls Apical Golgi Distribution and Cell Polarity during Neurogenesis.Developmental cell · 2018Article
- Dynamics and energetics of the mammalian phosphatidylinositol transfer protein phospholipid exchange cycle.The Journal of biological chemistry · 2017Article
- Quantitative profiling of the endonuclear glycerophospholipidome of murine embryonic fibroblasts.Journal of lipid research · 2016Article
- Phosphoinositides: tiny lipids with giant impact on cell regulation.Physiological reviews · 2013Review
- Modifier genes for mouse phosphatidylinositol transfer protein α (vibrator) that bypass juvenile lethality.Genetics · 2011Article
- Mammalian diseases of phosphatidylinositol transfer proteins and their homologs.Clinical lipidology · 2010Article
- Non-vesicular lipid transport by lipid-transfer proteins and beyond.Nature reviews. Molecular cell biology · 2010Review
- Zebrafish class 1 phosphatidylinositol transfer proteins: PITPbeta and double cone cell outer segment integrity in retina.Traffic (Copenhagen, Denmark) · 2010Article
- Phosphatidylinositol- and phosphatidylcholine-transfer activity of PITPbeta is essential for COPI-mediated retrograde transport from the Golgi to the endoplasmic reticulum.Journal of cell science · 2010Article
- Phosphoinositide signaling: new tools and insights.Physiology (Bethesda, Md.) · 2009Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Phosphatidylinositol transfer proteins (PITPs) regulate the interface between lipid metabolism and specific steps in membrane trafficking through the secretory pathway in eukaryotes. Herein, we describe the cis-acting information that controls PITPbeta localization in mammalian cells. We demonstrate PITPbeta localizes predominantly to the trans-Golgi network (TGN) and that this localization is independent of the phospholipid-bound state of PITPbeta. Domain mapping analyses show the targeting information within PITPbeta consists of three short C-terminal specificity elements and a nonspecific membrane-binding element defined by a small motif consisting of adjacent tryptophan residues (the W(202)W(203) motif). Combination of the specificity elements with the W(202)W(203) motif is necessary and sufficient to generate an efficient TGN-targeting module. Finally, we demonstrate that PITPbeta association with the TGN is tolerant to a range of missense mutations at residue serine 262, we describe the TGN localization of a novel PITPbeta isoform with a naturally occurring S262Q polymorphism, and we find no other genetic or pharmacological evidence to support the concept that PITPbeta localization to the TGN is obligately regulated by conventional protein kinase C (PKC) or the Golgi-localized PKC isoforms delta or epsilon. These latter findings are at odds with a previous report that conventional PKC-mediated phosphorylation of residue Ser262 is required for PITPbeta targeting to Golgi membranes.
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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.