Phosphatidylinositol Transfer Protein, Cytoplasmic 1 (PITPNC1) Binds and Transfers Phosphatidic Acid

Garner, Kathryn; Hunt, Alan N.; Koster, Grielof; Somerharju, Pentti; Groves, Emily; Li, Michelle; Raghu, Padinjat; Holic̆, Roman; Cockcroft, Shamshad

doi:10.1074/jbc.m112.375840

Cited by 82 publications

(89 citation statements)

References 44 publications

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“…Although Nir2 has been shown to transfer PI between membranes in vitro (9), in vivo evidence supporting inter-organelle lipid transfer mediated by Nir2 or other PITPs is missing. In this study, we devise approaches to selectively manipulate PIP 2 precursors at the ER and Golgi, and we demonstrate that Nir2-mediated PM PIP 2 replenishment is dependent on PI at the ER membrane.…”

Section: Phosphatidylinositol (Pi)mentioning

confidence: 99%

Phosphatidylinositol 4,5-Bisphosphate Homeostasis Regulated by Nir2 and Nir3 Proteins at Endoplasmic Reticulum-Plasma Membrane Junctions

Chang

Liou

2015

Journal of Biological Chemistry

119

146

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Background: Mechanisms coupling phosphatidylinositol (PI) 4,5-bisphosphate (PIP 2 ) hydrolysis to its rapid replenishment remain elusive. Results: Phosphatidic acid production triggers PIP 2 replenishment mediated by Nir2 and Nir3 at endoplasmic reticulum (ER)-plasma membrane (PM) junctions with PI at the ER membrane. Conclusion: Nir2 and Nir3 are feedback regulators for PIP 2 homeostasis. Significance: Nir2 and Nir3 maintain PIP 2 homeostasis via a nonvesicular mechanism at ER-PM junctions.

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Section: Phosphatidylinositol (Pi)mentioning

confidence: 99%

Phosphatidylinositol 4,5-Bisphosphate Homeostasis Regulated by Nir2 and Nir3 Proteins at Endoplasmic Reticulum-Plasma Membrane Junctions

Chang

Liou

2015

Journal of Biological Chemistry

119

146

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“…Biochemical analysis has shown that the PITP domain of class II PITPs have distinct lipid binding and transfer activities from those of the class I PITPs. Whereas class I PITPs are PI/phosphatidylcholine (PC) transfer proteins, the class II PITP domains have distinct properties [28,29]. In a recent study the PITP domain of RDGBα has been shown to bind and transfer both PI and phosphatidic acid (PA) but not PC in vitro [24].…”

Section: Proposed Functions Of the Sub-microvillar Cisternaementioning

confidence: 98%

The Drosophila photoreceptor as a model system for studying signalling at membrane contact sites

Yadav

Cockcroft

Raghu

2016

Biochemical Society Transactions

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Several recent studies have demonstrated the existence of membrane contact sites (MCS) between intracellular organelles in eukaryotic cells. Recent exciting studies have also demonstrated the existence of biomolecular interactions at these contact sites in mediating changes in the membrane composition of the cellular compartments. However, the role of such contact sites in regulating organelle function and physiological processes remains less clear. In this review we discuss the existence of a contact site between the plasma membrane (PM) and the endoplasmic reticulum (ER) inDrosophilaphotoreceptors. Further, we discuss the role of specific proteins present at this location in regulating phospholipid turnover and its impact in regulating a physiological process, namely phototransduction.

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“…family, bound either PtdIns or phosphatidic acid (PA) [35]). Recent studies indicate that human Nir2 (PITPNM1) and Drosophila RdgBα, which are multidomain homologues of RdgBβ, function at ER-PM contact sites, transferring PtdIns and PA in opposite directions [36,37].…”

Section: Heterotypic Lipid Exchange Between Organelles: a General Mecmentioning

confidence: 99%

“…Using a class II PITP domain [35], Nir2 would mediate PtdIns/PA exchange to promote PtdIns synthesis and the replenishment of the PM PtdIns(4,5)P2 pool, thereby maintaining the signalling competence of the cell. For clarity, E-Syt1 is represented as a monomer.…”

Section: Heterotypic Lipid Exchange Between Organelles: a General Mecmentioning

confidence: 99%

New molecular mechanisms of inter-organelle lipid transport

Drin

Filseck

Čopič

2016

Biochemical Society Transactions

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Lipids are precisely distributed in cell membranes, along with associated proteins defining organelle identity. Because the major cellular lipid factory is the endoplasmic reticulum (ER), a key issue is to understand how various lipids are subsequently delivered to other compartments by vesicular and non-vesicular transport pathways. Efforts are currently made to decipher how lipid transfer proteins (LTPs) work either across long distances or confined to membrane contact sites (MCSs) where two organelles are at close proximity. Recent findings reveal that proteins of the oxysterol-binding protein related-proteins (ORP)/oxysterol-binding homology (Osh) family are not all just sterol transporters/sensors: some can bind either phosphatidylinositol 4-phosphate (PtdIns(4)P) and sterol or PtdIns(4)P and phosphatidylserine (PS), exchange these lipids between membranes, and thereby use phosphoinositide metabolism to create cellular lipid gradients. Lipid exchange is likely a widespread mechanism also utilized by other LTPs to efficiently trade lipids between organelle membranes. Finally, the discovery of more proteins bearing a lipid-binding module (SMP or START-like domain) raises new questions on how lipids are conveyed in cells and how the activities of different LTPs are coordinated.

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Phosphatidylinositol Transfer Protein, Cytoplasmic 1 (PITPNC1) Binds and Transfers Phosphatidic Acid

Cited by 82 publications

References 44 publications

Phosphatidylinositol 4,5-Bisphosphate Homeostasis Regulated by Nir2 and Nir3 Proteins at Endoplasmic Reticulum-Plasma Membrane Junctions

Phosphatidylinositol 4,5-Bisphosphate Homeostasis Regulated by Nir2 and Nir3 Proteins at Endoplasmic Reticulum-Plasma Membrane Junctions

The Drosophila photoreceptor as a model system for studying signalling at membrane contact sites

New molecular mechanisms of inter-organelle lipid transport

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