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

Chang, Chi‐Lun; Liou, Jen

doi:10.1074/jbc.m114.621375

Cited by 112 publications

(144 citation statements)

References 31 publications

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“…Rather than depend on general ER or PM, PI and PI(4,5)P 2 synthesis appear highly dependent on ER-PM contact sites and substrate channeling. Nonvesicular transport of PA, DAG, and PI between the ER and PM is also implicated in this process (Chang and Liou, 2015; Kim et al. , 2015; Saheki et al.…”

Section: Discussionmentioning

confidence: 99%

The acyltransferase LYCAT controls specific phosphoinositides and related membrane traffic

Bone

Dayam

Lee

et al. 2017

MBoC

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Phosphoinositides (PIPs) are key regulators of membrane traffic and signaling. The interconversion of PIPs by lipid kinases and phosphatases regulates their functionality. Phosphatidylinositol (PI) and PIPs have a unique enrichment of 1-stearoyl-2-arachidonyl acyl species; however, the regulation and function of this specific acyl profile remains poorly understood. We examined the role of the PI acyltransferase LYCAT in control of PIPs and PIPdependent membrane traffic. LYCAT silencing selectively perturbed the levels and localization of phosphatidylinositol-4,5-bisphosphate [PI(4,5)P 2 ] and phosphatidylinositol-3-phosphate and the membrane traffic dependent on these specific PIPs but was without effect on phosphatidylinositol-4-phosphate or biosynthetic membrane traffic. The acyl profile of PI(4,5)P 2 was selectively altered in LYCAT-deficient cells, whereas LYCAT localized with phosphatidylinositol synthase. We propose that LYCAT remodels the acyl chains of PI, which is then channeled into PI(4,5)P 2 . Our observations suggest that the PIP acyl chain profile may exert broad control of cell physiology. INTRODUCTIONPhosphoinositides (PIPs) control many facets of cell physiology, such as nutrient uptake, receptor signaling, and cell adhesion by control of specific stages of membrane traffic (Di Paolo and De Camilli, 2006;Krauss and Haucke, 2007). Through the action of lipid kinases and phosphatases, PIPs can be interconverted into seven different species defined by phosphorylation of the inositol head group (Balla, 2013). Each of the seven PIPs exhibits unique enrichment within membrane compartments and helps to recruit a variety of cognate effector proteins. Phosphatidylinositol-4,5-bisphosphate (PI(4,5)P 2 ) and phosphatidylinositol-3-phosphate (PI(3)P) illustrate these concepts well.PI(4,5)P 2 predominates within the plasma membrane (PM) and regulates clathrin-mediated endocytosis (referred to here as endocytosis) to control the internalization of cell surface proteins such as transferrin (Tfn) receptor (TfR;Jost et al., 1998;Varnai et al., 2006;Zoncu et al., 2007;Posor et al., 2013). PI(4,5)P 2 binds to and recruits AP2 and other proteins, which, together with cargo molecules and clathrin, initiate the formation and assembly of clathrin-coated pits (CCPs; Gaidarov and Keen, 1999;Itoh et al., 2001;Jackson et al., 2010). CCPs couple cargo selection to membrane invagination and eventually undergo scission from the PM by the GTPase dynamin2 to yield endocytic vesicles (Conner and Schmid, 2003;McMahon and Boucrot, 2011). CCPs harbor lipid phosphatases such as synaptojanins and OCRL that mediate PI(4,5)P 2 turnover to control the efficiency of vesicle formation (Antonescu et al., 2011) and, afterMonitoring Editor

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Section: Discussionmentioning

confidence: 99%

The acyltransferase LYCAT controls specific phosphoinositides and related membrane traffic

Bone

Dayam

Lee

et al. 2017

MBoC

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“…2C) (22,30). This comingling of calcium signaling and lipid transfer reflects a close functional linkage: Lipid transfer supplies the phosphatidylinositol needed for PIP2 resynthesis during sustained calcium signaling, and plasma membrane lipid microdomains are integral to feedback regulation of the ORAI channel by calcium and SARAF (22,31,32); conversely, local calcium signals recruit E-Syt1 and thereby either expand ER-plasma membrane junctions or strengthen junctional contacts (11,12,22,30).…”

Section: Discussionmentioning

confidence: 99%

TMEM110 regulates the maintenance and remodeling of mammalian ER–plasma membrane junctions competent for STIM–ORAI signaling

Quintana

Vangipurapu

Farber-Katz

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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The stromal interaction molecule (STIM)–ORAI calcium release-activated calcium modulator (ORAI) pathway controls store-dependent calcium entry, a major mechanism of physiological calcium signaling in mammalian cells. The core elements of the pathway are the regulatory protein STIM1, located in the endoplasmic reticulum (ER) membrane, the calcium channel ORAI1 in the plasma membrane, and sites of close contact between the ER and the plasma membrane that permit the two proteins to interact. Research on calcium signaling has centered on STIM1, ORAI1, and a few proteins that directly modulate STIM–ORAI function. However, little is known about proteins that organize ER–plasma membrane junctions for STIM–ORAI-dependent calcium signaling. Here, we report that an ER-resident membrane protein identified in a previous genome-wide RNAi screen, transmembrane protein 110 (TMEM110), regulates the long-term maintenance of ER–plasma membrane junctions and the short-term physiological remodeling of the junctions during store-dependent calcium signaling.

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“…In mammalian cells, PITPNM1 is localized in the ER that has to translocate to position this protein at an ER-PM contact site where it presumably exerts its function. A number of mechanisms have been proposed to mediate this translocation of PITPNM1 to the PM during signalling including PA binding to its C-terminal LNS2 (lipin/ned1/smp2) domain [33,34] as well as the function of a putative diacylglycerol (DAG)-binding domain [32]. By contrast, in Drosophila photoreceptors, the SMC (where RDGBα is localized) is permanently located approximately 10 nm from the base of the microvillar PM, i.e.…”

Section: Proposed Functions Of the Sub-microvillar Cisternaementioning

confidence: 92%

“…The importance of the localization of RDGBα at the SMC and the molecular interactions underlying this localization remains to be investigated ( Figure 2). One of the possible interaction which might be involved in localizing RDGBα to SMC is the interaction of its FFAT (two phenylalanines (FF) in an Acidic Tract) motif with the VAMP-associated proteins (VAPs) of ER although the potential function of PA binding to the LNS2 domain and the role of the putative DAG-binding domain in Drosophila RDGBα function remains to be studied [32][33][34].…”

Section: Proposed Functions Of the Sub-microvillar Cisternaementioning

confidence: 99%

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

Cited by 112 publications

References 31 publications

The acyltransferase LYCAT controls specific phosphoinositides and related membrane traffic

The acyltransferase LYCAT controls specific phosphoinositides and related membrane traffic

TMEM110 regulates the maintenance and remodeling of mammalian ER–plasma membrane junctions competent for STIM–ORAI signaling

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

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