메뉴 건너뛰기




Volumn 33, Issue 5, 2015, Pages 549-561

Phosphatidylinositol-Phosphatidic Acid Exchange by Nir2 at ER-PM Contact Sites Maintains Phosphoinositide Signaling Competence

Author keywords

[No Author keywords available]

Indexed keywords

CYTIDINE DIPHOSPHATE; DIACYLGLYCEROL; MEMBRANE PROTEIN; NIR2 PROTEIN; PHOSPHATIDIC ACID; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL; UNCLASSIFIED DRUG; CALCIUM BINDING PROTEIN; EYE PROTEIN; PHOSPHOLIPASE C; PITPNM1 PROTEIN, HUMAN; POLYPHOSPHOINOSITIDE; SMALL INTERFERING RNA;

EID: 84930575796     PISSN: 15345807     EISSN: 18781551     Source Type: Journal    
DOI: 10.1016/j.devcel.2015.04.028     Document Type: Article
Times cited : (177)

References (41)
  • 1
    • 70449263450 scopus 로고
    • The enzymatic synthesis of inositol phosphatide
    • Agranoff B.W., Bradley R.M., Brady R.O. The enzymatic synthesis of inositol phosphatide. J.Biol. Chem. 1958, 233:1077-1083.
    • (1958) J.Biol. Chem. , vol.233 , pp. 1077-1083
    • Agranoff, B.W.1    Bradley, R.M.2    Brady, R.O.3
  • 2
    • 0015242494 scopus 로고
    • Reduced brain inositol in lithium-treated rats
    • Allison J.H., Stewart M.A. Reduced brain inositol in lithium-treated rats. Nat. New Biol. 1971, 233:267-268.
    • (1971) Nat. New Biol. , vol.233 , pp. 267-268
    • Allison, J.H.1    Stewart, M.A.2
  • 3
    • 14044268935 scopus 로고    scopus 로고
    • Differential regulation of endoplasmic reticulum structure through VAP-Nir protein interaction
    • Amarilio R., Ramachandran S., Sabanay H., Lev S. Differential regulation of endoplasmic reticulum structure through VAP-Nir protein interaction. J.Biol. Chem. 2005, 280:5934-5944.
    • (2005) J.Biol. Chem. , vol.280 , pp. 5934-5944
    • Amarilio, R.1    Ramachandran, S.2    Sabanay, H.3    Lev, S.4
  • 4
    • 84880962133 scopus 로고    scopus 로고
    • Phosphoinositides: tiny lipids with giant impact on cell regulation
    • Balla T. Phosphoinositides: tiny lipids with giant impact on cell regulation. Physiol. Rev. 2013, 93:1019-1137.
    • (2013) Physiol. Rev. , vol.93 , pp. 1019-1137
    • Balla, T.1
  • 5
    • 77649159735 scopus 로고    scopus 로고
    • The Sec14 superfamily and mechanisms for crosstalk between lipid metabolism and lipid signaling
    • Bankaitis V.A., Mousley C.J., Schaaf G. The Sec14 superfamily and mechanisms for crosstalk between lipid metabolism and lipid signaling. Trends Biochem. Sci. 2010, 35:150-160.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 150-160
    • Bankaitis, V.A.1    Mousley, C.J.2    Schaaf, G.3
  • 6
    • 0021443856 scopus 로고
    • Inositol trisphosphate and diacylglycerol as second messengers
    • Berridge M.J. Inositol trisphosphate and diacylglycerol as second messengers. Biochem. J. 1984, 220:345-360.
    • (1984) Biochem. J. , vol.220 , pp. 345-360
    • Berridge, M.J.1
  • 7
    • 0020465411 scopus 로고
    • Lithium amplifies agonist-dependent phosphatidylinositol responses in brain and salivary glands
    • Berridge M.J., Downes C.P., Hanley M.R. Lithium amplifies agonist-dependent phosphatidylinositol responses in brain and salivary glands. Biochem. J. 1982, 206:587-595.
    • (1982) Biochem. J. , vol.206 , pp. 587-595
    • Berridge, M.J.1    Downes, C.P.2    Hanley, M.R.3
  • 8
    • 84887617011 scopus 로고    scopus 로고
    • Feedback regulation of receptor-induced Ca2+ signaling mediated by E-Syt1 and Nir2 at endoplasmic reticulum-plasma membrane junctions
    • Chang C.L., Hsieh T.S., Yang T.T., Rothberg K.G., Azizoglu D.B., Volk E., Liao J.C., Liou J. Feedback regulation of receptor-induced Ca2+ signaling mediated by E-Syt1 and Nir2 at endoplasmic reticulum-plasma membrane junctions. Cell Rep. 2013, 5:813-825.
    • (2013) Cell Rep. , vol.5 , pp. 813-825
    • Chang, C.L.1    Hsieh, T.S.2    Yang, T.T.3    Rothberg, K.G.4    Azizoglu, D.B.5    Volk, E.6    Liao, J.C.7    Liou, J.8
  • 9
    • 79952915896 scopus 로고    scopus 로고
    • Function of the phosphatidylinositol transfer protein gene family: is phosphatidylinositol transfer the mechanism of action?
    • Cockcroft S., Garner K. Function of the phosphatidylinositol transfer protein gene family: is phosphatidylinositol transfer the mechanism of action?. Crit. Rev. Biochem. Mol. Biol. 2011, 46:89-117.
    • (2011) Crit. Rev. Biochem. Mol. Biol. , vol.46 , pp. 89-117
    • Cockcroft, S.1    Garner, K.2
  • 14
    • 0025719245 scopus 로고
    • Synthesis of phosphatidylinositol 4,5-bisphosphate in the endoplasmic reticulum of Chinese hamster ovary cells
    • Helms J.B., de Vries K.J., Wirtz K.W. Synthesis of phosphatidylinositol 4,5-bisphosphate in the endoplasmic reticulum of Chinese hamster ovary cells. J.Biol. Chem. 1991, 266:21368-21374.
    • (1991) J.Biol. Chem. , vol.266 , pp. 21368-21374
    • Helms, J.B.1    de Vries, K.J.2    Wirtz, K.W.3
  • 15
    • 0005521383 scopus 로고
    • Effects of acetylcholine on the turnover of phosphoryl units in individual phospholipids of pancreas slices and brain cortex slices
    • Hokin L.E., Hokin M.R. Effects of acetylcholine on the turnover of phosphoryl units in individual phospholipids of pancreas slices and brain cortex slices. Biochim. Biophys. Acta 1955, 18:102-110.
    • (1955) Biochim. Biophys. Acta , vol.18 , pp. 102-110
    • Hokin, L.E.1    Hokin, M.R.2
  • 16
    • 0000952205 scopus 로고
    • The incorporation of 32P from[32P]ATP into polyphosphoinositides and phosphatidic acid in erythrocyte membranes
    • Hokin L.E., Hokin M.R. The incorporation of 32P from[32P]ATP into polyphosphoinositides and phosphatidic acid in erythrocyte membranes. Biochim. Biophys. Acta 1964, 84:563-575.
    • (1964) Biochim. Biophys. Acta , vol.84 , pp. 563-575
    • Hokin, L.E.1    Hokin, M.R.2
  • 17
    • 33750264683 scopus 로고    scopus 로고
    • Phosphatidylinositol transfer proteins and cellular nanoreactors for lipid signaling
    • Ile K.E., Schaaf G., Bankaitis V.A. Phosphatidylinositol transfer proteins and cellular nanoreactors for lipid signaling. Nat. Chem. Biol. 2006, 2:576-583.
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 576-583
    • Ile, K.E.1    Schaaf, G.2    Bankaitis, V.A.3
  • 20
    • 80755129133 scopus 로고    scopus 로고
    • A highly dynamic ER-derived phosphatidylinositol-synthesizing organelle supplies phosphoinositides to cellular membranes
    • Kim Y.J., Guzman-Hernandez M.L., Balla T. A highly dynamic ER-derived phosphatidylinositol-synthesizing organelle supplies phosphoinositides to cellular membranes. Dev. Cell 2011, 21:813-824.
    • (2011) Dev. Cell , vol.21 , pp. 813-824
    • Kim, Y.J.1    Guzman-Hernandez, M.L.2    Balla, T.3
  • 21
    • 84885312590 scopus 로고    scopus 로고
    • The phosphatidylinositol-transfer protein Nir2 binds phosphatidic acid and positively regulates phosphoinositide signalling
    • Kim S., Kedan A., Marom M., Gavert N., Keinan O., Selitrennik M., Laufman O., Lev S. The phosphatidylinositol-transfer protein Nir2 binds phosphatidic acid and positively regulates phosphoinositide signalling. EMBO Rep. 2013, 14:891-899.
    • (2013) EMBO Rep. , vol.14 , pp. 891-899
    • Kim, S.1    Kedan, A.2    Marom, M.3    Gavert, N.4    Keinan, O.5    Selitrennik, M.6    Laufman, O.7    Lev, S.8
  • 22
    • 84878120585 scopus 로고    scopus 로고
    • Inositol lipid regulation of lipid transfer in specialized membrane domains
    • Kim Y.J., Hernandez M.L., Balla T. Inositol lipid regulation of lipid transfer in specialized membrane domains. Trends Cell Biol. 2013, 23:270-278.
    • (2013) Trends Cell Biol. , vol.23 , pp. 270-278
    • Kim, Y.J.1    Hernandez, M.L.2    Balla, T.3
  • 23
    • 84867619217 scopus 로고    scopus 로고
    • Nonvesicular lipid transfer from the endoplasmic reticulum
    • Lev S. Nonvesicular lipid transfer from the endoplasmic reticulum. Cold Spring Harb. Perspect. Biol. 2012, 4:a013300.
    • (2012) Cold Spring Harb. Perspect. Biol. , vol.4
    • Lev, S.1
  • 25
    • 0035834805 scopus 로고    scopus 로고
    • The mammalian retinal degeneration B2 gene is not required for photoreceptor function and survival
    • Lu C., Peng Y.W., Shang J., Pawlyk B.S., Yu F., Li T. The mammalian retinal degeneration B2 gene is not required for photoreceptor function and survival. Neuroscience 2001, 107:35-41.
    • (2001) Neuroscience , vol.107 , pp. 35-41
    • Lu, C.1    Peng, Y.W.2    Shang, J.3    Pawlyk, B.S.4    Yu, F.5    Li, T.6
  • 26
    • 0025726337 scopus 로고
    • Phosphatidylinositol synthase and phosphatidylinositol/inositol exchange reactions in turkey erythrocyte membranes
    • McPhee F., Lowe G., Vaziri C., Downes C.P. Phosphatidylinositol synthase and phosphatidylinositol/inositol exchange reactions in turkey erythrocyte membranes. Biochem. J. 1991, 275:187-192.
    • (1991) Biochem. J. , vol.275 , pp. 187-192
    • McPhee, F.1    Lowe, G.2    Vaziri, C.3    Downes, C.P.4
  • 27
    • 84887957821 scopus 로고    scopus 로고
    • A four-step cycle driven by PI(4)P hydrolysis directs sterol/PI(4)P exchange by the ER-Golgi tether OSBP
    • Mesmin B., Bigay J., Moser von Filseck J., Lacas-Gervais S., Drin G., Antonny B. A four-step cycle driven by PI(4)P hydrolysis directs sterol/PI(4)P exchange by the ER-Golgi tether OSBP. Cell 2013, 155:830-843.
    • (2013) Cell , vol.155 , pp. 830-843
    • Mesmin, B.1    Bigay, J.2    Moser von Filseck, J.3    Lacas-Gervais, S.4    Drin, G.5    Antonny, B.6
  • 28
    • 0030806560 scopus 로고    scopus 로고
    • The phosphatidylinositol transfer protein domain of Drosophila retinal degeneration B protein is essential for photoreceptor cell survival and recovery from light stimulation
    • Milligan S.C., Alb J.G., Elagina R.B., Bankaitis V.A., Hyde D.R. The phosphatidylinositol transfer protein domain of Drosophila retinal degeneration B protein is essential for photoreceptor cell survival and recovery from light stimulation. J.Cell Biol. 1997, 139:351-363.
    • (1997) J.Cell Biol. , vol.139 , pp. 351-363
    • Milligan, S.C.1    Alb, J.G.2    Elagina, R.B.3    Bankaitis, V.A.4    Hyde, D.R.5
  • 30
    • 84875008586 scopus 로고    scopus 로고
    • Sec14 like PITPs couple lipid metabolism with phosphoinositide synthesis to regulate Golgi functionality
    • Mousley C.J., Davison J.M., Bankaitis V.A. Sec14 like PITPs couple lipid metabolism with phosphoinositide synthesis to regulate Golgi functionality. Subcell. Biochem. 2012, 59:271-287.
    • (2012) Subcell. Biochem. , vol.59 , pp. 271-287
    • Mousley, C.J.1    Davison, J.M.2    Bankaitis, V.A.3
  • 31
    • 0029015694 scopus 로고
    • A wortmannin-sensitive phosphatidylinositol 4-kinase that regulates hormone-sensitive pools of inositolphospholipids
    • Nakanishi S., Catt K.J., Balla T. A wortmannin-sensitive phosphatidylinositol 4-kinase that regulates hormone-sensitive pools of inositolphospholipids. Proc. Natl. Acad. Sci. USA 1995, 92:5317-5321.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5317-5321
    • Nakanishi, S.1    Catt, K.J.2    Balla, T.3
  • 32
    • 55549111249 scopus 로고    scopus 로고
    • Coordinated lipid transfer between the endoplasmic reticulum and the Golgi complex requires the VAP proteins and is essential for Golgi-mediated transport
    • Peretti D., Dahan N., Shimoni E., Hirschberg K., Lev S. Coordinated lipid transfer between the endoplasmic reticulum and the Golgi complex requires the VAP proteins and is essential for Golgi-mediated transport. Mol. Biol. Cell 2008, 19:3871-3884.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3871-3884
    • Peretti, D.1    Dahan, N.2    Shimoni, E.3    Hirschberg, K.4    Lev, S.5
  • 33
    • 78649967779 scopus 로고    scopus 로고
    • Lipid trafficking sans vesicles: where, why, how?
    • Prinz W.A. Lipid trafficking sans vesicles: where, why, how?. Cell 2010, 143:870-874.
    • (2010) Cell , vol.143 , pp. 870-874
    • Prinz, W.A.1
  • 34
    • 0027465670 scopus 로고
    • Lithium enhances muscarinic receptor-stimulated CDP-diacylglycerol formation in inositol-depleted SK-N-SH neuroblastoma cells
    • Stubbs E.B., Agranoff B.W. Lithium enhances muscarinic receptor-stimulated CDP-diacylglycerol formation in inositol-depleted SK-N-SH neuroblastoma cells. J.Neurochem. 1993, 60:1292-1299.
    • (1993) J.Neurochem. , vol.60 , pp. 1292-1299
    • Stubbs, E.B.1    Agranoff, B.W.2
  • 35
    • 0028484074 scopus 로고
    • Immunolocalization of a Drosophila phosphatidylinositol transfer protein (rdgB) in normal and rdgA mutant photoreceptor cells with special reference to the subrhabdomeric cisternae
    • Suzuki E., Hirosawa K. Immunolocalization of a Drosophila phosphatidylinositol transfer protein (rdgB) in normal and rdgA mutant photoreceptor cells with special reference to the subrhabdomeric cisternae. J.Electron Microsc. (Tokyo) 1994, 43:183-189.
    • (1994) J.Electron Microsc. (Tokyo) , vol.43 , pp. 183-189
    • Suzuki, E.1    Hirosawa, K.2
  • 36
    • 70449413105 scopus 로고    scopus 로고
    • Live cell imaging with protein domains capable of recognizing phosphatidylinositol 4,5-bisphosphate; a comparative study
    • Szentpetery Z., Balla A., Kim Y.J., Lemmon M.A., Balla T. Live cell imaging with protein domains capable of recognizing phosphatidylinositol 4,5-bisphosphate; a comparative study. BMC Cell Biol. 2009, 10:67.
    • (2009) BMC Cell Biol. , vol.10 , pp. 67
    • Szentpetery, Z.1    Balla, A.2    Kim, Y.J.3    Lemmon, M.A.4    Balla, T.5
  • 37
    • 34249787876 scopus 로고    scopus 로고
    • RdgB proteins: functions in lipid homeostasis and signal transduction
    • Trivedi D., Padinjat R. RdgB proteins: functions in lipid homeostasis and signal transduction. Biochim. Biophys. Acta 2007, 1771:692-699.
    • (2007) Biochim. Biophys. Acta , vol.1771 , pp. 692-699
    • Trivedi, D.1    Padinjat, R.2
  • 38
    • 0035805510 scopus 로고    scopus 로고
    • Monitoring agonist-induced phospholipase C activation in live cells by fluorescence resonance energy transfer
    • van Der Wal J., Habets R., Varnai P., Balla T., Jalink K. Monitoring agonist-induced phospholipase C activation in live cells by fluorescence resonance energy transfer. J.Biol. Chem. 2001, 276:15337-15344.
    • (2001) J.Biol. Chem. , vol.276 , pp. 15337-15344
    • van Der Wal, J.1    Habets, R.2    Varnai, P.3    Balla, T.4    Jalink, K.5
  • 39
    • 0027491222 scopus 로고
    • Direct labelling of hormone-sensitive phosphoinositides by a plasma-membrane-associated PtdIns synthase in turkey erythrocytes
    • Vaziri C., Downes C.P., Macfarlane S.C. Direct labelling of hormone-sensitive phosphoinositides by a plasma-membrane-associated PtdIns synthase in turkey erythrocytes. Biochem. J. 1993, 294:793-799.
    • (1993) Biochem. J. , vol.294 , pp. 793-799
    • Vaziri, C.1    Downes, C.P.2    Macfarlane, S.C.3
  • 40
    • 0025833537 scopus 로고
    • Isolation and characterization of the Drosophila retinal degeneration B (rdgB) gene
    • Vihtelic T.S., Hyde D.R., O'Tousa J.E. Isolation and characterization of the Drosophila retinal degeneration B (rdgB) gene. Genetics 1991, 127:761-768.
    • (1991) Genetics , vol.127 , pp. 761-768
    • Vihtelic, T.S.1    Hyde, D.R.2    O'Tousa, J.E.3
  • 41
    • 0027216545 scopus 로고
    • Localization of Drosophila retinal degeneration B, a membrane-associated phosphatidylinositol transfer protein
    • Vihtelic T.S., Goebl M., Milligan S., O'Tousa J.E., Hyde D.R. Localization of Drosophila retinal degeneration B, a membrane-associated phosphatidylinositol transfer protein. J.Cell Biol. 1993, 122:1013-1022.
    • (1993) J.Cell Biol. , vol.122 , pp. 1013-1022
    • Vihtelic, T.S.1    Goebl, M.2    Milligan, S.3    O'Tousa, J.E.4    Hyde, D.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.