메뉴 건너뛰기




Volumn 4, Issue 3, 2014, Pages 302-318

Role of phospholipase D in G-protein coupled receptor function

Author keywords

Desensitization; Endocytosis; G protein coupled receptor; Internalization; Phospholipase D; Recycling; Resensitization

Indexed keywords

ENZYME ACTIVITY; MAMMALS; MOLECULAR BIOLOGY; NEURODEGENERATIVE DISEASES; PHOSPHOLIPIDS; RECYCLING;

EID: 84903881297     PISSN: None     EISSN: 20770375     Source Type: Journal    
DOI: 10.3390/membranes4030302     Document Type: Review
Times cited : (20)

References (103)
  • 2
    • 0015785399 scopus 로고
    • Solubilization and properties of a membrane-bound enzyme from rat brain catalyzing a base-exchange reaction
    • Saito, M.; Kanfer, J. Solubilization and properties of a membrane-bound enzyme from rat brain catalyzing a base-exchange reaction. Biochem. Biophys. Res. Commun. 1973, 53, 391-398.
    • (1973) Biochem. Biophys. Res. Commun. , vol.53 , pp. 391-398
    • Saito, M.1    Kanfer, J.2
  • 3
    • 0029564902 scopus 로고
    • Human adp-ribosylation factor-activated phosphatidylcholine-specific phospholipase d defines a new and highly conserved gene family
    • Hammond, S.M.; Altshuller, Y.M.; Sung, T.C.; Rudge, S.A.; Rose, K.; Engebrecht, J.; Morris, A.J.; Frohman, M.A. Human adp-ribosylation factor-activated phosphatidylcholine-specific phospholipase d defines a new and highly conserved gene family. J. Biol. Chem. 1995, 270, 29640-29643.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29640-29643
    • Hammond, S.M.1    Altshuller, Y.M.2    Sung, T.C.3    Rudge, S.A.4    Rose, K.5    Engebrecht, J.6    Morris, A.J.7    Frohman, M.A.8
  • 4
    • 0008855384 scopus 로고    scopus 로고
    • Characterization of two alternately spliced forms of phospholipase d1. Activation of the purified enzymes by phosphatidylinositol 4, 5-bisphosphate, adp-ribosylation factor, and rho family monomeric gtp-binding proteins and protein kinase c-alpha
    • Hammond, S.M.; Jenco, J.M.; Nakashima, S.; Cadwallader, K.; Gu, Q.; Cook, S.; Nozawa, Y.; Prestwich, G.D.; Frohman, M.A.; Morris, A.J.; et al. Characterization of two alternately spliced forms of phospholipase d1. Activation of the purified enzymes by phosphatidylinositol 4, 5-bisphosphate, adp-ribosylation factor, and rho family monomeric gtp-binding proteins and protein kinase c-alpha. J. Biol. Chem. 1997, 272, 3860-3868.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3860-3868
    • Hammond, S.M.1    Jenco, J.M.2    Nakashima, S.3    Cadwallader, K.4    Gu, Q.5    Cook, S.6    Nozawa, Y.7    Prestwich, G.D.8    Frohman, M.A.9    Morris, A.J.10
  • 5
    • 0031670386 scopus 로고    scopus 로고
    • Characterization of human pld2 and the analysis of pld isoform splice variants
    • Steed, P.M.; Clark, K.L.; Boyar, W.C.; Lasala, D.J. Characterization of human pld2 and the analysis of pld isoform splice variants. FASEB J. 1998, 12, 1309-1317.
    • (1998) FASEB J. , vol.12 , pp. 1309-1317
    • Steed, P.M.1    Clark, K.L.2    Boyar, W.C.3    Lasala, D.J.4
  • 6
    • 0032474821 scopus 로고    scopus 로고
    • Phospholipase d1 localises to secretory granules and lysosomes and is plasma-membrane translocated on cellular stimulation
    • Brown, F.D.; Thompson, N.; Saqib, K.M.; Clark, J.M.; Powner, D.; Thompson, N.T.; Solari, R.; Wakelam, M.J. Phospholipase d1 localises to secretory granules and lysosomes and is plasma-membrane translocated on cellular stimulation. Curr. Biol. CB 1998, 8, 835-838.
    • (1998) Curr. Biol. CB , vol.8 , pp. 835-838
    • Brown, F.D.1    Thompson, N.2    Saqib, K.M.3    Clark, J.M.4    Powner, D.5    Thompson, N.T.6    Solari, R.7    Wakelam, M.J.8
  • 8
    • 0035875158 scopus 로고    scopus 로고
    • Endosomal localization of phospholipase d 1a and 1b is defined by the c-termini of the proteins, and is independent of activity
    • Hughes, W.E.; Parker, P.J. Endosomal localization of phospholipase d 1a and 1b is defined by the c-termini of the proteins, and is independent of activity. Biochem. J. 2001, 356, 727-736.
    • (2001) Biochem. J. , vol.356 , pp. 727-736
    • Hughes, W.E.1    Parker, P.J.2
  • 9
    • 0033613943 scopus 로고    scopus 로고
    • Localization of phospholipase d in detergent-insoluble, caveolin-rich membrane domains. Modulation by caveolin-1 expression and caveolin-182-101
    • Czarny, M.; Lavie, Y.; Fiucci, G.; Liscovitch, M. Localization of phospholipase d in detergent-insoluble, caveolin-rich membrane domains. Modulation by caveolin-1 expression and caveolin-182-101. J. Biol. Chem. 1999, 274, 2717-2724.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2717-2724
    • Czarny, M.1    Lavie, Y.2    Fiucci, G.3    Liscovitch, M.4
  • 11
    • 80054069569 scopus 로고    scopus 로고
    • Phospholipase d: Enzymology, functionality, and chemical modulation
    • Selvy, P.E.; Lavieri, R.R.; Lindsley, C.W.; Brown, H.A. Phospholipase d: Enzymology, functionality, and chemical modulation. Chem. Rev. 2011, 111, 6064-6119.
    • (2011) Chem. Rev. , vol.111 , pp. 6064-6119
    • Selvy, P.E.1    Lavieri, R.R.2    Lindsley, C.W.3    Brown, H.A.4
  • 12
    • 0028139294 scopus 로고
    • Effect of interleukin 1, lipopolysaccharide and phorbol esters on phospholipase d activity in chondrocytes
    • Conquer, J.A.; Jones, S.A.; Cruz, T.F. Effect of interleukin 1, lipopolysaccharide and phorbol esters on phospholipase d activity in chondrocytes. Osteoarthr. Cartil. OARS Osteoarthr. Res. Soc. 1994, 2, 269-273.
    • (1994) Osteoarthr. Cartil. OARS Osteoarthr. Res. Soc. , vol.2 , pp. 269-273
    • Conquer, J.A.1    Jones, S.A.2    Cruz, T.F.3
  • 13
    • 0029921149 scopus 로고    scopus 로고
    • A novel family of phospholipase d homologues that includes phospholipid synthases and putative endonucleases: Identification of duplicated repeats and potential active site residues
    • Ponting, C.P.; Kerr, I.D. A novel family of phospholipase d homologues that includes phospholipid synthases and putative endonucleases: Identification of duplicated repeats and potential active site residues. Protein Sci. 1996, 5, 914-922.
    • (1996) Protein Sci. , vol.5 , pp. 914-922
    • Ponting, C.P.1    Kerr, I.D.2
  • 14
    • 0030803536 scopus 로고    scopus 로고
    • Mutagenesis of phospholipase d defines a superfamily including a trans-golgi viral protein required for poxvirus pathogenicity
    • Sung, T.C.; Roper, R.L.; Zhang, Y.; Rudge, S.A.; Temel, R.; Hammond, S.M.; Morris, A.J.; Moss, B.; Engebrecht, J.; Frohman, M.A.; et al. Mutagenesis of phospholipase d defines a superfamily including a trans-golgi viral protein required for poxvirus pathogenicity. EMBO J. 1997, 16, 4519-4530.
    • (1997) EMBO J. , vol.16 , pp. 4519-4530
    • Sung, T.C.1    Roper, R.L.2    Zhang, Y.3    Rudge, S.A.4    Temel, R.5    Hammond, S.M.6    Morris, A.J.7    Moss, B.8    Engebrecht, J.9    Frohman, M.A.10
  • 15
    • 0037164869 scopus 로고    scopus 로고
    • Dual role for phosphoinositides in regulation of yeast and mammalian phospholipase d enzymes
    • Sciorra, V.A.; Rudge, S.A.; Wang, J.; McLaughlin, S.; Engebrecht, J.; Morris, A.J. Dual role for phosphoinositides in regulation of yeast and mammalian phospholipase d enzymes. J. Cell Biol. 2002, 159, 1039-1049.
    • (2002) J. Cell Biol. , vol.159 , pp. 1039-1049
    • Sciorra, V.A.1    Rudge, S.A.2    Wang, J.3    McLaughlin, S.4    Engebrecht, J.5    Morris, A.J.6
  • 18
    • 0033231049 scopus 로고    scopus 로고
    • Identification of a phosphoinositide binding motif that mediates activation of mammalian and yeast phospholipase d isoenzymes
    • Sciorra, V.A.; Rudge, S.A.; Prestwich, G.D.; Frohman, M.A.; Engebrecht, J.; Morris, A.J. Identification of a phosphoinositide binding motif that mediates activation of mammalian and yeast phospholipase d isoenzymes. EMBO J. 1999, 18, 5911-5921.
    • (1999) EMBO J. , vol.18 , pp. 5911-5921
    • Sciorra, V.A.1    Rudge, S.A.2    Prestwich, G.D.3    Frohman, M.A.4    Engebrecht, J.5    Morris, A.J.6
  • 21
    • 55049140159 scopus 로고    scopus 로고
    • Differential regulation of apoptosis by caspase-mediated cleavage of phospholipase d isozymes
    • Jang, Y.H.; Ahn, B.H.; Namkoong, S.; Kim, Y.M.; Jin, J.K.; Kim, Y.S.; Min do, S. Differential regulation of apoptosis by caspase-mediated cleavage of phospholipase d isozymes. Cell. Signal. 2008, 20, 2198-2207.
    • (2008) Cell. Signal. , vol.20 , pp. 2198-2207
    • Jang, Y.H.1    Ahn, B.H.2    Namkoong, S.3    Kim, Y.M.4    Jin, J.K.5    Kim, Y.S.6    do Min, S.7
  • 22
    • 77951534832 scopus 로고    scopus 로고
    • Dependence of phospholipase d1 multi-monoubiquitination on its enzymatic activity and palmitoylation
    • Yin, H.; Gui, Y.; Du, G.; Frohman, M.A.; Zheng, X.L. Dependence of phospholipase d1 multi-monoubiquitination on its enzymatic activity and palmitoylation. J. Biol. Chem. 2010, 285, 13580-13588.
    • (2010) J. Biol. Chem. , vol.285 , pp. 13580-13588
    • Yin, H.1    Gui, Y.2    Du, G.3    Frohman, M.A.4    Zheng, X.L.5
  • 23
    • 23644455714 scopus 로고    scopus 로고
    • Phospholipase d: A lipid centric review
    • Jenkins, G.M.; Frohman, M.A. Phospholipase d: A lipid centric review. Cell. Mol. Life Sci 2005, 62, 2305-2316.
    • (2005) Cell. Mol. Life Sci , vol.62 , pp. 2305-2316
    • Jenkins, G.M.1    Frohman, M.A.2
  • 24
    • 0014945183 scopus 로고
    • On the mechanism of enzymatic phosphatidylation. Biosynthesis of cardiolipin catalyzed by phospholipase d
    • Stanacev, N.Z.; Stuhne-Sekalec, L. On the mechanism of enzymatic phosphatidylation. Biosynthesis of cardiolipin catalyzed by phospholipase d. Biochim. Biophys. Acta 1970, 210, 350-352.
    • (1970) Biochim. Biophys. Acta , vol.210 , pp. 350-352
    • Stanacev, N.Z.1    Stuhne-Sekalec, L.2
  • 25
    • 0029186775 scopus 로고
    • The measurement of phospholipase d-linked signaling in cells
    • Wakelam, M.J.; Hodgkin, M.; Martin, A. The measurement of phospholipase d-linked signaling in cells. Methods Mol. Biol. 1995, 41, 271-278.
    • (1995) Methods Mol. Biol. , vol.41 , pp. 271-278
    • Wakelam, M.J.1    Hodgkin, M.2    Martin, A.3
  • 26
    • 0032810278 scopus 로고    scopus 로고
    • Mammalian phospholipase d structure and regulation
    • Frohman, M.A.; Sung, T.C.; Morris, A.J. Mammalian phospholipase d structure and regulation. Biochim. Biophys. Acta 1999, 1439, 175-186.
    • (1999) Biochim. Biophys. Acta , vol.1439 , pp. 175-186
    • Frohman, M.A.1    Sung, T.C.2    Morris, A.J.3
  • 27
    • 33645651306 scopus 로고    scopus 로고
    • Kinetic analysis of a mammalian phospholipase d: Allosteric modulation by monomeric gtpases, protein kinase c, and polyphosphoinositides
    • Henage, L.G.; Exton, J.H.; Brown, H.A. Kinetic analysis of a mammalian phospholipase d: Allosteric modulation by monomeric gtpases, protein kinase c, and polyphosphoinositides. J. Biol. Chem. 2006, 281, 3408-3417.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3408-3417
    • Henage, L.G.1    Exton, J.H.2    Brown, H.A.3
  • 28
    • 0027953550 scopus 로고
    • Dominant inhibitory mutants of arf1 block endoplasmic reticulum to golgi transport and trigger disassembly of the golgi apparatus
    • Dascher, C.; Balch, W.E. Dominant inhibitory mutants of arf1 block endoplasmic reticulum to golgi transport and trigger disassembly of the golgi apparatus. J. Biol. Chem. 1994, 269, 1437-1448.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1437-1448
    • Dascher, C.1    Balch, W.E.2
  • 29
    • 0032514906 scopus 로고    scopus 로고
    • Adp-ribosylation factor proteins mediate agonist-induced activation of phospholipase d
    • Shome, K.; Nie, Y.; Romero, G. Adp-ribosylation factor proteins mediate agonist-induced activation of phospholipase d. J. Biol. Chem. 1998, 273, 30836-30841.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30836-30841
    • Shome, K.1    Nie, Y.2    Romero, G.3
  • 30
    • 79955546947 scopus 로고    scopus 로고
    • Evidence for two crib domains in phospholipase d2 (pld2) that the enzyme uses to specifically bind to the small gtpase rac2
    • Peng, H.J.; Henkels, K.M.; Mahankali, M.; Dinauer, M.C.; Gomez-Cambronero, J. Evidence for two crib domains in phospholipase d2 (pld2) that the enzyme uses to specifically bind to the small gtpase rac2. J. Biol. Chem. 2011, 286, 16308-16320.
    • (2011) J. Biol. Chem. , vol.286 , pp. 16308-16320
    • Peng, H.J.1    Henkels, K.M.2    Mahankali, M.3    Dinauer, M.C.4    Gomez-Cambronero, J.5
  • 31
    • 16844366239 scopus 로고    scopus 로고
    • Evidence for rho-mediated agonist stimulation of phospholipase d in rat1 fibroblasts. Effects of clostridium botulinum c3 exoenzyme
    • Malcolm, K.C.; Elliott, C.M.; Exton, J.H. Evidence for rho-mediated agonist stimulation of phospholipase d in rat1 fibroblasts. Effects of clostridium botulinum c3 exoenzyme. J. Biol. Chem. 1996, 271, 13135-13139.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13135-13139
    • Malcolm, K.C.1    Elliott, C.M.2    Exton, J.H.3
  • 32
    • 0028177567 scopus 로고
    • Protein kinase c alpha mediates phospholipase d activation by nucleotides and phorbol ester in madin-darby canine kidney cells. Stimulation of phospholipase d is independent of activation of polyphosphoinositide-specific phospholipase c and phospholipase a2
    • Balboa, M.A.; Firestein, B.L.; Godson, C.; Bell, K.S.; Insel, P.A. Protein kinase c alpha mediates phospholipase d activation by nucleotides and phorbol ester in madin-darby canine kidney cells. Stimulation of phospholipase d is independent of activation of polyphosphoinositide-specific phospholipase c and phospholipase a2. J. Biol. Chem. 1994, 269, 10511-10516.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10511-10516
    • Balboa, M.A.1    Firestein, B.L.2    Godson, C.3    Bell, K.S.4    Insel, P.A.5
  • 33
    • 0026011097 scopus 로고
    • Overexpression of protein kinase c beta 1 enhances phospholipase d activity and diacylglycerol formation in phorbol ester-stimulated rat fibroblasts
    • Pai, J.K.; Pachter, J.A.; Weinstein, I.B.; Bishop, W.R. Overexpression of protein kinase c beta 1 enhances phospholipase d activity and diacylglycerol formation in phorbol ester-stimulated rat fibroblasts. Proc. Natl. Acad. Sci. USA 1991, 88, 598-602.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 598-602
    • Pai, J.K.1    Pachter, J.A.2    Weinstein, I.B.3    Bishop, W.R.4
  • 34
    • 2542495782 scopus 로고    scopus 로고
    • Regulation of phospholipase d2 activity by protein kinase c alpha
    • Chen, J.S.; Exton, J.H. Regulation of phospholipase d2 activity by protein kinase c alpha. J. Biol. Chem. 2004, 279, 22076-22083.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22076-22083
    • Chen, J.S.1    Exton, J.H.2
  • 35
    • 0040737600 scopus 로고    scopus 로고
    • Phosphorylation and activation of phospholipase d1 by protein kinase c in vivo: Determination of multiple phosphorylation sites
    • Kim, Y.; Han, J.M.; Park, J.B.; Lee, S.D.; Oh, Y.S.; Chung, C.; Lee, T.G.; Kim, J.H.; Park, S.K.; Yoo, J.S.; et al. Phosphorylation and activation of phospholipase d1 by protein kinase c in vivo: Determination of multiple phosphorylation sites. Biochemistry 1999, 38, 10344-10351.
    • (1999) Biochemistry , vol.38 , pp. 10344-10351
    • Kim, Y.1    Han, J.M.2    Park, J.B.3    Lee, S.D.4    Oh, Y.S.5    Chung, C.6    Lee, T.G.7    Kim, J.H.8    Park, S.K.9    Yoo, J.S.10
  • 36
    • 23944499618 scopus 로고    scopus 로고
    • Identification of interaction sites of protein kinase calpha on phospholipase d1
    • Kook, S.; Exton, J.H. Identification of interaction sites of protein kinase calpha on phospholipase d1. Cell. Signal. 2005, 17, 1423-1432.
    • (2005) Cell. Signal. , vol.17 , pp. 1423-1432
    • Kook, S.1    Exton, J.H.2
  • 38
    • 0032557449 scopus 로고    scopus 로고
    • Cloning and initial characterization of a human phospholipase d2 (HPLD2). Adp-ribosylation factor regulates HPLD2
    • Lopez, I.; Arnold, R.S.; Lambeth, J.D. Cloning and initial characterization of a human phospholipase d2 (HPLD2). Adp-ribosylation factor regulates HPLD2. J. Biol. Chem. 1998, 273, 12846-12852.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12846-12852
    • Lopez, I.1    Arnold, R.S.2    Lambeth, J.D.3
  • 40
    • 84871887002 scopus 로고    scopus 로고
    • Molecular mechanisms of n-formyl-methionyl-leucyl-phenylalanine-induced superoxide generation and degranulation in mouse neutrophils: Phospholipase d is dispensable
    • Sato, T.; Hongu, T.; Sakamoto, M.; Funakoshi, Y.; Kanaho, Y. Molecular mechanisms of n-formyl-methionyl-leucyl-phenylalanine-induced superoxide generation and degranulation in mouse neutrophils: Phospholipase d is dispensable. Mol. Cell. Biol. 2013, 33, 136-145.
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 136-145
    • Sato, T.1    Hongu, T.2    Sakamoto, M.3    Funakoshi, Y.4    Kanaho, Y.5
  • 41
    • 0035957056 scopus 로고    scopus 로고
    • Potent direct inhibition of mammalian phospholipase d isoenzymes by calphostin-c
    • Sciorra, V.A.; Hammond, S.M.; Morris, A.J. Potent direct inhibition of mammalian phospholipase d isoenzymes by calphostin-c. Biochemistry 2001, 40, 2640-2646.
    • (2001) Biochemistry , vol.40 , pp. 2640-2646
    • Sciorra, V.A.1    Hammond, S.M.2    Morris, A.J.3
  • 44
    • 0033635117 scopus 로고    scopus 로고
    • Dual requirement for rho and protein kinase c in direct activation of phospholipase d1 through G protein-coupled receptor signaling
    • Du, G.; Altshuller, Y.M.; Kim, Y.; Han, J.M.; Ryu, S.H.; Morris, A.J.; Frohman, M.A. Dual requirement for rho and protein kinase c in direct activation of phospholipase d1 through G protein-coupled receptor signaling. Mol. Biol. Cell 2000, 11, 4359-4368.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4359-4368
    • Du, G.1    Altshuller, Y.M.2    Kim, Y.3    Han, J.M.4    Ryu, S.H.5    Morris, A.J.6    Frohman, M.A.7
  • 45
    • 0141925648 scopus 로고    scopus 로고
    • Involvement of phospholipase d2 in lysophosphatidate-induced transactivation of platelet-derived growth factor receptor-beta in human bronchial epithelial cells
    • Wang, L.; Cummings, R.; Zhao, Y.; Kazlauskas, A.; Sham, J.K.; Morris, A.; Georas, S.; Brindley, D.N.; Natarajan, V. Involvement of phospholipase d2 in lysophosphatidate-induced transactivation of platelet-derived growth factor receptor-beta in human bronchial epithelial cells. J. Biol. Chem. 2003, 278, 39931-39940.
    • (2003) J. Biol. Chem. , vol.278 , pp. 39931-39940
    • Wang, L.1    Cummings, R.2    Zhao, Y.3    Kazlauskas, A.4    Sham, J.K.5    Morris, A.6    Georas, S.7    Brindley, D.N.8    Natarajan, V.9
  • 46
    • 0038322031 scopus 로고    scopus 로고
    • Adp-ribosylation factor-dependent phospholipase d2 activation is required for agonist-induced mu-opioid receptor endocytosis
    • Koch, T.; Brandenburg, L.O.; Schulz, S.; Liang, Y.; Klein, J.; Hollt, V. Adp-ribosylation factor-dependent phospholipase d2 activation is required for agonist-induced mu-opioid receptor endocytosis. J. Biol. Chem. 2003, 278, 9979-9985.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9979-9985
    • Koch, T.1    Brandenburg, L.O.2    Schulz, S.3    Liang, Y.4    Klein, J.5    Hollt, V.6
  • 47
    • 38449115036 scopus 로고    scopus 로고
    • Role of receptor internalization in the agonist-induced desensitization of cannabinoid type 1 receptors
    • Wu, D.F.; Yang, L.Q.; Goschke, A.; Stumm, R.; Brandenburg, L.O.; Liang, Y.J.; Hollt, V.; Koch, T. Role of receptor internalization in the agonist-induced desensitization of cannabinoid type 1 receptors. J. Neurochem. 2008, 104, 1132-1143.
    • (2008) J. Neurochem. , vol.104 , pp. 1132-1143
    • Wu, D.F.1    Yang, L.Q.2    Goschke, A.3    Stumm, R.4    Brandenburg, L.O.5    Liang, Y.J.6    Hollt, V.7    Koch, T.8
  • 48
    • 34247336402 scopus 로고    scopus 로고
    • Internalization of PRP106-126 by the formyl-peptide-receptor-like-1 in glial cells
    • Brandenburg, L.O.; Koch, T.; Sievers, J.; Lucius, R. Internalization of PRP106-126 by the formyl-peptide-receptor-like-1 in glial cells. J. Neurochem. 2007, 101, 718-728.
    • (2007) J. Neurochem. , vol.101 , pp. 718-728
    • Brandenburg, L.O.1    Koch, T.2    Sievers, J.3    Lucius, R.4
  • 49
    • 0033931920 scopus 로고    scopus 로고
    • The d2s dopamine receptor stimulates phospholipase d activity: A novel signaling pathway for dopamine
    • Senogles, S.E. The d2s dopamine receptor stimulates phospholipase d activity: A novel signaling pathway for dopamine. Mol. Pharmacol. 2000, 58, 455-462.
    • (2000) Mol. Pharmacol. , vol.58 , pp. 455-462
    • Senogles, S.E.1
  • 50
    • 0037119432 scopus 로고    scopus 로고
    • Phospholipase d activation by sphingosine 1-phosphate regulates interleukin-8 secretion in human bronchial epithelial cells
    • Cummings, R.J.; Parinandi, N.L.; Zaiman, A.; Wang, L.; Usatyuk, P.V.; Garcia, J.G.; Natarajan, V. Phospholipase d activation by sphingosine 1-phosphate regulates interleukin-8 secretion in human bronchial epithelial cells. J. Biol. Chem. 2002, 277, 30227-30235.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30227-30235
    • Cummings, R.J.1    Parinandi, N.L.2    Zaiman, A.3    Wang, L.4    Usatyuk, P.V.5    Garcia, J.G.6    Natarajan, V.7
  • 51
    • 0035987146 scopus 로고    scopus 로고
    • Signalling components involved in the coupling of alpha 1-adrenoceptors to phospholipase d in neonatal rat cardiac myocytes
    • Gosau, N.; Fahimi-Vahid, M.; Michalek, C.; Schmidt, M.; Wieland, T. Signalling components involved in the coupling of alpha 1-adrenoceptors to phospholipase d in neonatal rat cardiac myocytes. Naunyn-Schmiedeberg's Arch. Pharmacol. 2002, 365, 468-476.
    • (2002) Naunyn-Schmiedeberg's Arch. Pharmacol. , vol.365 , pp. 468-476
    • Gosau, N.1    Fahimi-Vahid, M.2    Michalek, C.3    Schmidt, M.4    Wieland, T.5
  • 52
    • 0034529457 scopus 로고    scopus 로고
    • Phospholipase D in rat myometrium: Occurrence of a membrane-bound ARF6 (ADP-ribosylation factor 6)-regulated activity controlled by betagamma subunits of heterotrimeric G-proteins
    • Le Stunff, H.; Dokhac, L.; Bourgoin, S.; Bader, M.F.; Harbon, S. Phospholipase D in rat myometrium: Occurrence of a membrane-bound ARF6 (ADP-ribosylation factor 6)-regulated activity controlled by betagamma subunits of heterotrimeric G-proteins. Biochem. J. 2000, 352 Pt 2, 491-499.
    • (2000) Biochem. J. , vol.352 , Issue.PART 2 , pp. 491-499
    • Le Stunff, H.1    Dokhac, L.2    Bourgoin, S.3    Bader, M.F.4    Harbon, S.5
  • 54
    • 0032570827 scopus 로고    scopus 로고
    • The alpha-subunit of the heterotrimeric g protein g13 activates a phospholipase d isozyme by a pathway requiring rho family gtpases
    • Plonk, S.G.; Park, S.K.; Exton, J.H. The alpha-subunit of the heterotrimeric g protein g13 activates a phospholipase d isozyme by a pathway requiring rho family gtpases. J. Biol. Chem. 1998, 273, 4823-4826.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4823-4826
    • Plonk, S.G.1    Park, S.K.2    Exton, J.H.3
  • 55
    • 0031724592 scopus 로고    scopus 로고
    • Identification of a family of sorting nexin molecules and characterization of their association with receptors
    • Haft, C.R.; de la Luz Sierra, M.; Barr, V.A.; Haft, D.H.; Taylor, S.I. Identification of a family of sorting nexin molecules and characterization of their association with receptors. Mol. Cell. Biol. 1998, 18, 7278-7287.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7278-7287
    • Haft, C.R.1    de la Luz Sierra, M.2    Barr, V.A.3    Haft, D.H.4    Taylor, S.I.5
  • 56
    • 0035895878 scopus 로고    scopus 로고
    • Identification and characterization of snx15, a novel sorting nexin involved in protein trafficking
    • Phillips, S.A.; Barr, V.A.; Haft, D.H.; Taylor, S.I.; Haft, C.R. Identification and characterization of snx15, a novel sorting nexin involved in protein trafficking. J. Biol. Chem. 2001, 276, 5074-5084.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5074-5084
    • Phillips, S.A.1    Barr, V.A.2    Haft, D.H.3    Taylor, S.I.4    Haft, C.R.5
  • 57
    • 18444375296 scopus 로고    scopus 로고
    • Sustained diacylglycerol accumulation resulting from prolonged g protein-coupled receptor agonist-induced phosphoinositide breakdown in hepatocytes
    • Nilssen, L.S.; Dajani, O.; Christoffersen, T.; Sandnes, D. Sustained diacylglycerol accumulation resulting from prolonged g protein-coupled receptor agonist-induced phosphoinositide breakdown in hepatocytes. J. Cell. Biochem. 2005, 94, 389-402.
    • (2005) J. Cell. Biochem. , vol.94 , pp. 389-402
    • Nilssen, L.S.1    Dajani, O.2    Christoffersen, T.3    Sandnes, D.4
  • 58
    • 0034604717 scopus 로고    scopus 로고
    • The recruitment of raf-1 to membranes is mediated by direct interaction with phosphatidic acid and is independent of association with ras
    • Rizzo, M.A.; Shome, K.; Watkins, S.C.; Romero, G. The recruitment of raf-1 to membranes is mediated by direct interaction with phosphatidic acid and is independent of association with ras. J. Biol. Chem. 2000, 275, 23911-23918.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23911-23918
    • Rizzo, M.A.1    Shome, K.2    Watkins, S.C.3    Romero, G.4
  • 59
    • 80051802020 scopus 로고    scopus 로고
    • Raf kinases in cancer-roles and therapeutic opportunities
    • Maurer, G.; Tarkowski, B.; Baccarini, M. Raf kinases in cancer-roles and therapeutic opportunities. Oncogene 2011, 30, 3477-3488.
    • (2011) Oncogene , vol.30 , pp. 3477-3488
    • Maurer, G.1    Tarkowski, B.2    Baccarini, M.3
  • 60
    • 0033597867 scopus 로고    scopus 로고
    • Phosphatidic acid is a potent and selective inhibitor of protein phosphatase 1 and an inhibitor of ceramide-mediated responses
    • Kishikawa, K.; Chalfant, C.E.; Perry, D.K.; Bielawska, A.; Hannun, Y.A. Phosphatidic acid is a potent and selective inhibitor of protein phosphatase 1 and an inhibitor of ceramide-mediated responses. J. Biol. Chem. 1999, 274, 21335-21341.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21335-21341
    • Kishikawa, K.1    Chalfant, C.E.2    Perry, D.K.3    Bielawska, A.4    Hannun, Y.A.5
  • 61
    • 4043171462 scopus 로고    scopus 로고
    • Upstream and downstream of mtor
    • Hay, N.; Sonenberg, N. Upstream and downstream of mtor. Genes Dev. 2004, 18, 1926-1945.
    • (2004) Genes Dev. , vol.18 , pp. 1926-1945
    • Hay, N.1    Sonenberg, N.2
  • 62
    • 84878252749 scopus 로고    scopus 로고
    • Phosphatidic acid and lipid-sensing by mtor
    • Foster, D.A. Phosphatidic acid and lipid-sensing by mtor. Trends Endocrinol. Metab. 2013, 24, 272-278.
    • (2013) Trends Endocrinol. Metab. , vol.24 , pp. 272-278
    • Foster, D.A.1
  • 63
    • 84892657844 scopus 로고    scopus 로고
    • The role of diacylglycerol kinase zeta and phosphatidic acid in the mechanical activation of mammalian target of rapamycin (MTOR) signaling and skeletal muscle hypertrophy
    • You, J.S.; Lincoln, H.C.; Kim, C.R.; Frey, J.W.; Goodman, C.A.; Zhong, X.P.; Hornberger, T.A. The role of diacylglycerol kinase zeta and phosphatidic acid in the mechanical activation of mammalian target of rapamycin (MTOR) signaling and skeletal muscle hypertrophy. J. Biol. Chem. 2014, 289, 1551-1563.
    • (2014) J. Biol. Chem. , vol.289 , pp. 1551-1563
    • You, J.S.1    Lincoln, H.C.2    Kim, C.R.3    Frey, J.W.4    Goodman, C.A.5    Zhong, X.P.6    Hornberger, T.A.7
  • 64
    • 0028346383 scopus 로고
    • Type I phosphatidylinositol 4-phosphate 5-kinase isoforms are specifically stimulated by phosphatidic acid
    • Jenkins, G.H.; Fisette, P.L.; Anderson, R.A. Type I phosphatidylinositol 4-phosphate 5-kinase isoforms are specifically stimulated by phosphatidic acid. J. Biol. Chem. 1994, 269, 11547-11554.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11547-11554
    • Jenkins, G.H.1    Fisette, P.L.2    Anderson, R.A.3
  • 66
    • 0035159121 scopus 로고    scopus 로고
    • Role for phospholipase d in receptor-mediated endocytosis
    • Shen, Y.; Xu, L.; Foster, D.A. Role for phospholipase d in receptor-mediated endocytosis. Mol. Cell. Biol. 2001, 21, 595-602.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 595-602
    • Shen, Y.1    Xu, L.2    Foster, D.A.3
  • 67
    • 1542283816 scopus 로고    scopus 로고
    • Phospholipase d2 localizes to the plasma membrane and regulates angiotensin II receptor endocytosis
    • Du, G.; Huang, P.; Liang, B.T.; Frohman, M.A. Phospholipase d2 localizes to the plasma membrane and regulates angiotensin II receptor endocytosis. Mol. Biol. Cell 2004, 15, 1024-1030.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1024-1030
    • Du, G.1    Huang, P.2    Liang, B.T.3    Frohman, M.A.4
  • 68
    • 71849096122 scopus 로고    scopus 로고
    • Involvement of phospholipase d 1 and 2 in the subcellular localization and activity of formyl-peptide-receptors in the human colonic cell line ht29
    • Brandenburg, L.O.; Seyferth, S.; Wruck, C.J.; Koch, T.; Rosenstiel, P.; Lucius, R.; Pufe, T. Involvement of phospholipase d 1 and 2 in the subcellular localization and activity of formyl-peptide-receptors in the human colonic cell line ht29. Mol. Membr. Biol. 2009, 26, 371-383.
    • (2009) Mol. Membr. Biol. , vol.26 , pp. 371-383
    • Brandenburg, L.O.1    Seyferth, S.2    Wruck, C.J.3    Koch, T.4    Rosenstiel, P.5    Lucius, R.6    Pufe, T.7
  • 69
    • 33745007067 scopus 로고    scopus 로고
    • The phox homology domain of phospholipase d activates dynamin gtpase activity and accelerates egfr endocytosis
    • Lee, C.S.; Kim, I.S.; Park, J.B.; Lee, M.N.; Lee, H.Y.; Suh, P.G.; Ryu, S.H. The phox homology domain of phospholipase d activates dynamin gtpase activity and accelerates egfr endocytosis. Nat. Cell Biol. 2006, 8, 477-484.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 477-484
    • Lee, C.S.1    Kim, I.S.2    Park, J.B.3    Lee, M.N.4    Lee, H.Y.5    Suh, P.G.6    Ryu, S.H.7
  • 70
    • 33947314576 scopus 로고    scopus 로고
    • Regulation of receptor trafficking by grks and arrestins
    • Moore, C.A.; Milano, S.K.; Benovic, J.L. Regulation of receptor trafficking by grks and arrestins. Annu. Rev. Physiol. 2007, 69, 451-482.
    • (2007) Annu. Rev. Physiol. , vol.69 , pp. 451-482
    • Moore, C.A.1    Milano, S.K.2    Benovic, J.L.3
  • 71
    • 0037088608 scopus 로고    scopus 로고
    • beta-Arrestin/AP-2 interaction in G protein-coupled receptor internalization: Identification of a beta-arrestin binging site in beta 2-adaptin
    • Laporte, S.A.; Miller, W.E.; Kim, K.M.; Caron, M.G. beta-Arrestin/AP-2 interaction in G protein-coupled receptor internalization: Identification of a beta-arrestin binging site in beta 2-adaptin. J. Biol. Chem. 2002, 277, 9247-9254.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9247-9254
    • Laporte, S.A.1    Miller, W.E.2    Kim, K.M.3    Caron, M.G.4
  • 72
    • 0034616881 scopus 로고    scopus 로고
    • Type ialpha phosphatidylinositol 4-phosphate 5-kinase is a putative target for increased intracellular phosphatidic acid
    • Jones, D.R.; Sanjuan, M.A.; Merida, I. Type ialpha phosphatidylinositol 4-phosphate 5-kinase is a putative target for increased intracellular phosphatidic acid. FEBS Lett. 2000, 476, 160-165.
    • (2000) FEBS Lett. , vol.476 , pp. 160-165
    • Jones, D.R.1    Sanjuan, M.A.2    Merida, I.3
  • 73
    • 0037038412 scopus 로고    scopus 로고
    • Type I gamma phosphatidylinositol phosphate kinase targets and regulates focal adhesions
    • Ling, K.; Doughman, R.L.; Firestone, A.J.; Bunce, M.W.; Anderson, R.A. Type I gamma phosphatidylinositol phosphate kinase targets and regulates focal adhesions. Nature 2002, 420, 89-93.
    • (2002) Nature , vol.420 , pp. 89-93
    • Ling, K.1    Doughman, R.L.2    Firestone, A.J.3    Bunce, M.W.4    Anderson, R.A.5
  • 74
    • 0033580933 scopus 로고    scopus 로고
    • Coupled inositide phosphorylation and phospholipase d activation initiates clathrin-coat assembly on lysosomes
    • Arneson, L.S.; Kunz, J.; Anderson, R.A.; Traub, L.M. Coupled inositide phosphorylation and phospholipase d activation initiates clathrin-coat assembly on lysosomes. J. Biol. Chem. 1999, 274, 17794-17805.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17794-17805
    • Arneson, L.S.1    Kunz, J.2    Anderson, R.A.3    Traub, L.M.4
  • 76
    • 33645278358 scopus 로고    scopus 로고
    • Role of phospholipase d2 in the agonist-induced and constitutive endocytosis of g-protein coupled receptors
    • Koch, T.; Wu, D.F.; Yang, L.Q.; Brandenburg, L.O.; Hollt, V. Role of phospholipase d2 in the agonist-induced and constitutive endocytosis of g-protein coupled receptors. J. Neurochem. 2006, 97, 365-372.
    • (2006) J. Neurochem. , vol.97 , pp. 365-372
    • Koch, T.1    Wu, D.F.2    Yang, L.Q.3    Brandenburg, L.O.4    Hollt, V.5
  • 78
    • 34247383616 scopus 로고    scopus 로고
    • Clathrin-dependent mechanisms of g protein-coupled receptor endocytosis
    • Wolfe, B.L.; Trejo, J. Clathrin-dependent mechanisms of g protein-coupled receptor endocytosis. Traffic 2007, 8, 462-470.
    • (2007) Traffic , vol.8 , pp. 462-470
    • Wolfe, B.L.1    Trejo, J.2
  • 79
    • 0035802108 scopus 로고    scopus 로고
    • Phosphatidylinositol 4, 5-bisphosphate and arf6-regulated membrane traffic
    • Brown, F.D.; Rozelle, A.L.; Yin, H.L.; Balla, T.; Donaldson, J.G. Phosphatidylinositol 4, 5-bisphosphate and arf6-regulated membrane traffic. J. Cell Biol. 2001, 154, 1007-1017.
    • (2001) J. Cell Biol. , vol.154 , pp. 1007-1017
    • Brown, F.D.1    Rozelle, A.L.2    Yin, H.L.3    Balla, T.4    Donaldson, J.G.5
  • 80
    • 70349771766 scopus 로고    scopus 로고
    • Adp-ribosylation factor 6 regulates mu-opioid receptor trafficking and signaling via activation of phospholipase d2
    • Rankovic, M.; Jacob, L.; Rankovic, V.; Brandenburg, L.O.; Schroder, H.; Hollt, V.; Koch, T. Adp-ribosylation factor 6 regulates mu-opioid receptor trafficking and signaling via activation of phospholipase d2. Cell. Signal. 2009, 21, 1784-1793.
    • (2009) Cell. Signal. , vol.21 , pp. 1784-1793
    • Rankovic, M.1    Jacob, L.2    Rankovic, V.3    Brandenburg, L.O.4    Schroder, H.5    Hollt, V.6    Koch, T.7
  • 81
    • 31944435161 scopus 로고    scopus 로고
    • Phospholipase d2 is required for efficient endocytic recycling of transferrin receptors
    • Padron, D.; Tall, R.D.; Roth, M.G. Phospholipase d2 is required for efficient endocytic recycling of transferrin receptors. Mol. Biol. Cell 2006, 17, 598-606.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 598-606
    • Padron, D.1    Tall, R.D.2    Roth, M.G.3
  • 82
    • 64149121216 scopus 로고    scopus 로고
    • Arf6 regulates the synthesis of fusogenic lipids for calcium-regulated exocytosis in neuroendocrine cells
    • Begle, A.; Tryoen-Toth, P.; de Barry, J.; Bader, M.F.; Vitale, N. Arf6 regulates the synthesis of fusogenic lipids for calcium-regulated exocytosis in neuroendocrine cells. J. Biol. Chem. 2009, 284, 4836-4845.
    • (2009) J. Biol. Chem. , vol.284 , pp. 4836-4845
    • Begle, A.1    Tryoen-Toth, P.2    de Barry, J.3    Bader, M.F.4    Vitale, N.5
  • 83
    • 0035424718 scopus 로고    scopus 로고
    • Implications of lipid microdomains for membrane curvature, budding and fission
    • Huttner, W.B.; Zimmerberg, J. Implications of lipid microdomains for membrane curvature, budding and fission. Curr. Opin. Cell Biol. 2001, 13, 478-484.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 478-484
    • Huttner, W.B.1    Zimmerberg, J.2
  • 84
    • 30044435325 scopus 로고    scopus 로고
    • An effector domain mutant of arf6 implicates phospholipase d in endosomal membrane recycling
    • Jovanovic, O.A.; Brown, F.D.; Donaldson, J.G. An effector domain mutant of arf6 implicates phospholipase d in endosomal membrane recycling. Mol. Biol. Cell 2006, 17, 327-335.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 327-335
    • Jovanovic, O.A.1    Brown, F.D.2    Donaldson, J.G.3
  • 85
    • 0942287665 scopus 로고    scopus 로고
    • Phospholipase d2 modulates agonist-induced mu-opioid receptor desensitization and resensitization
    • Koch, T.; Brandenburg, L.O.; Liang, Y.; Schulz, S.; Beyer, A.; Schroder, H.; Hollt, V. Phospholipase d2 modulates agonist-induced mu-opioid receptor desensitization and resensitization. J. Neurochem. 2004, 88, 680-688.
    • (2004) J. Neurochem. , vol.88 , pp. 680-688
    • Koch, T.1    Brandenburg, L.O.2    Liang, Y.3    Schulz, S.4    Beyer, A.5    Schroder, H.6    Hollt, V.7
  • 87
    • 0032571340 scopus 로고    scopus 로고
    • Molecular mechanisms of g protein-coupled receptor desensitization and resensitization
    • Ferguson, S.S.; Zhang, J.; Barak, L.S.; Caron, M.G. Molecular mechanisms of g protein-coupled receptor desensitization and resensitization. Life Sci. 1998, 62, 1561-1565.
    • (1998) Life Sci. , vol.62 , pp. 1561-1565
    • Ferguson, S.S.1    Zhang, J.2    Barak, L.S.3    Caron, M.G.4
  • 88
    • 4444311166 scopus 로고    scopus 로고
    • Morphine induces terminal micro-opioid receptor desensitization by sustained phosphorylation of serine-375
    • Schulz, S.; Mayer, D.; Pfeiffer, M.; Stumm, R.; Koch, T.; Hollt, V. Morphine induces terminal micro-opioid receptor desensitization by sustained phosphorylation of serine-375. EMBO J. 2004, 23, 3282-3289.
    • (2004) EMBO J. , vol.23 , pp. 3282-3289
    • Schulz, S.1    Mayer, D.2    Pfeiffer, M.3    Stumm, R.4    Koch, T.5    Hollt, V.6
  • 89
    • 33646540454 scopus 로고    scopus 로고
    • Development of tolerance and sensitization to different opioid agonists in rats
    • Grecksch, G.; Bartzsch, K.; Widera, A.; Becker, A.; Hollt, V.; Koch, T. Development of tolerance and sensitization to different opioid agonists in rats. Psychopharmacology 2006, 186, 177-184.
    • (2006) Psychopharmacology , vol.186 , pp. 177-184
    • Grecksch, G.1    Bartzsch, K.2    Widera, A.3    Becker, A.4    Hollt, V.5    Koch, T.6
  • 90
    • 80051615294 scopus 로고    scopus 로고
    • Agonist-selective patterns of micro-opioid receptor phosphorylation revealed by phosphosite-specific antibodies
    • Doll, C.; Konietzko, J.; Poll, F.; Koch, T.; Hollt, V.; Schulz, S. Agonist-selective patterns of micro-opioid receptor phosphorylation revealed by phosphosite-specific antibodies. Br. J. Pharmacol. 2011, 164, 298-307.
    • (2011) Br. J. Pharmacol. , vol.164 , pp. 298-307
    • Doll, C.1    Konietzko, J.2    Poll, F.3    Koch, T.4    Hollt, V.5    Schulz, S.6
  • 91
    • 79956302829 scopus 로고    scopus 로고
    • Cellular morphine tolerance produced by betaarrestin-2-dependent impairment of mu-opioid receptor resensitization
    • Dang, V.C.; Chieng, B.; Azriel, Y.; Christie, M.J. Cellular morphine tolerance produced by betaarrestin-2-dependent impairment of mu-opioid receptor resensitization. J. Neurosci. 2011, 31, 7122-7130.
    • (2011) J. Neurosci. , vol.31 , pp. 7122-7130
    • Dang, V.C.1    Chieng, B.2    Azriel, Y.3    Christie, M.J.4
  • 92
    • 79953003987 scopus 로고    scopus 로고
    • Recovery from mu-opioid receptor desensitization after chronic treatment with morphine and methadone
    • Quillinan, N.; Lau, E.K.; Virk, M.; von Zastrow, M.; Williams, J.T. Recovery from mu-opioid receptor desensitization after chronic treatment with morphine and methadone. J. Neurosci. 2011, 31, 4434-4443.
    • (2011) J. Neurosci. , vol.31 , pp. 4434-4443
    • Quillinan, N.1    Lau, E.K.2    Virk, M.3    von Zastrow, M.4    Williams, J.T.5
  • 95
    • 52949101715 scopus 로고    scopus 로고
    • Involvement of formyl-peptide-receptor-like-1 and phospholipase d in the internalization and signal transduction of amyloid beta 1-42 in glial cells
    • Brandenburg, L.O.; Konrad, M.; Wruck, C.; Koch, T.; Pufe, T.; Lucius, R. Involvement of formyl-peptide-receptor-like-1 and phospholipase d in the internalization and signal transduction of amyloid beta 1-42 in glial cells. Neuroscience 2008, 156, 266-276.
    • (2008) Neuroscience , vol.156 , pp. 266-276
    • Brandenburg, L.O.1    Konrad, M.2    Wruck, C.3    Koch, T.4    Pufe, T.5    Lucius, R.6
  • 96
    • 77954485876 scopus 로고    scopus 로고
    • Platelet hyperreactivity and a prothrombotic phenotype in mice with a gain-of-function mutation in phospholipase Cgamma2
    • Elvers, M.; Pozgaj, R.; Pleines, I.; May, F.; Kuijpers, M.J.; Heemskerk, J.M.; Yu, P.; Nieswandt, B. Platelet hyperreactivity and a prothrombotic phenotype in mice with a gain-of-function mutation in phospholipase Cgamma2. J. Thromb. Haemost. 2010, 8, 1353-1363.
    • (2010) J. Thromb. Haemost. , vol.8 , pp. 1353-1363
    • Elvers, M.1    Pozgaj, R.2    Pleines, I.3    May, F.4    Kuijpers, M.J.5    Heemskerk, J.M.6    Yu, P.7    Nieswandt, B.8
  • 98
    • 79953735822 scopus 로고    scopus 로고
    • Morphoproteomic analysis reveals an overexpressed and constitutively activated phospholipase D1-mTORC2 pathway in endometrial carcinoma
    • Shen, Q.; Stanton, M.L.; Feng, W.; Rodriguez, M.E.; Ramondetta, L.; Chen, L.; Brown, R.E.; Duan, X. Morphoproteomic analysis reveals an overexpressed and constitutively activated phospholipase D1-mTORC2 pathway in endometrial carcinoma. Int. J. Clin. Exp. Pathol. 2010, 4, 13-21.
    • (2010) Int. J. Clin. Exp. Pathol. , vol.4 , pp. 13-21
    • Shen, Q.1    Stanton, M.L.2    Feng, W.3    Rodriguez, M.E.4    Ramondetta, L.5    Chen, L.6    Brown, R.E.7    Duan, X.8
  • 100
    • 0030875648 scopus 로고    scopus 로고
    • Amyloid beta-induced neurotoxicity is associated with phospholipase d activation in cultured rat hippocampal cells
    • Cox, D.A.; Cohen, M.L. Amyloid beta-induced neurotoxicity is associated with phospholipase d activation in cultured rat hippocampal cells. Neurosci. Lett. 1997, 229, 37-40.
    • (1997) Neurosci. Lett. , vol.229 , pp. 37-40
    • Cox, D.A.1    Cohen, M.L.2
  • 102
    • 0035158645 scopus 로고    scopus 로고
    • Beta amyloid peptide (Abeta42) is internalized via the G-protein-coupled receptor FPRL1 and forms fibrillar aggregates in macrophages
    • Yazawa, H.; Yu, Z.X.; Takeda; Le, Y.; Gong, W.; Ferrans, V.J.; Oppenheim, J.J.; Li, C.C.; Wang, J.M. Beta amyloid peptide (Abeta42) is internalized via the G-protein-coupled receptor FPRL1 and forms fibrillar aggregates in macrophages. FASEB J. 2001, 15, 2454-2462.
    • (2001) FASEB J. , vol.15 , pp. 2454-2462
    • Yazawa, H.1    Yu, Z.X.2    Takeda3    Le, Y.4    Gong, W.5    Ferrans, V.J.6    Oppenheim, J.J.7    Li, C.C.8    Wang, J.M.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.