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Volumn 1781, Issue 8, 2008, Pages 376-382

Caspase cleavage of phospholipase D1 in vitro alters its regulation and reveals a novel property of the "loop" region

Author keywords

Apoptosis; Caspase; Phosphatidic acid; Phospholipase D; Regulatory domain

Indexed keywords

CASPASE 3; CASPASE 7; CASPASE 8; GUANOSINE TRIPHOSPHATASE; PHOSPHOLIPASE D1; PHOSPHOLIPASE D2; PROTEIN KINASE C;

EID: 48649107037     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2008.05.007     Document Type: Article
Times cited : (8)

References (49)
  • 1
    • 0030892164 scopus 로고    scopus 로고
    • Phospholipase D: enzymology, mechanisms of regulation, and function
    • Exton J.H. Phospholipase D: enzymology, mechanisms of regulation, and function. Physiol. Rev. 77 (1997) 303-320
    • (1997) Physiol. Rev. , vol.77 , pp. 303-320
    • Exton, J.H.1
  • 2
    • 21544470248 scopus 로고    scopus 로고
    • Protein kinase C and phospholipase D: intimate interactions in intracellular signaling
    • Becker K.P., and Hannun Y.A. Protein kinase C and phospholipase D: intimate interactions in intracellular signaling. Cell. Mol. Life Sci. 62 (2005) 1448-1461
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 1448-1461
    • Becker, K.P.1    Hannun, Y.A.2
  • 3
    • 0028346383 scopus 로고
    • Type I phosphatidylinositol 4-phosphate 5-kinase isoforms are specifically stimulated by phosphatidic acid
    • Jenkins G.H., Fisette P.L., and Anderson R.A. Type I phosphatidylinositol 4-phosphate 5-kinase isoforms are specifically stimulated by phosphatidic acid. J. Biol. Chem. 269 (1994) 11547-11554
    • (1994) J. Biol. Chem. , vol.269 , pp. 11547-11554
    • Jenkins, G.H.1    Fisette, P.L.2    Anderson, R.A.3
  • 5
    • 33744907512 scopus 로고    scopus 로고
    • Phospholipase D1 regulates cell migration in a lipase activity-independent manner
    • Kim J.H., Kim H.W., Jeon H., Suh P.G., and Ryu S.H. Phospholipase D1 regulates cell migration in a lipase activity-independent manner. J. Biol. Chem. 281 (2006) 15747-15756
    • (2006) J. Biol. Chem. , vol.281 , pp. 15747-15756
    • Kim, J.H.1    Kim, H.W.2    Jeon, H.3    Suh, P.G.4    Ryu, S.H.5
  • 6
    • 0032775581 scopus 로고    scopus 로고
    • Phospholipase D and membrane traffic. Potential roles in regulated exocytosis, membrane delivery and vesicle budding
    • Jones D., Morgan C., and Cockcroft S. Phospholipase D and membrane traffic. Potential roles in regulated exocytosis, membrane delivery and vesicle budding. Biochim. Biophys. Acta 1439 (1999) 229-244
    • (1999) Biochim. Biophys. Acta , vol.1439 , pp. 229-244
    • Jones, D.1    Morgan, C.2    Cockcroft, S.3
  • 7
    • 0032540884 scopus 로고    scopus 로고
    • Secretory vesicle budding from the trans-Golgi network is mediated by phosphatidic acid levels
    • Siddhanta A., and Shields D. Secretory vesicle budding from the trans-Golgi network is mediated by phosphatidic acid levels. J. Biol. Chem. 273 (1998) 17995-17998
    • (1998) J. Biol. Chem. , vol.273 , pp. 17995-17998
    • Siddhanta, A.1    Shields, D.2
  • 8
    • 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., and Ryu S.H. The phox homology domain of phospholipase D activates dynamin GTPase activity and accelerates EGFR endocytosis. Nat. Cell Biol. 8 (2006) 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
  • 10
    • 33846438568 scopus 로고    scopus 로고
    • Regulation of mTOR by phosphatidic acid?
    • Foster D.A. Regulation of mTOR by phosphatidic acid?. Cancer Res. 67 (2007) 1-4
    • (2007) Cancer Res. , vol.67 , pp. 1-4
    • Foster, D.A.1
  • 11
    • 0037203353 scopus 로고    scopus 로고
    • Roles of phospholipase D in apoptosis and pro-survival
    • Nozawa Y. Roles of phospholipase D in apoptosis and pro-survival. Biochim. Biophys. Acta 1585 (2002) 77-86
    • (2002) Biochim. Biophys. Acta , vol.1585 , pp. 77-86
    • Nozawa, Y.1
  • 12
    • 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., and Frohman M.A. Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family. J. Biol. Chem. 270 (1995) 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
  • 14
    • 0027943755 scopus 로고
    • Purification and characterization of phosphatidylcholine phospholipase D from pig lung
    • Okamura S., and Yamashita S. Purification and characterization of phosphatidylcholine phospholipase D from pig lung. J. Biol. Chem. 269 (1994) 31207-31213
    • (1994) J. Biol. Chem. , vol.269 , pp. 31207-31213
    • Okamura, S.1    Yamashita, S.2
  • 15
    • 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., and Morris A.J. 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. 272 (1997) 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
  • 17
    • 0032492689 scopus 로고    scopus 로고
    • Regulation of phospholipase D2: selective inhibition of mammalian phospholipase D isoenzymes by alpha- and beta-synucleins
    • Jenco J.M., Rawlingson A., Daniels B., and Morris A.J. Regulation of phospholipase D2: selective inhibition of mammalian phospholipase D isoenzymes by alpha- and beta-synucleins. Biochemistry 37 (1998) 4901-4909
    • (1998) Biochemistry , vol.37 , pp. 4901-4909
    • Jenco, J.M.1    Rawlingson, A.2    Daniels, B.3    Morris, A.J.4
  • 18
    • 0027965240 scopus 로고
    • Novel function of phosphatidylinositol 4,5-bisphosphate as a cofactor for brain membrane phospholipase D
    • Liscovitch M., Chalifa V., Pertile P., Chen C.S., and Cantley L.C. Novel function of phosphatidylinositol 4,5-bisphosphate as a cofactor for brain membrane phospholipase D. J. Biol. Chem. 269 (1994) 21403-21406
    • (1994) J. Biol. Chem. , vol.269 , pp. 21403-21406
    • Liscovitch, M.1    Chalifa, V.2    Pertile, P.3    Chen, C.S.4    Cantley, L.C.5
  • 20
    • 0036854458 scopus 로고    scopus 로고
    • Phospholipase D2 is localized to the rims of the Golgi apparatus in Mammalian cells
    • Freyberg Z., Bourgoin S., and Shields D. Phospholipase D2 is localized to the rims of the Golgi apparatus in Mammalian cells. Mol. Biol. Cell 13 (2002) 3930-3942
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3930-3942
    • Freyberg, Z.1    Bourgoin, S.2    Shields, D.3
  • 21
    • 1542399170 scopus 로고    scopus 로고
    • "Slip, sliding away": phospholipase D and the Golgi apparatus
    • Freyberg Z., Siddhanta A., and Shields D. "Slip, sliding away": phospholipase D and the Golgi apparatus. Trends Cell Biol. 13 (2003) 540-546
    • (2003) Trends Cell Biol. , vol.13 , pp. 540-546
    • Freyberg, Z.1    Siddhanta, A.2    Shields, D.3
  • 22
    • 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., and Frohman M.A. Phospholipase D2 localizes to the plasma membrane and regulates angiotensin II receptor endocytosis. Mol. Biol. Cell. 15 (2004) 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
  • 23
    • 33947674706 scopus 로고    scopus 로고
    • Phospholipase D2-derived phosphatidic acid binds to and activates ribosomal p70 S6 kinase independently of mTOR
    • Lehman N., Ledford B., Di Fulvio M., Frondorf K., McPhail L.C., and Gomez-Cambronero J. Phospholipase D2-derived phosphatidic acid binds to and activates ribosomal p70 S6 kinase independently of mTOR. FASEB J. (2007)
    • (2007) FASEB J.
    • Lehman, N.1    Ledford, B.2    Di Fulvio, M.3    Frondorf, K.4    McPhail, L.C.5    Gomez-Cambronero, J.6
  • 24
    • 0038339003 scopus 로고    scopus 로고
    • Phospholipase D confers rapamycin resistance in human breast cancer cells
    • Chen Y., Zheng Y., and Foster D.A. Phospholipase D confers rapamycin resistance in human breast cancer cells. Oncogene 22 (2003) 3937-3942
    • (2003) Oncogene , vol.22 , pp. 3937-3942
    • Chen, Y.1    Zheng, Y.2    Foster, D.A.3
  • 25
    • 1542330140 scopus 로고    scopus 로고
    • Expression and regulation of phospholipase D isoenzymes in human melanoma cells and primary melanocytes
    • Riebeling C., Müller C., and Geilen C.C. Expression and regulation of phospholipase D isoenzymes in human melanoma cells and primary melanocytes. Melanoma Res. 13 (2003) 555-562
    • (2003) Melanoma Res. , vol.13 , pp. 555-562
    • Riebeling, C.1    Müller, C.2    Geilen, C.C.3
  • 26
    • 0032534566 scopus 로고    scopus 로고
    • Increased activity of oleate-dependent type phospholipase D during actinomycin D-induced apoptosis in Jurkat T cells
    • Kasai T., Ohguchi K., Nakashima S., Ito Y., Naganawa T., Kondo N., and Nozawa Y. Increased activity of oleate-dependent type phospholipase D during actinomycin D-induced apoptosis in Jurkat T cells. J. Immunol. 161 (1998) 6469-6474
    • (1998) J. Immunol. , vol.161 , pp. 6469-6474
    • Kasai, T.1    Ohguchi, K.2    Nakashima, S.3    Ito, Y.4    Naganawa, T.5    Kondo, N.6    Nozawa, Y.7
  • 27
    • 0032584077 scopus 로고    scopus 로고
    • Changes of phospholipase D activity in TNF-alpha and anti-Fas/Apo1 monoclonal antibody induced apoptosis in HL-60 and A20 cells
    • Kang J.H., Shin I., and Han J.S. Changes of phospholipase D activity in TNF-alpha and anti-Fas/Apo1 monoclonal antibody induced apoptosis in HL-60 and A20 cells. Exp. Mol. Med. 30 (1998) 21-27
    • (1998) Exp. Mol. Med. , vol.30 , pp. 21-27
    • Kang, J.H.1    Shin, I.2    Han, J.S.3
  • 28
    • 0034669405 scopus 로고    scopus 로고
    • Regulation of phospholipase D activity and ceramide production in daunorubicin-induced apoptosis in A-431 cells
    • Chen J.S., Chai M.Q., Chen H.H., Zhao S., and Song J.G. Regulation of phospholipase D activity and ceramide production in daunorubicin-induced apoptosis in A-431 cells. Biochim. Biophys. Acta 1488 (2000) 219-232
    • (2000) Biochim. Biophys. Acta , vol.1488 , pp. 219-232
    • Chen, J.S.1    Chai, M.Q.2    Chen, H.H.3    Zhao, S.4    Song, J.G.5
  • 30
    • 0032567338 scopus 로고    scopus 로고
    • Association of N- and C-terminal domains of phospholipase D is required for catalytic activity
    • Xie Z., Ho W.T., and Exton J.H. Association of N- and C-terminal domains of phospholipase D is required for catalytic activity. J. Biol. Chem. 273 (1998) 34679-34682
    • (1998) J. Biol. Chem. , vol.273 , pp. 34679-34682
    • Xie, Z.1    Ho, W.T.2    Exton, J.H.3
  • 32
    • 0030843298 scopus 로고    scopus 로고
    • Human phospholipase D1 can be tyrosine-phosphorylated in HL-60 granulocytes
    • Marcil J., Harbour D., Naccache P.H., and Bourgoin S. Human phospholipase D1 can be tyrosine-phosphorylated in HL-60 granulocytes. J. Biol. Chem. 272 (1997) 20660-20664
    • (1997) J. Biol. Chem. , vol.272 , pp. 20660-20664
    • Marcil, J.1    Harbour, D.2    Naccache, P.H.3    Bourgoin, S.4
  • 33
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c
    • Liu X., Kim C.N., Yang J., Jemmerson R., and Wang X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 86 (1996) 147-157
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 34
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh E.G., and Dyer W.J. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37 (1959) 911-917
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 39
    • 0027142022 scopus 로고
    • ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity
    • Brown H.A., Gutowski S., Moomaw C.R., Slaughter C., and Sternweis P.C. ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity. Cell 75 (1993) 1137-1144
    • (1993) Cell , vol.75 , pp. 1137-1144
    • Brown, H.A.1    Gutowski, S.2    Moomaw, C.R.3    Slaughter, C.4    Sternweis, P.C.5
  • 40
    • 0024537947 scopus 로고
    • Phosphatidylethanol biosynthesis in ethanol-exposed NG108-15 neuroblastoma X glioma hybrid cells. Evidence for activation of a phospholipase D phosphatidyl transferase activity by protein kinase C
    • Liscovitch M. Phosphatidylethanol biosynthesis in ethanol-exposed NG108-15 neuroblastoma X glioma hybrid cells. Evidence for activation of a phospholipase D phosphatidyl transferase activity by protein kinase C. J. Biol. Chem. 264 (1989) 1450-1456
    • (1989) J. Biol. Chem. , vol.264 , pp. 1450-1456
    • Liscovitch, M.1
  • 42
    • 0034283578 scopus 로고    scopus 로고
    • Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8
    • Stennicke H.R., Renatus M., Meldal M., and Salvesen G.S. Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8. Biochem. J. 350 (2000) 563-568
    • (2000) Biochem. J. , vol.350 , pp. 563-568
    • Stennicke, H.R.1    Renatus, M.2    Meldal, M.3    Salvesen, G.S.4
  • 44
    • 23944499618 scopus 로고    scopus 로고
    • Identification of interaction sites of protein kinase Calpha on phospholipase D1
    • Kook S., and Exton J.H. Identification of interaction sites of protein kinase Calpha on phospholipase D1. Cell. Signal 17 (2005) 1423-1432
    • (2005) Cell. Signal , vol.17 , pp. 1423-1432
    • Kook, S.1    Exton, J.H.2
  • 45
    • 0037436828 scopus 로고    scopus 로고
    • Phospholipase D prevents apoptosis in v-Src-transformed rat fibroblasts and MDA-MB-231 breast cancer cells
    • Zhong M., Shen Y., Zheng Y., Joseph T., Jackson D., and Foster D.A. Phospholipase D prevents apoptosis in v-Src-transformed rat fibroblasts and MDA-MB-231 breast cancer cells. Biochem. Biophys. Res. Commun. 302 (2003) 615-619
    • (2003) Biochem. Biophys. Res. Commun. , vol.302 , pp. 615-619
    • Zhong, M.1    Shen, Y.2    Zheng, Y.3    Joseph, T.4    Jackson, D.5    Foster, D.A.6
  • 46
    • 13244289821 scopus 로고    scopus 로고
    • Alternative phospholipase D/mTOR survival signal in human breast cancer cells
    • Chen Y., Rodrik V., and Foster D.A. Alternative phospholipase D/mTOR survival signal in human breast cancer cells. Oncogene 24 (2005) 672-679
    • (2005) Oncogene , vol.24 , pp. 672-679
    • Chen, Y.1    Rodrik, V.2    Foster, D.A.3
  • 47
    • 0035910461 scopus 로고    scopus 로고
    • Regulation of apoptosis by phosphatidylinositol 4,5-bisphosphate inhibition of caspases, and caspase inactivation of phosphatidylinositol phosphate 5-kinases
    • Mejillano M., Yamamoto M., Rozelle A.L., Sun H.Q., Wang X., and Yin H.L. Regulation of apoptosis by phosphatidylinositol 4,5-bisphosphate inhibition of caspases, and caspase inactivation of phosphatidylinositol phosphate 5-kinases. J. Biol. Chem. 276 (2001) 1865-1872
    • (2001) J. Biol. Chem. , vol.276 , pp. 1865-1872
    • Mejillano, M.1    Yamamoto, M.2    Rozelle, A.L.3    Sun, H.Q.4    Wang, X.5    Yin, H.L.6
  • 48
    • 0032476047 scopus 로고    scopus 로고
    • DAD1 is required for the function and the structural integrity of the oligosaccharyltransferase complex
    • Sanjay A., Fu J., and Kreibich G. DAD1 is required for the function and the structural integrity of the oligosaccharyltransferase complex. J. Biol. Chem. 273 (1998) 26094-26099
    • (1998) J. Biol. Chem. , vol.273 , pp. 26094-26099
    • Sanjay, A.1    Fu, J.2    Kreibich, G.3
  • 49
    • 0035339648 scopus 로고    scopus 로고
    • Determination of interaction sites of phospholipase D1 for RhoA
    • Cai S., and Exton J.H. Determination of interaction sites of phospholipase D1 for RhoA. Biochem. J. 355 (2001) 779-785
    • (2001) Biochem. J. , vol.355 , pp. 779-785
    • Cai, S.1    Exton, J.H.2


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