메뉴 건너뛰기




Volumn 10, Issue 1, 2000, Pages 43-46

Phospholipase D regulation and localisation is dependent upon a phosphatidylinositol 4, 5-bisphosphate-specific PH domain

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CLONE; CYTOSKELETON; DELETION MUTAGENESIS; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME LOCALIZATION; ENZYME REGULATION; GENE ACTIVATION; GLUTATHIONE TRANSFERASE; HYDROLYSIS; MONOLAYER; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHOLIPASE D; POINT MUTATION; PROTEIN LIPID INTERACTION; SIGNAL TRANSDUCTION;

EID: 0033985026     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(99)00264-X     Document Type: Article
Times cited : (121)

References (17)
  • 1
    • 0032102323 scopus 로고    scopus 로고
    • Diacylglycerols and phosphatidates: Which molecular species are intracellular messengers?
    • Hodgkin M., Pettitt T.R., Martin A., Michell R.H., Wakelam M.J.O. Diacylglycerols and phosphatidates: which molecular species are intracellular messengers? Trends Biochem Science 23:1998;200-204
    • (1998) Trends Biochem Sci , vol.23 , pp. 200-204
    • Hodgkin, M.1    Pettitt, T.R.2    Martin, A.3    Michell, R.H.4    Wakelam, M.J.O.5
  • 3
    • 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.C., Powner D., Thompson N.T.et al. Phospholipase D1 localises to secretory granules and lysosomes and is plasma-membrane translocated on cellular stimulation. Curr Biol. 8:1998;835-838
    • (1998) Curr Biol , vol.8 , pp. 835-838
    • Brown, F.D.1    Thompson, N.2    Saqib, K.M.3    Clark, J.C.4    Powner, D.5    Thompson, N.T.6
  • 5
    • 0033119178 scopus 로고    scopus 로고
    • Characterisation of the regulation of phospholipase D activity in the detergent-insoluble fraction of HL60 cells by protein kinase C and small G-proteins
    • Hodgkin M.N., Clark J.M., Rose S., Saqib K., Wakelam M.J.O. Characterisation of the regulation of phospholipase D activity in the detergent-insoluble fraction of HL60 cells by protein kinase C and small G-proteins. Biochem J. 339:1999;87-93
    • (1999) Biochem J , vol.339 , pp. 87-93
    • Hodgkin, M.N.1    Clark, J.M.2    Rose, S.3    Saqib, K.4    Wakelam, M.J.O.5
  • 6
    • 0030037396 scopus 로고    scopus 로고
    • Activation of phospholipase D and phosphatidylinositol 4-phosphate 5-kinase in HL60 cells is mediated by endogenous Arf but not Rho
    • Martin A., Brown D.B., Hodgkin M.N., Bradwell A.J., Cook S.J., Hart M.et al. Activation of phospholipase D and phosphatidylinositol 4-phosphate 5-kinase in HL60 cells is mediated by endogenous Arf but not Rho. J Biol Chem. 271:1996;17397-17403
    • (1996) J Biol Chem , vol.271 , pp. 17397-17403
    • Martin, A.1    Brown, D.B.2    Hodgkin, M.N.3    Bradwell, A.J.4    Cook, S.J.5    Hart, M.6
  • 7
    • 0030200347 scopus 로고    scopus 로고
    • A duplicated catalytic motif in a new superfamily of phosphohydrolases and phospholipid synthases that includes poxvirus coat proteins
    • Koonin E.V. A duplicated catalytic motif in a new superfamily of phosphohydrolases and phospholipid synthases that includes poxvirus coat proteins. Trends Biochem Science 21:1996;242-243
    • (1996) Trends Biochem Sci , vol.21 , pp. 242-243
    • Koonin, E.V.1
  • 8
    • 0031670386 scopus 로고    scopus 로고
    • Characterization of human PLD2 and the analysis of PLD isoform variants
    • Steed P.M., Clark K.L., Boyar W.C., Lasala D.J. Characterization of human PLD2 and the analysis of PLD isoform variants. FASEB J. 12:1998;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
  • 9
    • 0032923142 scopus 로고    scopus 로고
    • Recognizing the pleckstrin homology domain fold in mammalian phospholipase D using hidden Markov models
    • Holbrook P., Geetha V., Beavan M.A., Munson P.J. Recognizing the pleckstrin homology domain fold in mammalian phospholipase D using hidden Markov models. FEBS Lett. 448:1999;269-272
    • (1999) FEBS Lett , vol.448 , pp. 269-272
    • Holbrook, P.1    Geetha, V.2    Beavan, M.A.3    Munson, P.J.4
  • 10
    • 0032142903 scopus 로고    scopus 로고
    • Bacillus thuringiensis Cry1Ac toxin interaction with Manduca sexta aminopeptidase N in a model membrane environment
    • Cooper M.A., Carroll J., Travis E.R., Williams D.H., Ellar D.J. Bacillus thuringiensis Cry1Ac toxin interaction with Manduca sexta aminopeptidase N in a model membrane environment. Biochem J. 333:1998;677-683
    • (1998) Biochem J , vol.333 , pp. 677-683
    • Cooper, M.A.1    Carroll, J.2    Travis, E.R.3    Williams, D.H.4    Ellar, D.J.5
  • 11
    • 0032548993 scopus 로고    scopus 로고
    • Solution structure of the C-terminal domain of the p85α regulatory subunit of phosphoinositide 3-kinase
    • Siegal G., Davis B., Kristensen S.M., Sanker A., Lincre J., Stein R.C.et al. Solution structure of the C-terminal domain of the p85α regulatory subunit of phosphoinositide 3-kinase. J Mol Biol. 276:1998;461-478
    • (1998) J Mol Biol , vol.276 , pp. 461-478
    • Siegal, G.1    Davis, B.2    Kristensen, S.M.3    Sanker, A.4    Lincre, J.5    Stein, R.C.6
  • 12
    • 0033084143 scopus 로고    scopus 로고
    • Role of phosphatidylinositol 3, 4, 5-trisphosphate in regulating the activity and localisation of 3-phosphoinositide-dependent kinase-1
    • Currie R.A., Walker K.S., Gray A., Deak M., Casamayor A., Downes C.P.et al. Role of phosphatidylinositol 3, 4, 5-trisphosphate in regulating the activity and localisation of 3-phosphoinositide-dependent kinase-1. Biochem J. 337:1999;575-583
    • (1999) Biochem J , vol.337 , pp. 575-583
    • Currie, R.A.1    Walker, K.S.2    Gray, A.3    Deak, M.4    Casamayor, A.5    Downes, C.P.6
  • 13
    • 0032515042 scopus 로고    scopus 로고
    • Specificity and promiscuity in phosphoinositide binding by pleckstrin homology domains
    • Kavran J.M., Klein D.E., Lee A., Falasca M., Isakoff S.J., Skolnik E.Y.et al. Specificity and promiscuity in phosphoinositide binding by pleckstrin homology domains. J Biol Chem. 273:1998;30497-30508
    • (1998) J Biol Chem , vol.273 , pp. 30497-30508
    • Kavran, J.M.1    Klein, D.E.2    Lee, A.3    Falasca, M.4    Isakoff, S.J.5    Skolnik, E.Y.6
  • 15
    • 0029824848 scopus 로고    scopus 로고
    • Mutation of the pleckstrin homology domain of Bruton's tyrosine kinase in immunodeficiency impaired inositol 1, 3, 4, 5-tetrakisphosphate binding capacity
    • Fukada M., Kojima T., Kabayama H., Mikoshiba K. Mutation of the pleckstrin homology domain of Bruton's tyrosine kinase in immunodeficiency impaired inositol 1, 3, 4, 5-tetrakisphosphate binding capacity. J Biol Chem. 271:1996;30303-30306
    • (1996) J Biol Chem , vol.271 , pp. 30303-30306
    • Fukada, M.1    Kojima, T.2    Kabayama, H.3    Mikoshiba, K.4
  • 16
    • 0032568655 scopus 로고    scopus 로고
    • SMART a simple modular architecture research tool: Identification of signaling domains
    • Schultz J., Milpetz F., Bork P., Ponting C.P. SMART a simple modular architecture research tool: identification of signaling domains. Proc Natl Acad Sci USA. 95:1998;5857-5864
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 17
    • 8244263617 scopus 로고    scopus 로고
    • A target of phosphatidylinositol 3, 4, 5-trisphosphate with a zinc finger motif similar to that of the ADP-ribosylation factor GTPase-activating protein and two pleckstrin homology domains
    • Tanaka K., Imajoh-Ohmi S., Sawada T., Shirai R., Hashimoto Y., Iwasaki S.et al. A target of phosphatidylinositol 3, 4, 5-trisphosphate with a zinc finger motif similar to that of the ADP-ribosylation factor GTPase-activating protein and two pleckstrin homology domains. Eur J Biochem. 245:1997;512-519
    • (1997) Eur J Biochem , vol.245 , pp. 512-519
    • Tanaka, K.1    Imajoh-Ohmi, S.2    Sawada, T.3    Shirai, R.4    Hashimoto, Y.5    Iwasaki, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.