메뉴 건너뛰기




Volumn 287, Issue 14, 2012, Pages 10844-10852

Autophosphorylation of Ser428 of EhC2PK plays a critical role in regulating erythrophagocytosis in the parasite Entamoeba histolytica

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ANTIGEN-ANTIBODY REACTIONS; DEFECTS; MACROPHAGES; MASS SPECTROMETRY;

EID: 84859486840     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.308874     Document Type: Article
Times cited : (15)

References (28)
  • 3
    • 0021199319 scopus 로고
    • Virulence of Entamoeba histolytica trophozoites. Effects of bacteria, microaerobic conditions, and metronidazole
    • Bracha, R. and Mirelman, D. (1984) Virulence of Entamoeba histolytica trophozoites: Effects of bacteria, microaerobic conditions, and metronidazole. J. Exp. Med. 160, 353-368 (Pubitemid 14052502)
    • (1984) Journal of Experimental Medicine , vol.160 , Issue.2 , pp. 353-368
    • Bracha, R.1    Mirelman, D.2
  • 4
    • 0037305026 scopus 로고    scopus 로고
    • Apoptotic killing and phagocytosis of host cells by the parasite Entamoeba histolytica
    • DOI 10.1128/IAI.71.2.964-972.2003
    • Huston, C. D., Boettner, D. R., Miller-Sims, V., and Petri, W. A., Jr. (2003) Apoptotic killing and phagocytosis of host cells by the parasite Entamoeba histolytica. Infect. Immun. 71, 964-972 (Pubitemid 36150793)
    • (2003) Infection and Immunity , vol.71 , Issue.2 , pp. 964-972
    • Huston, C.D.1    Boettner, D.R.2    Miller-Sims, V.3    Petri Jr., W.A.4
  • 5
    • 4444262526 scopus 로고    scopus 로고
    • Calcium binding protein 1 of the protozoan parasite Entamoeba histolytica interacts with actin and is involved in cytoskeleton dynamics
    • DOI 10.1242/jcs.01198
    • Sahoo, N., Labruyère, E., Bhattacharya, S., Sen, P., Guillén, N., and Bhattacharya, A. (2004) Calcium-binding protein 1 of the protozoan parasite Entamoeba histolytica interacts with actin and is involved in cytoskeleton dynamics. J. Cell Sci. 117, 3625-3634 (Pubitemid 39206402)
    • (2004) Journal of Cell Science , vol.117 , Issue.16 , pp. 3625-3634
    • Sahoo, N.1    Labruyere, E.2    Bhattacharya, S.3    Sen, P.4    Guillen, N.5    Bhattacharya, A.6
  • 6
    • 79952473943 scopus 로고    scopus 로고
    • A C2 domain protein kinase initiates phagocytosis in the protozoan parasite Entamoeba histolytica
    • DOI: 10.1038/ncomms1199
    • Somlata, Bhattacharya, S., and Bhattacharya, A. (2011) A C2 domain protein kinase initiates phagocytosis in the protozoan parasite Entamoeba histolytica. Nat. Commun. DOI: 10.1038/ncomms1199
    • (2011) Nat. Commun.
    • Somlata1    Bhattacharya, S.2    Bhattacharya, A.3
  • 7
    • 43449100343 scopus 로고    scopus 로고
    • Calcium-binding protein 1 of Entamoeba histolytica transiently associates with phagocytic cups in a calcium-independent manner
    • DOI 10.1111/j.1462-5822.2008.01134.x
    • Jain, R., Santi-Rocca, J., Padhan, N., Bhattacharya, S., Guillen, N., and Bhattacharya, A. (2008) Calcium-binding protein 1 of Entamoeba histolytica transiently associates with phagocytic cups in a calcium-independent manner. Cell. Microbiol. 10, 1373-1389 (Pubitemid 351663927)
    • (2008) Cellular Microbiology , vol.10 , Issue.6 , pp. 1373-1389
    • Jain, R.1    Santi-Rocca, J.2    Padhan, N.3    Bhattacharya, S.4    Guillen, N.5    Bhattacharya, A.6
  • 9
    • 0037108571 scopus 로고    scopus 로고
    • Atypical protein kinase C-ζ is essential for delayed phagocytosis of Helicobacter pylori
    • Allen, L. H., and Allgood, J. A. (2002) Atypical protein kinase C-ζ is essential for delayed phagocytosis of Helicobacter pylori. Curr. Biol. 12, 1762-1766
    • (2002) Curr. Biol. , vol.12 , pp. 1762-1766
    • Allen, L.H.1    Allgood, J.A.2
  • 10
    • 66349132474 scopus 로고    scopus 로고
    • Lipid Binding Domains: More than simple lipid effectors
    • Stahelin, R. V. (2009) Lipid Binding Domains: More than simple lipid effectors. J. Lipid Res. 50, S299-304
    • (2009) J. Lipid Res. , vol.50
    • Stahelin, R.V.1
  • 11
    • 0029020282 scopus 로고
    • Protein kinases. The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks, S. K., and Hunter, T. (1995) Protein kinases. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. Faseb J. 9, 576-596
    • (1995) Faseb J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 12
    • 33745713815 scopus 로고    scopus 로고
    • Characterization of the binding of the fluorescent ATP analogue TNP-ATP to insulysin
    • Yao, H. and Hersh, L. B. (2006) Characterization of the binding of the fluorescent ATP analogue TNP-ATP to insulysin. Arch. Biochem. Biophys. 451, 175-181
    • (2006) Arch. Biochem. Biophys. , vol.451 , pp. 175-181
    • Yao, H.1    Hersh, L.B.2
  • 13
    • 0024394417 scopus 로고
    • Staurosporine, K-252 and UCN-01: Potent but nonspecific inhibitors of protein kinases
    • DOI 10.1016/0165-6147(89)90263-0
    • Rüegg, U. T., and Burgess, G. M. (1989) Staurosporine, K-252 and UCN-01: potent but nonspecific inhibitors of protein kinases. Trends Pharmacol Sci 10, 218-220 (Pubitemid 19146392)
    • (1989) Trends in Pharmacological Sciences , vol.10 , Issue.6 , pp. 218-220
    • Ruegg, U.T.1    Burgess, G.M.2
  • 16
    • 0037330372 scopus 로고    scopus 로고
    • Blocking the expression of a calcium binding protein of the protozoan parasite Entamoeba histolytica by tetracycline regulatable antisense-RNA
    • DOI 10.1016/S0166-6851(02)00284-0, PII S0166685102002840
    • Sahoo, N., Bhattacharya, S., and Bhattacharya, A. (2003) Blocking the expression of a calcium-binding protein of the protozoan parasite E. histolytica by tetracycline regulatable antisense-RNA. Mol. Biochem. Parasitol. 126, 281-284 (Pubitemid 36255627)
    • (2003) Molecular and Biochemical Parasitology , vol.126 , Issue.2 , pp. 281-284
    • Sahoo, N.1    Bhattacharya, S.2    Bhattacharya, A.3
  • 17
    • 0030987070 scopus 로고    scopus 로고
    • Regulation of protein kinase C
    • Newton, A. C. (1997) Regulation of protein kinase C. Curr. Opin. Cell Biol. 9, 161-167
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 161-167
    • Newton, A.C.1
  • 18
    • 33750691391 scopus 로고    scopus 로고
    • Role of threonine residues in the regulation of manganese-dependent arabidopsis serine/threonine/tyrosine protein kinase activity
    • DOI 10.1016/j.abb.2006.09.009, PII S0003986106003468
    • Reddy, M. M., and Rajasekharan, R. (2006) Role of threonine residues in the regulation of manganese-dependent Arabidopsis serine/threonine/tyrosine protein kinase activity. Arch. Biochem. Biophys. 455, 99-109 (Pubitemid 44708844)
    • (2006) Archives of Biochemistry and Biophysics , vol.455 , Issue.2 , pp. 99-109
    • Reddy, M.M.1    Rajasekharan, R.2
  • 19
    • 0024361631 scopus 로고
    • Activation of the purified protein tyrosine kinase domain of the epidermal growth factor receptor
    • Wedegaertner, P. B., and Gill, G. N. (1989) Activation of the purified protein-tyrosine kinase domain of the epidermal growth factor receptor. J. Biol. Chem. 264, 11346-11353 (Pubitemid 19168869)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.19 , pp. 11346-11353
    • Wedegaertner, P.B.1    Gill, G.N.2
  • 20
    • 0027250459 scopus 로고
    • Phosphorylase kinase, a metal ion-dependent dual specificity kinase
    • Yuan, C. J., Huang, C. Y., and Graves, D. J. (1993) Phosphorylase kinase, a metal ion-dependent dual specificity kinase. J. Biol. Chem. 268, 17683-17686
    • (1993) J. Biol. Chem. , vol.268 , pp. 17683-17686
    • Yuan, C.J.1    Huang, C.Y.2    Graves, D.J.3
  • 21
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases: Controlling activity through activation segment conformation
    • DOI 10.1016/j.molcel.2004.08.024, PII S1097276504004800
    • Nolen, B. S., Taylor, S., and Ghosh, G. (2004) Regulation of protein kinases; controlling activity through activation segment conformation. Mol. Cell 15, 661-675 (Pubitemid 39194898)
    • (2004) Molecular Cell , vol.15 , Issue.5 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 22
    • 33750456519 scopus 로고    scopus 로고
    • Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks
    • DOI 10.1016/j.cell.2006.09.026, PII S0092867406012748
    • Olsen J. V., Blagoev, B., Gnad, F., Macek, B., Kumar, C., Mortensen, P., and Mann, M. (2006) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127, 635-648 (Pubitemid 44647421)
    • (2006) Cell , vol.127 , Issue.3 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 24
    • 20444387985 scopus 로고    scopus 로고
    • Activation-loop autophosphorylation is mediated by a novel transitional intermediate form of DYRKs
    • DOI 10.1016/j.cell.2005.03.034, PII S009286740500351X
    • Lochhead, P. A., Sibbet, G., Morrice, N., and Cleghon, V. (2005) Activation-loop autophosphorylation is mediated by a novel transitional intermediate form of DYRKs. Cell 121, 925-936 (Pubitemid 40806423)
    • (2005) Cell , vol.121 , Issue.6 , pp. 925-936
    • Lochhead, P.A.1    Sibbet, G.2    Morrice, N.3    Cleghon, V.4
  • 25
    • 33745080013 scopus 로고    scopus 로고
    • Regulatory mechanisms and functions of MAP kinase signaling pathways
    • DOI 10.1080/15216540600746393, PII N771034425181
    • Imajo, M., Tsuchiya, Y., and Nishida, E. (2006) Regulatory mechanisms and functions of MAP kinase signaling pathways. IUBMB Life 58, 312-317 (Pubitemid 43880022)
    • (2006) IUBMB Life , vol.58 , Issue.5-6 , pp. 312-317
    • Imajo, M.1    Tsuchiya, Y.2    Nishida, E.3
  • 26
    • 34247865533 scopus 로고    scopus 로고
    • A chaperone-dependent GSK3β transitional intermediate mediates activation-loop autophosphorylation
    • DOI 10.1016/j.molcel.2006.10.009
    • Lochhead, P. A., Kinstrie, R., Sibbet, G., Rawjee, T., and Morrice, N. (2006) A chaperone-dependent GSK3β transitional intermediate mediates activation-loop autophosphorylation. Mol. Cell 24, 627-633 (Pubitemid 350284229)
    • (2006) Molecular Cell , vol.24 , Issue.4 , pp. 627-633
    • Lochhead, P.A.1    Kinstrie, R.2    Sibbet, G.3    Rawjee, T.4    Morrice, N.5    Cleghone, V.6
  • 28
    • 34547154729 scopus 로고    scopus 로고
    • Activation segment exchange: A common mechanism of kinase autophosphorylation?
    • DOI 10.1016/j.tibs.2007.06.004, PII S0968000407001478
    • Oliver, A. W., Knapp, S., and Pearl, L. H. (2007) Activation segment exchange: A common mechanism of kinase autophosphorylation? Trends Biochem. Sci. 32, 351-356 (Pubitemid 47126856)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.8 , pp. 351-356
    • Oliver, A.W.1    Knapp, S.2    Pearl, L.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.