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Volumn 4, Issue APR, 2013, Pages

An emerging role for PI5P in T cell biology

Author keywords

Dok proteins; Phosphoinositide; PI5P; PtdIns5P; T cell signaling

Indexed keywords

AUTOTAXIN; DOK PROTEIN; GLYCEROPHOSPHOLIPID; MYOTUBULARIN 1; NUCLEAR PROTEIN; PEPTIDES AND PROTEINS; PHOSPHATIDYLINOSITOL 3 PHOSPHATE; PHOSPHATIDYLINOSITOL 5 PHOSPHATE; PHOSPHATIDYLINOSITOL KINASE; PHOSPHATIDYLINOSITOL P2 4 PHOSPHATASE; PROTEIN ING2; PROTEIN KINASE B; PROTEIN KINASE FYN; PROTEIN KINASE LCK; T LYMPHOCYTE RECEPTOR; UNCLASSIFIED DRUG;

EID: 84883735821     PISSN: None     EISSN: 16643224     Source Type: Journal    
DOI: 10.3389/fimmu.2013.00080     Document Type: Article
Times cited : (9)

References (73)
  • 1
    • 50249105938 scopus 로고    scopus 로고
    • Tailoring T-cell receptor signals by proximal negative feedback mechanisms
    • Acuto, O., Bartolo, V. D., and Michel, F. (2008). Tailoring T-cell receptor signals by proximal negative feedback mechanisms. Nat. Rev. Immunol. 8, 699-712.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 699-712
    • Acuto, O.1    Bartolo, V.D.2    Michel, F.3
  • 2
    • 33645820226 scopus 로고    scopus 로고
    • The Arabidopsis homolog of trithorax, ATX1, binds phosphatidylinositol 5-phosphate, and the two regulate a common set of target genes
    • Alvarez-Venegas, R., Sadder, M., Hlavacka, A., Baluska, F., Xia, Y., Lu, G., et al. (2006). The Arabidopsis homolog of trithorax, ATX1, binds phosphatidylinositol 5-phosphate, and the two regulate a common set of target genes. Proc. Natl. Acad. Sci. U.S.A. 103, 6049-6054.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 6049-6054
    • Alvarez-Venegas, R.1    Sadder, M.2    Hlavacka, A.3    Baluska, F.4    Xia, Y.5    Lu, G.6
  • 3
    • 34249085248 scopus 로고    scopus 로고
    • CCR7 ligands control basal T cell motility within lymph node slices in a phosphoinositide 3-kinase-independent manner
    • Asperti-Boursin, F., Real, E., Bismuth, G., Trautmann, A., and Donnadieu, E. (2007). CCR7 ligands control basal T cell motility within lymph node slices in a phosphoinositide 3-kinase-independent manner. J. Exp. Med. 204, 1167-1179.
    • (2007) J. Exp. Med. , vol.204 , pp. 1167-1179
    • Asperti-Boursin, F.1    Real, E.2    Bismuth, G.3    Trautmann, A.4    Donnadieu, E.5
  • 4
    • 0035451761 scopus 로고    scopus 로고
    • PI 3-K and T-cell activation: limitations of T-leukemic cell lines as signaling models
    • Astoul, E., Edmunds, C., Cantrell, D. A., and Ward, S. G. (2001). PI 3-K and T-cell activation: limitations of T-leukemic cell lines as signaling models. Trends Immunol. 22, 490-496.
    • (2001) Trends Immunol. , vol.22 , pp. 490-496
    • Astoul, E.1    Edmunds, C.2    Cantrell, D.A.3    Ward, S.G.4
  • 5
    • 0037096759 scopus 로고    scopus 로고
    • Loss of phosphatase activity in myotubularin-related protein 2 is associated with Charcot-Marie-Tooth disease type 4B1
    • Berger, P., Bonneick, S., Willi, S., Wymann, M., and Suter, U. (2002). Loss of phosphatase activity in myotubularin-related protein 2 is associated with Charcot-Marie-Tooth disease type 4B1. Hum. Mol. Genet. 11, 1569-1579.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1569-1579
    • Berger, P.1    Bonneick, S.2    Willi, S.3    Wymann, M.4    Suter, U.5
  • 6
    • 0021750054 scopus 로고
    • Inositol trisphosphate, a novel second messenger in cellular signal transduction
    • Berridge, M. J., and Irvine, R. F. (1984). Inositol trisphosphate, a novel second messenger in cellular signal transduction. Nature 312, 315-321.
    • (1984) Nature , vol.312 , pp. 315-321
    • Berridge, M.J.1    Irvine, R.F.2
  • 7
    • 58549086016 scopus 로고    scopus 로고
    • Regulation of conformer-specific activation of the integrin LFA-1 by a chemokine-triggered Rho signaling module
    • Bolomini-Vittori, M., Montresor, A., Giagulli, C., Staunton, D., Rossi, B., Martinello, M., et al. (2009). Regulation of conformer-specific activation of the integrin LFA-1 by a chemokine-triggered Rho signaling module. Nat. Immunol. 10, 185-194.
    • (2009) Nat. Immunol. , vol.10 , pp. 185-194
    • Bolomini-Vittori, M.1    Montresor, A.2    Giagulli, C.3    Staunton, D.4    Rossi, B.5    Martinello, M.6
  • 8
    • 25444456370 scopus 로고    scopus 로고
    • Phosphotyrosine binding-mediated oligomerization of downstream of tyrosine kinase (Dok)-1 and Dok-2 is involved in CD2-induced Dok phosphorylation
    • Boulay, I., Nemorin, J. G., and Duplay, P. (2005). Phosphotyrosine binding-mediated oligomerization of downstream of tyrosine kinase (Dok)-1 and Dok-2 is involved in CD2-induced Dok phosphorylation. J. Immunol. 175, 4483-4489.
    • (2005) J. Immunol. , vol.175 , pp. 4483-4489
    • Boulay, I.1    Nemorin, J.G.2    Duplay, P.3
  • 9
    • 0042191732 scopus 로고    scopus 로고
    • The phosphatidylinositol (PI)-5-phosphate 4-kinase type II enzyme controls insulin signaling by regulating PI-3,4,5-trisphosphate degradation
    • Carricaburu, V., Lamia, K. A., Lo, E., Favereaux, L., Payrastre, B., Cantley, L. C., et al. (2003). The phosphatidylinositol (PI)-5-phosphate 4-kinase type II enzyme controls insulin signaling by regulating PI-3,4,5-trisphosphate degradation. Proc. Natl. Acad. Sci. U.S.A. 100, 9867-9872.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 9867-9872
    • Carricaburu, V.1    Lamia, K.A.2    Lo, E.3    Favereaux, L.4    Payrastre, B.5    Cantley, L.C.6
  • 11
    • 77949881462 scopus 로고    scopus 로고
    • The PI3K pathway as drug target in human cancer
    • Courtney, K. D., Corcoran, R. B., and Engelman, J. A. (2010). The PI3K pathway as drug target in human cancer. J. Clin. Oncol. 28, 1075-1083.
    • (2010) J. Clin. Oncol. , vol.28 , pp. 1075-1083
    • Courtney, K.D.1    Corcoran, R.B.2    Engelman, J.A.3
  • 12
    • 2942718545 scopus 로고    scopus 로고
    • PI-loting membrane traffic
    • De Matteis, M. A., and Godi, A. (2004). PI-loting membrane traffic. Nat. Cell Biol. 6, 487-492.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 487-492
    • De Matteis, M.A.1    Godi, A.2
  • 13
    • 79959542722 scopus 로고    scopus 로고
    • The CD3 zeta subunit contains a phosphoinositide-binding motif that is required for the stable accumulation of TCR-CD3 complex at the immunological synapse
    • DeFord-Watts, L. M., Dougall, D. S., Belkaya, S., Johnson, B. A., Eitson, J. L., Roybal, K. T., et al. (2011). The CD3 zeta subunit contains a phosphoinositide-binding motif that is required for the stable accumulation of TCR-CD3 complex at the immunological synapse. J. Immunol. 186, 6839-6847.
    • (2011) J. Immunol. , vol.186 , pp. 6839-6847
    • DeFord-Watts, L.M.1    Dougall, D.S.2    Belkaya, S.3    Johnson, B.A.4    Eitson, J.L.5    Roybal, K.T.6
  • 14
    • 19644388865 scopus 로고    scopus 로고
    • NMR structure of the amino-terminal domain from the Tfb1 subunit of TFIIH and characterization of its phosphoinositide and VP16 binding sites
    • Di Lello, P., Nguyen, B. D., Jones, T. N., Potempa, K., Kobor, M. S., Legault, P., et al. (2005). NMR structure of the amino-terminal domain from the Tfb1 subunit of TFIIH and characterization of its phosphoinositide and VP16 binding sites. Biochemistry 44, 7678-7686.
    • (2005) Biochemistry , vol.44 , pp. 7678-7686
    • Di Lello, P.1    Nguyen, B.D.2    Jones, T.N.3    Potempa, K.4    Kobor, M.S.5    Legault, P.6
  • 15
    • 0042817834 scopus 로고    scopus 로고
    • Phosphatidylinositol phosphate kinases put PI4,5P(2) in its place
    • Doughman, R. L., Firestone, A. J., and Anderson, R. A. (2003). Phosphatidylinositol phosphate kinases put PI4,5P(2) in its place. J. Membr. Biol. 194, 77-89.
    • (2003) J. Membr. Biol. , vol.194 , pp. 77-89
    • Doughman, R.L.1    Firestone, A.J.2    Anderson, R.A.3
  • 16
    • 15444369929 scopus 로고    scopus 로고
    • Stable activation of phosphatidylinositol 3-kinase in the T cell immunological synapse stimulates Akt signaling to FoxO1 nuclear exclusion and cell growth control
    • Fabre, S., Lang, V., Harriague, J., Jobart, A., Unterman, T. G., Trautmann, A., et al. (2005). Stable activation of phosphatidylinositol 3-kinase in the T cell immunological synapse stimulates Akt signaling to FoxO1 nuclear exclusion and cell growth control. J. Immunol. 174, 4161-4171.
    • (2005) J. Immunol. , vol.174 , pp. 4161-4171
    • Fabre, S.1    Lang, V.2    Harriague, J.3    Jobart, A.4    Unterman, T.G.5    Trautmann, A.6
  • 18
    • 0036850549 scopus 로고    scopus 로고
    • Different HATS of the ING1 gene family
    • Feng, X., Hara, Y., and Riabowol, K. (2002). Different HATS of the ING1 gene family. Trends Cell Biol. 12, 532-538.
    • (2002) Trends Cell Biol. , vol.12 , pp. 532-538
    • Feng, X.1    Hara, Y.2    Riabowol, K.3
  • 19
    • 79958101846 scopus 로고    scopus 로고
    • Misregulated alternative splicing of BIN1 is associated with T tubule alterations and muscle weakness in myotonic dystrophy
    • Fugier, C., Klein, A. F., Hammer, C., Vassilopoulos, S., Ivarsson, Y., Toussaint, A., et al. (2011). Misregulated alternative splicing of BIN1 is associated with T tubule alterations and muscle weakness in myotonic dystrophy. Nat. Med. 17, 720-725.
    • (2011) Nat. Med. , vol.17 , pp. 720-725
    • Fugier, C.1    Klein, A.F.2    Hammer, C.3    Vassilopoulos, S.4    Ivarsson, Y.5    Toussaint, A.6
  • 20
    • 17944375813 scopus 로고    scopus 로고
    • Haematopoietic cell-specific CDM family protein DOCK2 is essential for lymphocyte migration
    • Fukui, Y., Hashimoto, O., Sanui, T., Oono, T., Koga, H., Abe, M., et al. (2001). Haematopoietic cell-specific CDM family protein DOCK2 is essential for lymphocyte migration. Nature 412, 826-831.
    • (2001) Nature , vol.412 , pp. 826-831
    • Fukui, Y.1    Hashimoto, O.2    Sanui, T.3    Oono, T.4    Koga, H.5    Abe, M.6
  • 21
    • 0037158744 scopus 로고    scopus 로고
    • Dynamics of ATP-dependent chromatin assembly by ACF
    • Fyodorov, D. V., and Kadonaga, J. T. (2002). Dynamics of ATP-dependent chromatin assembly by ACF. Nature 418, 897-900.
    • (2002) Nature , vol.418 , pp. 897-900
    • Fyodorov, D.V.1    Kadonaga, J.T.2
  • 22
    • 1542427147 scopus 로고    scopus 로고
    • Functional interaction of RasGAP-binding proteins Dok-1 and Dok-2 with the Tec protein tyrosine kinase
    • Gerard, A., Favre, C., Garcon, F., Nemorin, J. G., Duplay, P., Pastor, S., et al. (2004). Functional interaction of RasGAP-binding proteins Dok-1 and Dok-2 with the Tec protein tyrosine kinase. Oncogene 23, 1594-1598.
    • (2004) Oncogene , vol.23 , pp. 1594-1598
    • Gerard, A.1    Favre, C.2    Garcon, F.3    Nemorin, J.G.4    Duplay, P.5    Pastor, S.6
  • 24
    • 0038784526 scopus 로고    scopus 로고
    • The PHD finger of the chromatin-associated protein ING2 functions as a nuclear phosphoinositide receptor
    • Gozani, O., Karuman, P., Jones, D. R., Ivanov, D., Cha, J., Lugovskoy, A. A., et al. (2003). The PHD finger of the chromatin-associated protein ING2 functions as a nuclear phosphoinositide receptor. Cell 114, 99-111.
    • (2003) Cell , vol.114 , pp. 99-111
    • Gozani, O.1    Karuman, P.2    Jones, D.R.3    Ivanov, D.4    Cha, J.5    Lugovskoy, A.A.6
  • 25
    • 84856283782 scopus 로고    scopus 로고
    • The emerging role of PtdIns5P: another signalling phosphoinositide takes its place
    • Grainger, D. L., Tavelis, C., Ryan, A. J., and Hinchliffe, K. A. (2012). The emerging role of PtdIns5P: another signalling phosphoinositide takes its place. Biochem. Soc. Trans. 40, 257-261.
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 257-261
    • Grainger, D.L.1    Tavelis, C.2    Ryan, A.J.3    Hinchliffe, K.A.4
  • 26
    • 64249093846 scopus 로고    scopus 로고
    • Cutting edge: Dok-1 and Dok-2 adaptor molecules are regulated by phosphatidylinositol 5-phosphate production in T cells
    • Guittard, G., Gerard, A., Dupuis-Coronas, S., Tronchere, H., Mortier, E., Favre, C., et al. (2009). Cutting edge: Dok-1 and Dok-2 adaptor molecules are regulated by phosphatidylinositol 5-phosphate production in T cells. J. Immunol. 182, 3974-3978.
    • (2009) J. Immunol. , vol.182 , pp. 3974-3978
    • Guittard, G.1    Gerard, A.2    Dupuis-Coronas, S.3    Tronchere, H.4    Mortier, E.5    Favre, C.6
  • 27
    • 77952958465 scopus 로고    scopus 로고
    • Evidence for a positive role of PtdIns5P in T-cell signal transduction pathways
    • Guittard, G., Mortier, E., Tronchere, H., Firaguay, G., Gerard, A., Zimmermann, P., et al. (2010). Evidence for a positive role of PtdIns5P in T-cell signal transduction pathways. FEBS Lett. 584, 2455-2460.
    • (2010) FEBS Lett. , vol.584 , pp. 2455-2460
    • Guittard, G.1    Mortier, E.2    Tronchere, H.3    Firaguay, G.4    Gerard, A.5    Zimmermann, P.6
  • 28
    • 33748193467 scopus 로고    scopus 로고
    • Nuclear PtdIns5P as a transducer of stress signaling: an in vivo role for PIP4Kbeta
    • Jones, D. R., Bultsma, Y., Keune, W. J., Halstead, J. R., Elouarrat, D., Mohammed, S., et al. (2006). Nuclear PtdIns5P as a transducer of stress signaling: an in vivo role for PIP4Kbeta. Mol. Cell 23, 685-695.
    • (2006) Mol. Cell , vol.23 , pp. 685-695
    • Jones, D.R.1    Bultsma, Y.2    Keune, W.J.3    Halstead, J.R.4    Elouarrat, D.5    Mohammed, S.6
  • 29
    • 0036120635 scopus 로고    scopus 로고
    • The PHD type zinc finger is an integral part of the CBP acetyltransferase domain
    • Kalkhoven, E., Teunissen, H., Houweling, A., Verrijzer, C. P., and Zantema, A. (2002). The PHD type zinc finger is an integral part of the CBP acetyltransferase domain. Mol. Cell. Biol. 22, 1961-1970.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1961-1970
    • Kalkhoven, E.1    Teunissen, H.2    Houweling, A.3    Verrijzer, C.P.4    Zantema, A.5
  • 30
    • 79955062048 scopus 로고    scopus 로고
    • The Shigella flexneri type three secretion system effector IpgD inhibits T cell migration by manipulating host phosphoinositide metabolism
    • Konradt, C., Frigimelica, E., Nothelfer, K., Puhar, A., Salgado-Pabon, W., Di Bartolo, V., et al. (2011). The Shigella flexneri type three secretion system effector IpgD inhibits T cell migration by manipulating host phosphoinositide metabolism. Cell Host Microbe 9, 263-272.
    • (2011) Cell Host Microbe , vol.9 , pp. 263-272
    • Konradt, C.1    Frigimelica, E.2    Nothelfer, K.3    Puhar, A.4    Salgado-Pabon, W.5    Di Bartolo, V.6
  • 31
    • 0031665007 scopus 로고    scopus 로고
    • Characterization of the myotubularin dual specificity phosphatase gene family from yeast to human
    • Laporte, J., Blondeau, F., Buj-Bello, A., Tentler, D., Kretz, C., Dahl, N., et al. (1998). Characterization of the myotubularin dual specificity phosphatase gene family from yeast to human. Hum. Mol. Genet. 7, 1703-1712.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1703-1712
    • Laporte, J.1    Blondeau, F.2    Buj-Bello, A.3    Tentler, D.4    Kretz, C.5    Dahl, N.6
  • 32
    • 9044222886 scopus 로고    scopus 로고
    • A gene mutated in X-linked myotubular myopathy defines a new putative tyrosine phosphatase family conserved in yeast
    • Laporte, J., Hu, L. J., Kretz, C., Mandel, J. L., Kioschis, P., Coy, J. F., et al. (1996). A gene mutated in X-linked myotubular myopathy defines a new putative tyrosine phosphatase family conserved in yeast. Nat. Genet. 13, 175-182.
    • (1996) Nat. Genet. , vol.13 , pp. 175-182
    • Laporte, J.1    Hu, L.J.2    Kretz, C.3    Mandel, J.L.4    Kioschis, P.5    Coy, J.F.6
  • 33
    • 49949094771 scopus 로고    scopus 로고
    • Raft nanodomains contribute to Akt/PKB plasma membrane recruitment and activation
    • Lasserre, R., Guo, X. J., Conchonaud, F., Hamon, Y., Hawchar, O., Bernard, A. M., et al. (2008). Raft nanodomains contribute to Akt/PKB plasma membrane recruitment and activation. Nat. Chem. Biol. 4, 538-547.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 538-547
    • Lasserre, R.1    Guo, X.J.2    Conchonaud, F.3    Hamon, Y.4    Hawchar, O.5    Bernard, A.M.6
  • 34
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon, M. A. (2008). Membrane recognition by phospholipid-binding domains. Nat. Rev. Mol. Cell Biol. 9, 99-111.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 35
    • 33746820982 scopus 로고    scopus 로고
    • Systematic analysis of myotubularins: heteromeric interactions, subcellular localisation and endosome related functions
    • Lorenzo, O., Urbe, S., and Clague, M. J. (2006). Systematic analysis of myotubularins: heteromeric interactions, subcellular localisation and endosome related functions. J. Cell Sci. 119, 2953-2959.
    • (2006) J. Cell Sci. , vol.119 , pp. 2953-2959
    • Lorenzo, O.1    Urbe, S.2    Clague, M.J.3
  • 36
    • 33947719117 scopus 로고    scopus 로고
    • Alteration of epithelial structure and function associated with PtdIns(4,5)P2 degradation by a bacterial phosphatase
    • Mason, D., Mallo, G. V., Terebiznik, M. R., Payrastre, B., Finlay, B. B., Brumell, J. H., et al. (2007). Alteration of epithelial structure and function associated with PtdIns(4,5)P2 degradation by a bacterial phosphatase. J. Gen. Physiol. 129, 267-283.
    • (2007) J. Gen. Physiol. , vol.129 , pp. 267-283
    • Mason, D.1    Mallo, G.V.2    Terebiznik, M.R.3    Payrastre, B.4    Finlay, B.B.5    Brumell, J.H.6
  • 37
    • 59849125052 scopus 로고    scopus 로고
    • Mutations in phosphoinositide metabolizing enzymes and human disease
    • McCrea, H. J., and De Camilli, P. (2009). Mutations in phosphoinositide metabolizing enzymes and human disease. Physiology (Bethesda) 24, 8-16.
    • (2009) Physiology (Bethesda) , vol.24 , pp. 8-16
    • McCrea, H.J.1    De Camilli, P.2
  • 39
    • 43249090885 scopus 로고    scopus 로고
    • PI5KI-dependent signals are critical regulators of the cytolytic secretory pathway
    • Micucci, F., Capuano, C., Marchetti, E., Piccoli, M., Frati, L., Santoni, A., et al. (2008). PI5KI-dependent signals are critical regulators of the cytolytic secretory pathway. Blood 111, 4165-4172.
    • (2008) Blood , vol.111 , pp. 4165-4172
    • Micucci, F.1    Capuano, C.2    Marchetti, E.3    Piccoli, M.4    Frati, L.5    Santoni, A.6
  • 40
    • 34548341774 scopus 로고    scopus 로고
    • Mutations in amphiphysin 2 (BIN1) disrupt interaction with dynamin 2 and cause autosomal recessive centronuclear myopathy
    • Nicot, A. S., Toussaint, A., Tosch, V., Kretz, C., Wallgren-Pettersson, C., Iwarsson, E., et al. (2007). Mutations in amphiphysin 2 (BIN1) disrupt interaction with dynamin 2 and cause autosomal recessive centronuclear myopathy. Nat. Genet. 39, 1134-1139.
    • (2007) Nat. Genet. , vol.39 , pp. 1134-1139
    • Nicot, A.S.1    Toussaint, A.2    Tosch, V.3    Kretz, C.4    Wallgren-Pettersson, C.5    Iwarsson, E.6
  • 41
    • 18644379244 scopus 로고    scopus 로고
    • Conversion of PtdIns(4,5)P(2) into PtdIns(5)P by the S flexneri effector IpgD reorganizes host cell morphology.
    • Niebuhr, K., Giuriato, S., Pedron, T., Philpott, D. J., Gaits, F., Sable, J., et al. (2002). Conversion of PtdIns(4,5)P(2) into PtdIns(5)P by the S. flexneri effector IpgD reorganizes host cell morphology. EMBO J. 21, 5069-5078.
    • (2002) EMBO J. , vol.21 , pp. 5069-5078
    • Niebuhr, K.1    Giuriato, S.2    Pedron, T.3    Philpott, D.J.4    Gaits, F.5    Sable, J.6
  • 42
    • 77953911933 scopus 로고    scopus 로고
    • Constitutively active Lck kinase in T cells drives antigen receptor signal transduction
    • Nika, K., Soldani, C., Salek, M., Paster, W., Gray, A., Etzensperger, R., et al. (2010). Constitutively active Lck kinase in T cells drives antigen receptor signal transduction. Immunity 32, 766-777.
    • (2010) Immunity , vol.32 , pp. 766-777
    • Nika, K.1    Soldani, C.2    Salek, M.3    Paster, W.4    Gray, A.5    Etzensperger, R.6
  • 43
    • 84871920676 scopus 로고    scopus 로고
    • Production of phosphatidylinositol 5-phosphate via PIKfyve and MTMR3 regulates cell migration
    • Oppelt, A., Lobert, V. H., Haglund, K., Mackey, A. M., Rameh, L. E., Liestol, K., et al. (2012). Production of phosphatidylinositol 5-phosphate via PIKfyve and MTMR3 regulates cell migration. EMBO Rep. 14, 57-64.
    • (2012) EMBO Rep. , vol.14 , pp. 57-64
    • Oppelt, A.1    Lobert, V.H.2    Haglund, K.3    Mackey, A.M.4    Rameh, L.E.5    Liestol, K.6
  • 44
    • 4644335846 scopus 로고    scopus 로고
    • A PTEN-like phosphatase with a novel substrate specificity
    • Pagliarini, D. J., Worby, C. A., and Dixon, J. E. (2004). A PTEN-like phosphatase with a novel substrate specificity. J. Biol. Chem. 279, 38590-38596.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38590-38596
    • Pagliarini, D.J.1    Worby, C.A.2    Dixon, J.E.3
  • 45
    • 33644850315 scopus 로고    scopus 로고
    • PtdIns5P activates the host cell PI3-kinase/Akt pathway during Shigella flexneri infection
    • Pendaries, C., Tronchere, H., Arbibe, L., Mounier, J., Gozani, O., Cantley, L., et al. (2006). PtdIns5P activates the host cell PI3-kinase/Akt pathway during Shigella flexneri infection. EMBO J. 25, 1024-1034.
    • (2006) EMBO J. , vol.25 , pp. 1024-1034
    • Pendaries, C.1    Tronchere, H.2    Arbibe, L.3    Mounier, J.4    Gozani, O.5    Cantley, L.6
  • 47
    • 0030721527 scopus 로고    scopus 로고
    • A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate
    • Rameh, L. E., Tolias, K. F., Duckworth, B. C., and Cantley, L. C. (1997). A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate. Nature 390, 192-196.
    • (1997) Nature , vol.390 , pp. 192-196
    • Rameh, L.E.1    Tolias, K.F.2    Duckworth, B.C.3    Cantley, L.C.4
  • 48
    • 80053111626 scopus 로고    scopus 로고
    • Shigella flexneri infection generates the lipid PI5P to alter endocytosis and prevent termination of EGFR signaling
    • Ramel, D., Lagarrigue, F., Pons, V., Mounier, J., Dupuis-Coronas, S., Chicanne, G., et al. (2011). Shigella flexneri infection generates the lipid PI5P to alter endocytosis and prevent termination of EGFR signaling. Sci. Signal. 4, ra61.
    • (2011) Sci. Signal. , vol.4
    • Ramel, D.1    Lagarrigue, F.2    Pons, V.3    Mounier, J.4    Dupuis-Coronas, S.5    Chicanne, G.6
  • 49
    • 77954930785 scopus 로고    scopus 로고
    • A novel HPLC-based approach makes possible the spatial characterization of cellular PtdIns5P and other phosphoinositides
    • Sarkes, D., and Rameh, L. E. (2010). A novel HPLC-based approach makes possible the spatial characterization of cellular PtdIns5P and other phosphoinositides. Biochem. J. 428, 375-384.
    • (2010) Biochem. J. , vol.428 , pp. 375-384
    • Sarkes, D.1    Rameh, L.E.2
  • 50
    • 0037033079 scopus 로고    scopus 로고
    • Phosphatidylinositol 5-phosphate biosynthesis is linked to PIKfyve and is involved in osmotic response pathway in mammalian cells
    • Sbrissa, D., Ikonomov, O. C., Deeb, R., and Shisheva, A. (2002). Phosphatidylinositol 5-phosphate biosynthesis is linked to PIKfyve and is involved in osmotic response pathway in mammalian cells. J. Biol. Chem. 277, 47276-47284.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47276-47284
    • Sbrissa, D.1    Ikonomov, O.C.2    Deeb, R.3    Shisheva, A.4
  • 51
    • 84865140750 scopus 로고    scopus 로고
    • Functional dissociation between PIKfyve-synthesized PtdIns5P and PtdIns(3,5)P2 by means of the PIKfyve inhibitor YM201636
    • Sbrissa, D., Ikonomov, O. C., Filios, C., Delvecchio, K., and Shisheva, A. (2012). Functional dissociation between PIKfyve-synthesized PtdIns5P and PtdIns(3,5)P2 by means of the PIKfyve inhibitor YM201636. Am. J. Physiol. Cell Physiol. 303, C436-446.
    • (2012) Am. J. Physiol. Cell Physiol. , vol.303
    • Sbrissa, D.1    Ikonomov, O.C.2    Filios, C.3    Delvecchio, K.4    Shisheva, A.5
  • 52
    • 0033618375 scopus 로고    scopus 로고
    • PIKfyve, a mammalian ortholog of yeast Fab1p lipid kinase, synthesizes 5-phosphoinositides
    • Sbrissa, D., Ikonomov, O. C., and Shisheva, A. (1999). PIKfyve, a mammalian ortholog of yeast Fab1p lipid kinase, synthesizes 5-phosphoinositides. Effect of insulin. J. Biol. Chem. 274, 21589-21597.
    • (1999) Effect of insulin. J. Biol. Chem. , vol.274 , pp. 21589-21597
    • Sbrissa, D.1    Ikonomov, O.C.2    Shisheva, A.3
  • 53
    • 8644279885 scopus 로고    scopus 로고
    • Role for a novel signaling intermediate, phosphatidylinositol 5-phosphate, in insulin-regulated F-actin stress fiber breakdown and GLUT4 translocation
    • Sbrissa, D., Ikonomov, O. C., Strakova, J., and Shisheva, A. (2004). Role for a novel signaling intermediate, phosphatidylinositol 5-phosphate, in insulin-regulated F-actin stress fiber breakdown and GLUT4 translocation. Endocrinology 145, 4853-4865.
    • (2004) Endocrinology , vol.145 , pp. 4853-4865
    • Sbrissa, D.1    Ikonomov, O.C.2    Strakova, J.3    Shisheva, A.4
  • 54
    • 0037452874 scopus 로고    scopus 로고
    • Phosphatidylinositol-5-phosphate activation and conserved substrate specificity of the myotubularin phosphatidylinositol 3-phosphatases
    • Schaletzky, J., Dove, S. K., Short, B., Lorenzo, O., Clague, M. J., and Barr, F. A. (2003). Phosphatidylinositol-5-phosphate activation and conserved substrate specificity of the myotubularin phosphatidylinositol 3-phosphatases. Curr. Biol. 13, 504-509.
    • (2003) Curr. Biol. , vol.13 , pp. 504-509
    • Schaletzky, J.1    Dove, S.K.2    Short, B.3    Lorenzo, O.4    Clague, M.J.5    Barr, F.A.6
  • 55
    • 80052946904 scopus 로고    scopus 로고
    • Feedback circuits monitor and adjust basal Lck-dependent events in T cell receptor signaling
    • Schoenborn, J. R., Tan, Y. X., Zhang, C., Shokat, K. M., and Weiss, A. (2011). Feedback circuits monitor and adjust basal Lck-dependent events in T cell receptor signaling. Sci. Signal. 4, ra59.
    • (2011) Sci. Signal. , vol.4
    • Schoenborn, J.R.1    Tan, Y.X.2    Zhang, C.3    Shokat, K.M.4    Weiss, A.5
  • 57
    • 84857875585 scopus 로고    scopus 로고
    • PI3K signalling in B- and T-lymphocytes: new developments and therapeutic advances
    • So, L., and Fruman, D. A. (2012). PI3K signalling in B- and T-lymphocytes: new developments and therapeutic advances. Biochem. J. 442, 465-481.
    • (2012) Biochem. J. , vol.442 , pp. 465-481
    • So, L.1    Fruman, D.A.2
  • 58
    • 17644405474 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-phosphate phosphatase myotubularin-related protein 6 (MTMR6) is a negative regulator of the Ca2+-activated K+ channel KCa3.1.
    • Srivastava, S., Li, Z., Lin, L., Liu, G., Ko, K., Coetzee, W. A., et al. (2005). The phosphatidylinositol 3-phosphate phosphatase myotubularin-related protein 6 (MTMR6) is a negative regulator of the Ca2+-activated K+ channel KCa3.1. Mol. Cell. Biol. 25, 3630-3638.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 3630-3638
    • Srivastava, S.1    Li, Z.2    Lin, L.3    Liu, G.4    Ko, K.5    Coetzee, W.A.6
  • 59
    • 1342304076 scopus 로고    scopus 로고
    • Production of phosphatidylinositol 5-phosphate by the phosphoinositide 3-phosphatase myotubularin in mammalian cells
    • Tronchere, H., Laporte, J., Pendaries, C., Chaussade, C., Liaubet, L., Pirola, L., et al. (2004). Production of phosphatidylinositol 5-phosphate by the phosphoinositide 3-phosphatase myotubularin in mammalian cells. J. Biol. Chem. 279, 7304-7312.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7304-7312
    • Tronchere, H.1    Laporte, J.2    Pendaries, C.3    Chaussade, C.4    Liaubet, L.5    Pirola, L.6
  • 60
    • 30044446496 scopus 로고    scopus 로고
    • The identification and characterization of two phosphatidylinositol-4,5-bisphosphate 4-phosphatases
    • Ungewickell, A., Hugge, C., Kisseleva, M., Chang, S. C., Zou, J., Feng, Y., et al. (2005). The identification and characterization of two phosphatidylinositol-4,5-bisphosphate 4-phosphatases. Proc. Natl. Acad. Sci. U.S.A. 102, 18854-18859.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 18854-18859
    • Ungewickell, A.1    Hugge, C.2    Kisseleva, M.3    Chang, S.C.4    Zou, J.5    Feng, Y.6
  • 61
    • 80055083463 scopus 로고    scopus 로고
    • Genetic interaction between MTMR2 and FIG4 phospholipid phosphatases involved in Charcot-Marie-Tooth neuropathies
    • doi:10.1371/journal.pgen.1002319
    • Vaccari, I., Dina, G., Tronchere, H., Kaufman, E., Chicanne, G., Cerri, F., et al. (2011). Genetic interaction between MTMR2 and FIG4 phospholipid phosphatases involved in Charcot-Marie-Tooth neuropathies. PLoS Genet. 7:e1002319. doi:10.1371/journal.pgen.1002319
    • (2011) PLoS Genet. , vol.7
    • Vaccari, I.1    Dina, G.2    Tronchere, H.3    Kaufman, E.4    Chicanne, G.5    Cerri, F.6
  • 62
    • 69649087487 scopus 로고    scopus 로고
    • The beta- and gamma-isoforms of type I PIP5K regulate distinct stages of Ca2+ signaling in mast cells
    • Vasudevan, L., Jeromin, A., Volpicelli-Daley, L., De Camilli, P., Holowka, D., and Baird, B. (2009). The beta- and gamma-isoforms of type I PIP5K regulate distinct stages of Ca2+ signaling in mast cells. J. Cell Sci. 122, 2567-2574.
    • (2009) J. Cell Sci. , vol.122 , pp. 2567-2574
    • Vasudevan, L.1    Jeromin, A.2    Volpicelli-Daley, L.3    De Camilli, P.4    Holowka, D.5    Baird, B.6
  • 63
    • 58249110560 scopus 로고    scopus 로고
    • DNA-binding and -bending activities of SAP30L and SAP30 are mediated by a zinc-dependent module and monophosphoinositides
    • Viiri, K. M., Janis, J., Siggers, T., Heinonen, T. Y., Valjakka, J., Bulyk, M. L., et al. (2009). DNA-binding and -bending activities of SAP30L and SAP30 are mediated by a zinc-dependent module and monophosphoinositides. Mol. Cell. Biol. 29, 342-356.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 342-356
    • Viiri, K.M.1    Janis, J.2    Siggers, T.3    Heinonen, T.Y.4    Valjakka, J.5    Bulyk, M.L.6
  • 64
    • 0035899863 scopus 로고    scopus 로고
    • Characterization of MTMR3. an inositol lipid. 3-phosphatase with novel substrate specificity
    • Walker, D. M., Urbe, S., Dove, S. K., Tenza, D., Raposo, G., and Clague, M. J. (2001). Characterization of MTMR3. an inositol lipid 3-phosphatase with novel substrate specificity. Curr. Biol. 11, 1600-1605.
    • (2001) Curr. Biol. , vol.11 , pp. 1600-1605
    • Walker, D.M.1    Urbe, S.2    Dove, S.K.3    Tenza, D.4    Raposo, G.5    Clague, M.J.6
  • 65
    • 0026502874 scopus 로고
    • Regulation of D-3 phosphoinositides during T cell activation via the T cell antigen receptor/CD3 complex and CD2 antigens
    • Ward, S. G., Ley, S. C., Macphee, C., and Cantrell, D. A. (1992). Regulation of D-3 phosphoinositides during T cell activation via the T cell antigen receptor/CD3 complex and CD2 antigens. Eur. J. Immunol. 22, 45-49.
    • (1992) Eur. J. Immunol. , vol.22 , pp. 45-49
    • Ward, S.G.1    Ley, S.C.2    Macphee, C.3    Cantrell, D.A.4
  • 66
    • 78049522007 scopus 로고    scopus 로고
    • PIPKI gamma 90 negatively regulates LFA-1-mediated adhesion and activation in antigen-induced CD4+ T cells
    • Wernimont, S. A., Legate, K. R., Simonson, W. T., Fassler, R., and Huttenlocher, A. (2010). PIPKI gamma 90 negatively regulates LFA-1-mediated adhesion and activation in antigen-induced CD4+ T cells. J. Immunol. 185, 4714-4723.
    • (2010) J. Immunol. , vol.185 , pp. 4714-4723
    • Wernimont, S.A.1    Legate, K.R.2    Simonson, W.T.3    Fassler, R.4    Huttenlocher, A.5
  • 67
    • 0023897684 scopus 로고
    • Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate
    • Whitman, M., Downes, C. P., Keeler, M., Keller, T., and Cantley, L. (1988). Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate. Nature 332, 644-646.
    • (1988) Nature , vol.332 , pp. 644-646
    • Whitman, M.1    Downes, C.P.2    Keeler, M.3    Keller, T.4    Cantley, L.5
  • 68
    • 41449083237 scopus 로고    scopus 로고
    • Regulation of extranuclear PtdIns5P production by phosphatidylinositol phosphate 4-kinase 2alpha
    • Wilcox, A., and Hinchliffe, K. A. (2008). Regulation of extranuclear PtdIns5P production by phosphatidylinositol phosphate 4-kinase 2alpha. FEBS Lett. 582, 1391-1394.
    • (2008) FEBS Lett. , vol.582 , pp. 1391-1394
    • Wilcox, A.1    Hinchliffe, K.A.2
  • 69
    • 0037174928 scopus 로고    scopus 로고
    • SKAP55 recruits to lipid rafts and positively mediates the MAPK pathway upon T cell receptor activation
    • Wu, L., Yu, Z., and Shen, S. H. (2002). SKAP55 recruits to lipid rafts and positively mediates the MAPK pathway upon T cell receptor activation. J. Biol. Chem. 277, 40420-40427.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40420-40427
    • Wu, L.1    Yu, Z.2    Shen, S.H.3
  • 70
    • 0035167696 scopus 로고    scopus 로고
    • Tec kinase signaling in T cells is regulated by phosphatidylinositol 3-kinase and the Tec Pleckstrin homology domain
    • Yang, W. C., Ching, K. A., Tsoukas, C. D., and Berg, L. J. (2001). Tec kinase signaling in T cells is regulated by phosphatidylinositol 3-kinase and the Tec Pleckstrin homology domain. J. Immunol. 166, 387-395.
    • (2001) J. Immunol. , vol.166 , pp. 387-395
    • Yang, W.C.1    Ching, K.A.2    Tsoukas, C.D.3    Berg, L.J.4
  • 71
    • 79958034094 scopus 로고    scopus 로고
    • Mitochondrial phosphatase PTPMT1 is essential for cardiolipin biosynthesis
    • Zhang, J., Guan, Z., Murphy, A. N., Wiley, S. E., Perkins, G. A., Worby, C. A., et al. (2011). Mitochondrial phosphatase PTPMT1 is essential for cardiolipin biosynthesis. Cell Metab. 13, 690-700.
    • (2011) Cell Metab. , vol.13 , pp. 690-700
    • Zhang, J.1    Guan, Z.2    Murphy, A.N.3    Wiley, S.E.4    Perkins, G.A.5    Worby, C.A.6
  • 72
    • 84867908738 scopus 로고    scopus 로고
    • In vivo, Pikfyve generates PI(3,5)P2, which serves as both a signaling lipid and the major precursor for PI5P
    • Zolov, S. N., Bridges, D., Zhang, Y., Lee, W. W., Riehle, E., Verma, R., et al. (2012). In vivo, Pikfyve generates PI(3,5)P2, which serves as both a signaling lipid and the major precursor for PI5P. Proc. Natl. Acad. Sci. U.S.A. 109, 17472-17477.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 17472-17477
    • Zolov, S.N.1    Bridges, D.2    Zhang, Y.3    Lee, W.W.4    Riehle, E.5    Verma, R.6
  • 73
    • 36749043176 scopus 로고    scopus 로고
    • Type I phosphatidylinositol-4,5-bisphosphate 4-phosphatase regulates stress-induced apoptosis
    • Zou, J., Marjanovic, J., Kisseleva, M. V., Wilson, M., and Majerus, P. W. (2007). Type I phosphatidylinositol-4,5-bisphosphate 4-phosphatase regulates stress-induced apoptosis. Proc. Natl. Acad. Sci. U.S.A. 104, 16834-16839.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 16834-16839
    • Zou, J.1    Marjanovic, J.2    Kisseleva, M.V.3    Wilson, M.4    Majerus, P.W.5


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