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Volumn 50, Issue 2, 2011, Pages 157-167

The endo-lysosomal system as an NAADP-sensitive acidic Ca2+ store: Role for the two-pore channels

Author keywords

Acidic calcium stores; Calcium; Endosomes; Lysosomes; NAADP; TPC1; TPC2; TPCN1; TPCN2; Two pore channels

Indexed keywords

CALCIUM CHANNEL; CALCIUM ION; NICOTINIC ACID ADENINE DINUCLEOTIDE PHOSPHATE; TWO PORE CHANNEL; UNCLASSIFIED DRUG;

EID: 80051474461     PISSN: 01434160     EISSN: 15321991     Source Type: Journal    
DOI: 10.1016/j.ceca.2011.03.011     Document Type: Review
Times cited : (59)

References (103)
  • 2
    • 0037941588 scopus 로고    scopus 로고
    • When calcium goes wrong: genetic alterations of a ubiquitous signaling route
    • Rizzuto R., Pozzan T. When calcium goes wrong: genetic alterations of a ubiquitous signaling route. Nat. Genet. 2003, 34:135-141.
    • (2003) Nat. Genet. , vol.34 , pp. 135-141
    • Rizzuto, R.1    Pozzan, T.2
  • 3
    • 37149029370 scopus 로고    scopus 로고
    • Calcium signaling
    • Clapham D.E. Calcium signaling. Cell 2007, 131:1047-1058.
    • (2007) Cell , vol.131 , pp. 1047-1058
    • Clapham, D.E.1
  • 4
    • 0033105984 scopus 로고    scopus 로고
    • Molecular properties of inositol 1,4,5-trisphosphate receptors
    • Patel S., Joseph S.K., Thomas A.P. Molecular properties of inositol 1,4,5-trisphosphate receptors. Cell Calcium 1999, 25:247-264.
    • (1999) Cell Calcium , vol.25 , pp. 247-264
    • Patel, S.1    Joseph, S.K.2    Thomas, A.P.3
  • 5
    • 0033378368 scopus 로고    scopus 로고
    • Expression of inositol trisphosphate receptors
    • Taylor C.W., Genazzani A.A., Morris S.A. Expression of inositol trisphosphate receptors. Cell Calcium 1999, 26:237-251.
    • (1999) Cell Calcium , vol.26 , pp. 237-251
    • Taylor, C.W.1    Genazzani, A.A.2    Morris, S.A.3
  • 7
    • 0345609814 scopus 로고    scopus 로고
    • Mechanisms of calcium signaling by cyclic ADP-ribose and NAADP
    • Lee H.C. Mechanisms of calcium signaling by cyclic ADP-ribose and NAADP. Physiol. Rev. 1997, 77:1133-1164.
    • (1997) Physiol. Rev. , vol.77 , pp. 1133-1164
    • Lee, H.C.1
  • 8
    • 0036788917 scopus 로고    scopus 로고
    • Ryanodine receptor calcium release channels
    • Fill M., Copello J.A. Ryanodine receptor calcium release channels. Physiol. Rev. 2002, 82:893-922.
    • (2002) Physiol. Rev. , vol.82 , pp. 893-922
    • Fill, M.1    Copello, J.A.2
  • 9
    • 0037418583 scopus 로고    scopus 로고
    • Calcium signaling: NAADP ascends as a new messenger
    • Lee H.C. Calcium signaling: NAADP ascends as a new messenger. Curr. Biol. 2003, 13:R186-R188.
    • (2003) Curr. Biol. , vol.13
    • Lee, H.C.1
  • 10
    • 1242321159 scopus 로고    scopus 로고
    • 2+ release-a new signaling pathway
    • 2+ release-a new signaling pathway. Biol. Cell 2004, 96:19-28.
    • (2004) Biol. Cell , vol.96 , pp. 19-28
    • Patel, S.1
  • 11
    • 0028950282 scopus 로고
    • A derivative of NADP mobilizes calcium stores insensitive to inositol trisphosphate and cyclic ADP-ribose
    • Lee H.C., Aarhus R. A derivative of NADP mobilizes calcium stores insensitive to inositol trisphosphate and cyclic ADP-ribose. J. Biol. Chem. 1995, 270:2152-2157.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2152-2157
    • Lee, H.C.1    Aarhus, R.2
  • 12
  • 13
    • 11144227270 scopus 로고    scopus 로고
    • Lysosome-sarcoplasmic reticulum junctions: a trigger zone for calcium signalling by NAADP and endothelin-1
    • Kinnear N.P., Boittin F.X., Thomas J.M., Galione A., Evans A.M. Lysosome-sarcoplasmic reticulum junctions: a trigger zone for calcium signalling by NAADP and endothelin-1. J. Biol. Chem. 2004, 279:54319-54326.
    • (2004) J. Biol. Chem. , vol.279 , pp. 54319-54326
    • Kinnear, N.P.1    Boittin, F.X.2    Thomas, J.M.3    Galione, A.4    Evans, A.M.5
  • 15
    • 73649108888 scopus 로고    scopus 로고
    • 2+ signaling contributes to angiotensin II-induced activation of hepatic stellate cells: attenuation of hepatic fibrosis by CD38 ablation
    • 2+ signaling contributes to angiotensin II-induced activation of hepatic stellate cells: attenuation of hepatic fibrosis by CD38 ablation. J. Biol. Chem. 2010, 285:576-582.
    • (2010) J. Biol. Chem. , vol.285 , pp. 576-582
    • Kim, S.Y.1    Cho, B.H.2    Kim, U.H.3
  • 16
    • 78649670802 scopus 로고    scopus 로고
    • 2+ mobilization from lysosomes in pancreatic acinar cells
    • 2+ mobilization from lysosomes in pancreatic acinar cells. J. Biol. Chem. 2010, 285:38251-38259.
    • (2010) J. Biol. Chem. , vol.285 , pp. 38251-38259
    • Cosker, F.1    Cheviron, N.2    Yamasaki, M.3
  • 18
    • 0033522228 scopus 로고    scopus 로고
    • 2+-signalling patterns by NAADP in pancreatic acinar cells
    • 2+-signalling patterns by NAADP in pancreatic acinar cells. Nature 1999, 398:74-76.
    • (1999) Nature , vol.398 , pp. 74-76
    • Cancela, J.M.1    Churchill, G.C.2    Galione, A.3
  • 20
    • 78649721315 scopus 로고    scopus 로고
    • NAADP as an intracellular messenger regulating lysosomal calcium-release channels
    • Galione A., Morgan A.J., Arredouani A., et al. NAADP as an intracellular messenger regulating lysosomal calcium-release channels. Biochem. Soc. Trans. 2010, 38:1424-1431.
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 1424-1431
    • Galione, A.1    Morgan, A.J.2    Arredouani, A.3
  • 24
    • 78549238600 scopus 로고    scopus 로고
    • Acidic NAADP-sensitive calcium stores in the endothelium: agonist-specific recruitment and role in regulating blood pressure
    • Brailoiu G.C., Gurzu B., Gao X., et al. Acidic NAADP-sensitive calcium stores in the endothelium: agonist-specific recruitment and role in regulating blood pressure. J. Biol. Chem. 2010, 285:37133-37137.
    • (2010) J. Biol. Chem. , vol.285 , pp. 37133-37137
    • Brailoiu, G.C.1    Gurzu, B.2    Gao, X.3
  • 25
    • 0023219685 scopus 로고
    • Pyridine nucleotide metabolites stimulate calcium release from sea urchin egg microsomes desensitized to inositol trisphosphate
    • Clapper D.L., Walseth T.F., Dargie P.J., Lee H.C. Pyridine nucleotide metabolites stimulate calcium release from sea urchin egg microsomes desensitized to inositol trisphosphate. J. Biol. Chem. 1987, 262:9561-9568.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9561-9568
    • Clapper, D.L.1    Walseth, T.F.2    Dargie, P.J.3    Lee, H.C.4
  • 26
    • 0029870401 scopus 로고    scopus 로고
    • 2+ from a thapsigargin-insensitive pool
    • 2+ from a thapsigargin-insensitive pool. Biochem. J. 1996, 315:721-725.
    • (1996) Biochem. J. , vol.315 , pp. 721-725
    • Genazzani, A.A.1    Galione, A.2
  • 27
    • 0034496224 scopus 로고    scopus 로고
    • Functional visualisation of the separate but interacting calcium stores sensitive to NAADP and cyclic ADP-ribose
    • Lee H.C., Aarhus R. Functional visualisation of the separate but interacting calcium stores sensitive to NAADP and cyclic ADP-ribose. J. Cell Sci. 2000, 113:4413-4420.
    • (2000) J. Cell Sci. , vol.113 , pp. 4413-4420
    • Lee, H.C.1    Aarhus, R.2
  • 29
    • 0021426953 scopus 로고
    • Intralysosomal hydrolysis of glycyl-l-phenylalanine 2-naphthylamide
    • Jadot M., Colmant C., Wattiaux-de C.S., Wattiaux R. Intralysosomal hydrolysis of glycyl-l-phenylalanine 2-naphthylamide. Biochem. J. 1984, 219:965-970.
    • (1984) Biochem. J. , vol.219 , pp. 965-970
    • Jadot, M.1    Colmant, C.2    Wattiaux-de, C.S.3    Wattiaux, R.4
  • 31
    • 0036472494 scopus 로고    scopus 로고
    • PH-dependent regulation of lysosomal calcium in macrophages
    • Christensen K.A., Myers J.T., Swanson J.A. pH-dependent regulation of lysosomal calcium in macrophages. J. Cell Sci. 2002, 115:599-607.
    • (2002) J. Cell Sci. , vol.115 , pp. 599-607
    • Christensen, K.A.1    Myers, J.T.2    Swanson, J.A.3
  • 33
    • 55549134611 scopus 로고    scopus 로고
    • Niemann-Pick disease type C1 is a sphingosine storage disease that causes deregulation of lysosomal calcium
    • Lloyd-Evans E., Morgan A.J., He X., et al. Niemann-Pick disease type C1 is a sphingosine storage disease that causes deregulation of lysosomal calcium. Nat. Med. 2008, 14:1247-1255.
    • (2008) Nat. Med. , vol.14 , pp. 1247-1255
    • Lloyd-Evans, E.1    Morgan, A.J.2    He, X.3
  • 34
    • 0032481105 scopus 로고    scopus 로고
    • Calcium uptake via endocytosis with rapid release from acidifying endosomes
    • Gerasimenko J.V., Tepikin A.V., Petersen O.H., Gerasimenko O.V. Calcium uptake via endocytosis with rapid release from acidifying endosomes. Curr. Biol. 1998, 8:1335-1338.
    • (1998) Curr. Biol. , vol.8 , pp. 1335-1338
    • Gerasimenko, J.V.1    Tepikin, A.V.2    Petersen, O.H.3    Gerasimenko, O.V.4
  • 35
    • 34248363193 scopus 로고    scopus 로고
    • Activation of trypsinogen in large endocytic vacuoles of pancreatic acinar cells
    • Sherwood M.W., Prior I.A., Voronina S.G., et al. Activation of trypsinogen in large endocytic vacuoles of pancreatic acinar cells. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:5674-5679.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 5674-5679
    • Sherwood, M.W.1    Prior, I.A.2    Voronina, S.G.3
  • 37
    • 59149095897 scopus 로고    scopus 로고
    • Inhibitors of V-ATPases: old and new players
    • Huss M., Wieczorek H. Inhibitors of V-ATPases: old and new players. J Exp Biol 2009, 212:341-346.
    • (2009) J Exp Biol , vol.212 , pp. 341-346
    • Huss, M.1    Wieczorek, H.2
  • 38
    • 0034643304 scopus 로고    scopus 로고
    • Molecular cloning of a novel form (two-repeat) protein related to voltage-gated sodium and calcium channels
    • Ishibashi K., Suzuki M., Imai M. Molecular cloning of a novel form (two-repeat) protein related to voltage-gated sodium and calcium channels. Biochem. Biophys. Res. Commun. 2000, 270:370-376.
    • (2000) Biochem. Biophys. Res. Commun. , vol.270 , pp. 370-376
    • Ishibashi, K.1    Suzuki, M.2    Imai, M.3
  • 40
    • 15244350821 scopus 로고    scopus 로고
    • 2+-activated channel TPC1 regulates germination and stomatal movement
    • 2+-activated channel TPC1 regulates germination and stomatal movement. Nature 2005, 434:404-408.
    • (2005) Nature , vol.434 , pp. 404-408
    • Peiter, E.1    Maathuis, F.J.2    Mills, L.N.3
  • 41
    • 67749143745 scopus 로고    scopus 로고
    • Essential requirement for two-pore channel 1 in NAADP-mediated calcium signaling
    • Brailoiu E., Churamani D., Cai X., et al. Essential requirement for two-pore channel 1 in NAADP-mediated calcium signaling. J. Cell Biol. 2009, 186:201-209.
    • (2009) J. Cell Biol. , vol.186 , pp. 201-209
    • Brailoiu, E.1    Churamani, D.2    Cai, X.3
  • 42
    • 77449093874 scopus 로고    scopus 로고
    • An ancestral deuterostome family of two-pore channels mediate nicotinic acid adenine dinucleotide phosphate-dependent calcium release from acidic organelles
    • Brailoiu E., Hooper R., Cai X., et al. An ancestral deuterostome family of two-pore channels mediate nicotinic acid adenine dinucleotide phosphate-dependent calcium release from acidic organelles. J .Biol. Chem. 2010, 285:2897-2901.
    • (2010) J .Biol. Chem. , vol.285 , pp. 2897-2901
    • Brailoiu, E.1    Hooper, R.2    Cai, X.3
  • 44
    • 47249113820 scopus 로고    scopus 로고
    • Carbon nanopipettes characterize calcium release pathways in breast cancer cells
    • Schrlau M.G., Brailoiu E., Patel S., Gogotsi Y., Dun N.J., Bau H.M. Carbon nanopipettes characterize calcium release pathways in breast cancer cells. Nanotechnology 2008, 19:325102.
    • (2008) Nanotechnology , vol.19 , pp. 325102
    • Schrlau, M.G.1    Brailoiu, E.2    Patel, S.3    Gogotsi, Y.4    Dun, N.J.5    Bau, H.M.6
  • 45
    • 77953916412 scopus 로고    scopus 로고
    • Two-pore channels: regulation by NAADP and customized roles in triggering calcium signals
    • Patel S., Marchant J.S., Brailoiu E. Two-pore channels: regulation by NAADP and customized roles in triggering calcium signals. Cell Calcium 2010, 47:480-490.
    • (2010) Cell Calcium , vol.47 , pp. 480-490
    • Patel, S.1    Marchant, J.S.2    Brailoiu, E.3
  • 46
    • 67349287016 scopus 로고    scopus 로고
    • NAADP mobilizes calcium from acidic organelles through two-pore channels
    • Calcraft P.J., Ruas M., Pan Z., et al. NAADP mobilizes calcium from acidic organelles through two-pore channels. Nature 2009, 459:596-600.
    • (2009) Nature , vol.459 , pp. 596-600
    • Calcraft, P.J.1    Ruas, M.2    Pan, Z.3
  • 49
    • 79953173921 scopus 로고    scopus 로고
    • Cyclic adenosine diphosphate ribose activates ryanodine receptors, whereas NAADP activates two-pore domain channels
    • Ogunbayo O.A., Zhu Y., Rossi D., Sorrentino V., Ma J., Zhu M.X., Evans A.M. Cyclic adenosine diphosphate ribose activates ryanodine receptors, whereas NAADP activates two-pore domain channels. J. Biol. Chem. 2011, 286:9136-9140.
    • (2011) J. Biol. Chem. , vol.286 , pp. 9136-9140
    • Ogunbayo, O.A.1    Zhu, Y.2    Rossi, D.3    Sorrentino, V.4    Ma, J.5    Zhu, M.X.6    Evans, A.M.7
  • 50
    • 0242552230 scopus 로고    scopus 로고
    • + ions: evidence for multiple NAADP receptor conformations
    • + ions: evidence for multiple NAADP receptor conformations. Biochem. J. 2003, 375:805-812.
    • (2003) Biochem. J. , vol.375 , pp. 805-812
    • Dickinson, G.D.1    Patel, S.2
  • 52
    • 62749114761 scopus 로고    scopus 로고
    • NAADP-mediated channel "chatter" in neurons of the rat medulla oblongata
    • Brailoiu G.C., Brailoiu E., Parkesh R., et al. NAADP-mediated channel "chatter" in neurons of the rat medulla oblongata. Biochem. J. 2009, 419:91-97.
    • (2009) Biochem. J. , vol.419 , pp. 91-97
    • Brailoiu, G.C.1    Brailoiu, E.2    Parkesh, R.3
  • 53
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino J.S., Traub L.M. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 2003, 72:395-447.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 55
    • 0034623716 scopus 로고    scopus 로고
    • 2+ signalling by nicotinic acid adenine dinucleotide phosphate diffusion and gradients
    • 2+ signalling by nicotinic acid adenine dinucleotide phosphate diffusion and gradients. J. Biol. Chem. 2000, 275:38687-38692.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38687-38692
    • Churchill, G.C.1    Galione, A.2
  • 58
    • 79953207656 scopus 로고    scopus 로고
    • Membrane topology of NAADP-sensitive two-pore channels and their regulation by N-linked glycosylation
    • Hooper R., Churamani D., Brailoiu E., Taylor C.W., Patel S. Membrane topology of NAADP-sensitive two-pore channels and their regulation by N-linked glycosylation. J. Biol. Chem. 2011, 286:9141-9149.
    • (2011) J. Biol. Chem. , vol.286 , pp. 9141-9149
    • Hooper, R.1    Churamani, D.2    Brailoiu, E.3    Taylor, C.W.4    Patel, S.5
  • 59
    • 0036487068 scopus 로고    scopus 로고
    • + channel gating: functional sialic acids are localized to the S5-S6 loop of domain I
    • + channel gating: functional sialic acids are localized to the S5-S6 loop of domain I. J. Physiol. 2002, 538:675-690.
    • (2002) J. Physiol. , vol.538 , pp. 675-690
    • Bennett, E.S.1
  • 60
    • 70450250052 scopus 로고    scopus 로고
    • Triple N-glycosylation in the long S5-P loop regulates the activation and trafficking of the Kv12.2 potassium channel
    • Noma K., Kimura K., Minatohara K., et al. Triple N-glycosylation in the long S5-P loop regulates the activation and trafficking of the Kv12.2 potassium channel. J. Biol. Chem. 2009, 284:33139-33150.
    • (2009) J. Biol. Chem. , vol.284 , pp. 33139-33150
    • Noma, K.1    Kimura, K.2    Minatohara, K.3
  • 61
    • 21344439776 scopus 로고    scopus 로고
    • Characterization of rat transient receptor potential vanilloid 1 receptors lacking the N-glycosylation site N604
    • Wirkner K., Hognestad H., Jahnel R., Hucho F., Illes P. Characterization of rat transient receptor potential vanilloid 1 receptors lacking the N-glycosylation site N604. Neuroreport 2005, 16:997-1001.
    • (2005) Neuroreport , vol.16 , pp. 997-1001
    • Wirkner, K.1    Hognestad, H.2    Jahnel, R.3    Hucho, F.4    Illes, P.5
  • 62
    • 0027977519 scopus 로고
    • + channels and calcium-induced calcium release by slow vacuolar ion channels in guard cell vacuoles implicated in the control of stomatal closure
    • + channels and calcium-induced calcium release by slow vacuolar ion channels in guard cell vacuoles implicated in the control of stomatal closure. Plant Cell 1994, 6:669-683.
    • (1994) Plant Cell , vol.6 , pp. 669-683
    • Ward, J.M.1    Schroeder, J.I.2
  • 63
    • 28944452146 scopus 로고    scopus 로고
    • A perspective on the slow vacuolar channel in vacuoles from higher plant cells
    • Scholz-Starke J., Naso A., Carpaneto A. A perspective on the slow vacuolar channel in vacuoles from higher plant cells. J. Chem. Inf. Model 2005, 45:1502-1506.
    • (2005) J. Chem. Inf. Model , vol.45 , pp. 1502-1506
    • Scholz-Starke, J.1    Naso, A.2    Carpaneto, A.3
  • 65
    • 0029199613 scopus 로고
    • Protons and calcium modulate SV-type channels in the vacuolar-lysosomal compartment-channel interaction with calmodulin inhibitors
    • Schulz-Lessdorf B., Hedrich R. Protons and calcium modulate SV-type channels in the vacuolar-lysosomal compartment-channel interaction with calmodulin inhibitors. Planta 1995, 197:655-671.
    • (1995) Planta , vol.197 , pp. 655-671
    • Schulz-Lessdorf, B.1    Hedrich, R.2
  • 66
    • 0034682499 scopus 로고    scopus 로고
    • Calcium release from the endoplasmic reticulum of higher plants elicited by the NADP metabolite nicotinic acid adenine dinucleotide phosphate
    • Navazio L., Bewell M.A., Siddiqua A., Dickinson G.D., Galione A., Sanders D. Calcium release from the endoplasmic reticulum of higher plants elicited by the NADP metabolite nicotinic acid adenine dinucleotide phosphate. Proc. Natl. Acad. Sci. 2000, 97:8693-8698.
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 8693-8698
    • Navazio, L.1    Bewell, M.A.2    Siddiqua, A.3    Dickinson, G.D.4    Galione, A.5    Sanders, D.6
  • 68
    • 34548479246 scopus 로고    scopus 로고
    • 2+ release channel from liver lysosomes of rats
    • 2+ release channel from liver lysosomes of rats. J. Biol. Chem. 2007, 282:25259-25269.
    • (2007) J. Biol. Chem. , vol.282 , pp. 25259-25269
    • Zhang, F.1    Li, P.L.2
  • 70
    • 54049156405 scopus 로고    scopus 로고
    • The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel
    • Dong X.P., Cheng X., Mills E., et al. The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel. Nature 2008, 455:992-996.
    • (2008) Nature , vol.455 , pp. 992-996
    • Dong, X.P.1    Cheng, X.2    Mills, E.3
  • 71
    • 77955291039 scopus 로고    scopus 로고
    • TPC2 proteins mediate nicotinic acid adenine dinucleotide phosphate (NAADP)- and agonist-evoked contractions of smooth muscle
    • Tugba Durlu-Kandilci N., Ruas M., Chuang K.T., Brading A., Parrington J., Galione A. TPC2 proteins mediate nicotinic acid adenine dinucleotide phosphate (NAADP)- and agonist-evoked contractions of smooth muscle. J. Biol. Chem. 2010, 285:24925-24932.
    • (2010) J. Biol. Chem. , vol.285 , pp. 24925-24932
    • Tugba Durlu-Kandilci, N.1    Ruas, M.2    Chuang, K.T.3    Brading, A.4    Parrington, J.5    Galione, A.6
  • 73
    • 85013732713 scopus 로고    scopus 로고
    • Transcriptional mechanisms regulating Ca2+ homeostasis, Cell Calcium, in press.
    • M.F. Ritchie, Y. Zhou, J. Soboloff, Transcriptional mechanisms regulating Ca2+ homeostasis, Cell Calcium, in press.
    • Ritchie, M.F.1    Zhou, Y.2    Soboloff, V.3
  • 74
    • 33744912796 scopus 로고    scopus 로고
    • Messenger-specific role for NAADP in neuronal differentiation
    • Brailoiu E., Churamani D., Pandey V., et al. Messenger-specific role for NAADP in neuronal differentiation. J. Biol. Chem. 2006, 281:15923-15928.
    • (2006) J. Biol. Chem. , vol.281 , pp. 15923-15928
    • Brailoiu, E.1    Churamani, D.2    Pandey, V.3
  • 76
    • 78650525751 scopus 로고    scopus 로고
    • Nicotinic acid adenine dinucleotide phosphate regulates skeletal muscle differentiation via action at two-pore channels
    • Aley P.K., Mikolajczyk A.M., Munz B., Churchill G.C., Galione A., Berger F. Nicotinic acid adenine dinucleotide phosphate regulates skeletal muscle differentiation via action at two-pore channels. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:19927-19932.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 19927-19932
    • Aley, P.K.1    Mikolajczyk, A.M.2    Munz, B.3    Churchill, G.C.4    Galione, A.5    Berger, F.6
  • 77
    • 69249227502 scopus 로고    scopus 로고
    • Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function
    • Saftig P., Klumperman J. Lysosome biogenesis and lysosomal membrane proteins: trafficking meets function. Nat. Rev. Mol. Cell Biol. 2009, 10:623-635.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 623-635
    • Saftig, P.1    Klumperman, J.2
  • 78
    • 36749070036 scopus 로고    scopus 로고
    • The role of calcium and other ions in sorting and delivery in the late endocytic pathway
    • Luzio J.P., Bright N.A., Pryor P.R. The role of calcium and other ions in sorting and delivery in the late endocytic pathway. Biochem. Soc. Trans. 2007, 35:1088-1091.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1088-1091
    • Luzio, J.P.1    Bright, N.A.2    Pryor, P.R.3
  • 79
    • 0032824099 scopus 로고    scopus 로고
    • Fusion of endosomes involved in synaptic vesicle recycling
    • Holroyd C., Kistner U., Annaert W., Jahn R. Fusion of endosomes involved in synaptic vesicle recycling. Mol. Biol. Cell 1999, 10:3035-3044.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3035-3044
    • Holroyd, C.1    Kistner, U.2    Annaert, W.3    Jahn, R.4
  • 80
    • 0034729167 scopus 로고    scopus 로고
    • 2+ in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles
    • 2+ in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles. J. Cell Biol. 2000, 149:1053-1062.
    • (2000) J. Cell Biol. , vol.149 , pp. 1053-1062
    • Pryor, P.R.1    Mullock, B.M.2    Bright, N.A.3    Gray, S.R.4    Luzio, J.P.5
  • 81
    • 0033822172 scopus 로고    scopus 로고
    • Identification of the gene causing mucolipidosis type IV
    • Bargal R., Avidan N., Ben-Asher E., et al. Identification of the gene causing mucolipidosis type IV. Nat. Genet. 2000, 26:118-123.
    • (2000) Nat. Genet. , vol.26 , pp. 118-123
    • Bargal, R.1    Avidan, N.2    Ben-Asher, E.3
  • 85
    • 45549095745 scopus 로고    scopus 로고
    • Two newly identified genetic determinants of pigmentation in Europeans
    • Sulem P., Gudbjartsson D.F., Stacey S.N., et al. Two newly identified genetic determinants of pigmentation in Europeans. Nat. Genet. 2008, 40:835-837.
    • (2008) Nat. Genet. , vol.40 , pp. 835-837
    • Sulem, P.1    Gudbjartsson, D.F.2    Stacey, S.N.3
  • 86
    • 80051470335 scopus 로고    scopus 로고
    • The cell biology of human hair follicle pigmentation
    • Tobin D.J. The cell biology of human hair follicle pigmentation. Pigment Cell Melanoma Res. 2010.
    • (2010) Pigment Cell Melanoma Res.
    • Tobin, D.J.1
  • 87
    • 0343674513 scopus 로고    scopus 로고
    • Calcium uptake, release and ryanodine binding in melanosomes from retinal pigment epithelium
    • Salceda R., Sanchez-Chavez G. Calcium uptake, release and ryanodine binding in melanosomes from retinal pigment epithelium. Cell Calcium 2000, 27:223-229.
    • (2000) Cell Calcium , vol.27 , pp. 223-229
    • Salceda, R.1    Sanchez-Chavez, G.2
  • 89
    • 78651449422 scopus 로고    scopus 로고
    • Human hair melanins: what we have learned and have not learned from mouse coat color pigmentation
    • Ito S., Wakamatsu K. Human hair melanins: what we have learned and have not learned from mouse coat color pigmentation. Pigment Cell Melanoma Res. 2010.
    • (2010) Pigment Cell Melanoma Res.
    • Ito, S.1    Wakamatsu, K.2
  • 91
    • 73949092362 scopus 로고    scopus 로고
    • In with the TRP channels: intracellular functions for TRPM1 and TRPM2
    • Patel S., Docampo R. In with the TRP channels: intracellular functions for TRPM1 and TRPM2. Sci. Signal. 2009, 2:e69.
    • (2009) Sci. Signal. , vol.2
    • Patel, S.1    Docampo, R.2
  • 92
    • 0027497515 scopus 로고
    • Molecular evolution of voltage-sensitive ion channel genes: on the origins of electrical excitability
    • Strong M., Chandy K.G., Gutman G.A. Molecular evolution of voltage-sensitive ion channel genes: on the origins of electrical excitability. Mol. Biol. Evol. 1993, 10:221-242.
    • (1993) Mol. Biol. Evol. , vol.10 , pp. 221-242
    • Strong, M.1    Chandy, K.G.2    Gutman, G.A.3
  • 97
    • 0033832141 scopus 로고    scopus 로고
    • NAADP-induced calcium release in sea urchin eggs
    • Galione A., Patel S., Churchill G.C. NAADP-induced calcium release in sea urchin eggs. Biol. Cell. 2000, 92:197-204.
    • (2000) Biol. Cell. , vol.92 , pp. 197-204
    • Galione, A.1    Patel, S.2    Churchill, G.C.3
  • 98
    • 77957228498 scopus 로고    scopus 로고
    • Degeneration of an intracellular ion channel in the primate lineage by relaxation of selective constraints
    • Cai X., Patel S. Degeneration of an intracellular ion channel in the primate lineage by relaxation of selective constraints. Mol. Biol. Evol. 2010, 27:2352-2359.
    • (2010) Mol. Biol. Evol. , vol.27 , pp. 2352-2359
    • Cai, X.1    Patel, S.2
  • 99
    • 17844368321 scopus 로고    scopus 로고
    • The NAADP receptor: new receptors or new regulation?
    • Galione A., Petersen O.H. The NAADP receptor: new receptors or new regulation?. Mol. Interv. 2005, 5:73-79.
    • (2005) Mol. Interv. , vol.5 , pp. 73-79
    • Galione, A.1    Petersen, O.H.2
  • 100
    • 67649856596 scopus 로고    scopus 로고
    • Second messenger signaling: multiple receptors for NAADP
    • Guse A.H. Second messenger signaling: multiple receptors for NAADP. Curr. Biol. 2009, 19:R521-R523.
    • (2009) Curr. Biol. , vol.19
    • Guse, A.H.1
  • 102
    • 62649161780 scopus 로고    scopus 로고
    • Identification of a chemical probe for NAADP by virtual screening
    • Naylor E., Arredouani A., Vasudevan S.R., et al. Identification of a chemical probe for NAADP by virtual screening. Nat. Chem. Biol. 2009, 5:220-226.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 220-226
    • Naylor, E.1    Arredouani, A.2    Vasudevan, S.R.3
  • 103
    • 67649743775 scopus 로고    scopus 로고
    • 2+ signaling via type 1 ryanodine receptor in T cells revealed by a synthetic NAADP antagonist
    • 2+ signaling via type 1 ryanodine receptor in T cells revealed by a synthetic NAADP antagonist. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:10678-10683.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 10678-10683
    • Dammermann, W.1    Zhang, B.2    Nebel, M.3


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