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Volumn 39, Issue 1, 2009, Pages 91-102

Homer and the ryanodine receptor

Author keywords

Homer; Protein targeting; Protein protein interactions; Ryanodine receptors

Indexed keywords

CALCIUM ION; ION CHANNEL; PROTEIN HOMER; RYANODINE RECEPTOR; RYANODINE RECEPTOR 1; RYANODINE RECEPTOR 2; RYANODINE RECEPTOR 3;

EID: 70450248659     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-009-0494-1     Document Type: Review
Times cited : (31)

References (105)
  • 2
    • 34547845237 scopus 로고    scopus 로고
    • Multiple activation mechanisms of store-operated TRPC channels in smooth muscle cells
    • DOI 10.1113/jphysiol.2007.137802
    • AP Albert SN Saleh CM Peppiatt-Wildman, et al. 2007 Multiple activation mechanisms of store-operated TRPC channels in smooth muscle cells J Physiol 583 25 36 10.1113/jphysiol.2007.137802 17615095 (Pubitemid 47244242)
    • (2007) Journal of Physiology , vol.583 , Issue.1 , pp. 25-36
    • Albert, A.P.1    Saleh, S.N.2    Peppiatt-Wildman, C.M.3    Large, W.A.4
  • 4
    • 34248597540 scopus 로고    scopus 로고
    • The mAKAP signalosome and cardiac myocyte hypertrophy
    • DOI 10.1080/15216540701358593, PII 778368024
    • AL Bauman JJ Michel E Henson, et al. 2007 The mAKAP signalosome and cardiac myocyte hypertrophy IUBMB Life 59 163 169 10.1080/15216540701358593 17487687 (Pubitemid 46752479)
    • (2007) IUBMB Life , vol.59 , Issue.3 , pp. 163-169
    • Bauman, A.L.1    Michel, J.J.C.2    Henson, E.3    Dodge-Kafka, K.L.4    Kapiloff, M.S.5
  • 5
    • 0033679292 scopus 로고    scopus 로고
    • Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition
    • 10.1016/S0896-6273(00)81145-9 10798399
    • J Beneken JC Tu B Xiao, et al. 2000 Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition Neuron 26 143 154 10.1016/S0896-6273(00)81145-9 10798399
    • (2000) Neuron , vol.26 , pp. 143-154
    • Beneken, J.1    Tu, J.C.2    Xiao, B.3
  • 6
    • 34248209169 scopus 로고    scopus 로고
    • DNA methylation regulates tissue-speci.c expression of Shank3
    • DOI 10.1111/j.1471-4159.2007.04539.x
    • S Beri N Tonna G Menozzi, et al. 2007 DNA methylation regulates tissue-specific expression of Shank3 J Neurochem 101 1380 1391 10.1111/j.1471-4159.2007.04539.x 17419801 (Pubitemid 46718829)
    • (2007) Journal of Neurochemistry , vol.101 , Issue.5 , pp. 1380-1391
    • Beri, S.1    Tonna, N.2    Menozzi, G.3    Bonaglia, M.C.4    Sala, C.5    Giorda, R.6
  • 7
    • 0035877582 scopus 로고    scopus 로고
    • Identification of a ryanodine receptor in rat heart mitochondria
    • 10.1074/jbc.M101486200 11297554
    • G Beutner VK Sharma DR Giovannucci, et al. 2001 Identification of a ryanodine receptor in rat heart mitochondria J Biol Chem 276 21482 21488 10.1074/jbc.M101486200 11297554
    • (2001) J Biol Chem , vol.276 , pp. 21482-21488
    • Beutner, G.1    Sharma, V.K.2    Giovannucci, D.R.3
  • 9
    • 0036316727 scopus 로고    scopus 로고
    • ProSAP/Shank proteins - A family of higher order organizing molecules of the postsynaptic density with an emerging role in human neurological disease
    • DOI 10.1046/j.1471-4159.2002.00931.x
    • TM Boeckers J Bockmann MR Kreutz, et al. 2002 ProSAP/Shank proteins-a family of higher order organizing molecules of the postsynaptic density with an emerging role in human neurological disease J Neurochem 81 903 910 10.1046/j.1471-4159.2002.00931.x 12065602 (Pubitemid 34809273)
    • (2002) Journal of Neurochemistry , vol.81 , Issue.5 , pp. 903-910
    • Boeckers, T.M.1    Bockmann, J.2    Kreutz, M.R.3    Gundelfinger, E.D.4
  • 10
    • 33645451579 scopus 로고    scopus 로고
    • Transition of Homer isoforms during skeletal muscle regeneration
    • 10.1152/ajpcell.00217.2005 16236824
    • E Bortoloso N Pilati A Megighian, et al. 2006 Transition of Homer isoforms during skeletal muscle regeneration Am J Physiol Cell Physiol 290 C711 C718 10.1152/ajpcell.00217.2005 16236824
    • (2006) Am J Physiol Cell Physiol , vol.290
    • Bortoloso, E.1    Pilati, N.2    Megighian, A.3
  • 13
    • 0029810979 scopus 로고    scopus 로고
    • Functional coupling between ryanodine receptors and L-type calcium channels in neurons
    • DOI 10.1038/382719a0
    • P Chavis L Fagni JB Lansman, et al. 1996 Functional coupling between ryanodine receptors and L-type calcium channels in neurons Nature 382 719 722 10.1038/382719a0 8751443 (Pubitemid 26282178)
    • (1996) Nature , vol.382 , Issue.6593 , pp. 719-722
    • Chavis, P.1    Fagni, L.2    Lansman, J.B.3    Bockaert, J.4
  • 16
    • 0942290432 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase IIδ associates with the ryanodine receptor complex and regulates channel function in rabbit heart
    • DOI 10.1042/BJ20031043
    • S Currie CM Loughrey MA Craig, et al. 2004 Calcium/calmodulin-dependent protein kinase IIdelta associates with the ryanodine receptor complex and regulates channel function in rabbit heart Biochem J 377 357 366 10.1042/BJ20031043 14556649 (Pubitemid 38142191)
    • (2004) Biochemical Journal , vol.377 , Issue.2 , pp. 357-366
    • Currie, S.1    Loughrey, C.M.2    Craig, M.-A.3    Smith, G.L.4
  • 17
    • 20444376155 scopus 로고    scopus 로고
    • 2+ signaling in T-lymphocytes
    • DOI 10.1074/jbc.M413085200
    • 2+ signaling in T-lymphocytes J Biol Chem 280 21394 21399 10.1074/jbc.M413085200 15774471 (Pubitemid 40805703)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.22 , pp. 21394-21399
    • Dammermann, W.1    Guse, A.H.2
  • 18
    • 34848927132 scopus 로고    scopus 로고
    • 2+ exchanger and ryanodine receptor during development
    • DOI 10.1529/biophysj.107.104943
    • 2+ exchanger and ryanodine receptor during development Biophys J 93 2504 2518 10.1529/biophysj.107.104943 17557789 (Pubitemid 47511150)
    • (2007) Biophysical Journal , vol.93 , Issue.7 , pp. 2504-2518
    • Dan, P.1    Lin, E.2    Huang, J.3    Biln, P.4    Tibbits, G.F.5
  • 20
    • 0037080171 scopus 로고    scopus 로고
    • Mutation of Drosophila homer disrupts control of locomotor activity and behavioral plasticity
    • 11784787
    • TT Diagana U Thomas SN Prokopenko, et al. 2002 Mutation of Drosophila homer disrupts control of locomotor activity and behavioral plasticity J Neurosci 22 428 436 11784787
    • (2002) J Neurosci , vol.22 , pp. 428-436
    • Diagana, T.T.1    Thomas, U.2    Prokopenko, S.N.3
  • 21
    • 0025193394 scopus 로고
    • 2+ release channel activity from sarcoplasmic reticulum by annexin VI (67-kDa calcimedin)
    • 2168425
    • 2+ release channel activity from sarcoplasmic reticulum by annexin VI (67-kDa calcimedin) J Biol Chem 265 15894 15899 2168425
    • (1990) J Biol Chem , vol.265 , pp. 15894-15899
    • Diaz-Munoz, M.1    Hamilton, S.L.2    Kaetzel, M.A.3
  • 23
    • 33645796192 scopus 로고    scopus 로고
    • Functional properties of ryanodine receptors carrying three amino acid substitutions identified in patients affected by multi-minicore disease and central core disease, expressed in immortalized lymphocytes
    • 10.1042/BJ20051282 16372898
    • S Ducreux F Zorzato A Ferreiro, et al. 2006 Functional properties of ryanodine receptors carrying three amino acid substitutions identified in patients affected by multi-minicore disease and central core disease, expressed in immortalized lymphocytes Biochem J 395 259 266 10.1042/BJ20051282 16372898
    • (2006) Biochem J , vol.395 , pp. 259-266
    • Ducreux, S.1    Zorzato, F.2    Ferreiro, A.3
  • 25
    • 24144454793 scopus 로고    scopus 로고
    • Effects of Vesl/Homer proteins on intracellular signaling
    • RS Duncan SY Hwang P Koulen 2005 Effects of Vesl/Homer proteins on intracellular signaling Exp Biol Med (Maywood) 230 527 535
    • (2005) Exp Biol Med (Maywood) , vol.230 , pp. 527-535
    • Duncan, R.S.1    Hwang, S.Y.2    Koulen, P.3
  • 26
    • 0038699101 scopus 로고    scopus 로고
    • Homer as both a scaffold and transduction molecule
    • doi:10.1126/stke.2002.137.re8
    • Fagni L, Worley PF, Ango F (2002) Homer as both a scaffold and transduction molecule. Sci STKE 137:RE8. doi: 10.1126/stke.2002.137.re8
    • (2002) Sci STKE 137:RE8
    • Fagni, L.1    Worley, P.F.2    Ango, F.3
  • 30
    • 0036788917 scopus 로고    scopus 로고
    • Ryanodine receptor calcium release channels
    • 12270947
    • M Fill JA Copello 2002 Ryanodine receptor calcium release channels Physiol Rev 82 893 922 12270947
    • (2002) Physiol Rev , vol.82 , pp. 893-922
    • Fill, M.1    Copello, J.A.2
  • 31
    • 0033166454 scopus 로고    scopus 로고
    • Modulation of ion channels: A 'current' view of AKAPs
    • DOI 10.1016/S0896-6273(00)80795-3
    • ID Fraser JD Scott 1999 Modulation of ion channels: a "current" view of AKAPs Neuron 23 423 426 10.1016/S0896-6273(00)80795-3 10433254 (Pubitemid 29359913)
    • (1999) Neuron , vol.23 , Issue.3 , pp. 423-426
    • Fraser, I.D.C.1    Scott, J.D.2
  • 32
    • 0030818896 scopus 로고    scopus 로고
    • 2+ release channel (ryanodine receptor) function
    • DOI 10.1016/S0014-5793(97)00781-3, PII S0014579397007813
    • 2+ release channel (ryanodine receptor) function FEBS Lett 412 223 226 10.1016/S0014-5793(97)00781- 3 9257724 (Pubitemid 27310034)
    • (1997) FEBS Letters , vol.412 , Issue.1 , pp. 223-226
    • Gao, L.1    Tripathy, A.2    Lu, X.3    Meissner, G.4
  • 35
    • 0028925223 scopus 로고
    • The ryanodine receptor/calcium channel genes are widely and differentially expressed in murine brain and peripheral tissues
    • 10.1083/jcb.128.5.893 7876312
    • G Giannini A Conti S Mammarella, et al. 1995 The ryanodine receptor/calcium channel genes are widely and differentially expressed in murine brain and peripheral tissues J Cell Biol 128 893 904 10.1083/jcb.128.5.893 7876312
    • (1995) J Cell Biol , vol.128 , pp. 893-904
    • Giannini, G.1    Conti, A.2    Mammarella, S.3
  • 36
    • 45449105994 scopus 로고    scopus 로고
    • 2+ regulates cardiomyocyte function
    • 10.1016/j.ceca.2007.11.016 18201761
    • 2+ regulates cardiomyocyte function Cell Calcium 44 230 242 10.1016/j.ceca.2007.11. 016 18201761
    • (2008) Cell Calcium , vol.44 , pp. 230-242
    • Guatimosim, S.1    Amaya, M.J.2    Guerra, M.T.3
  • 37
    • 0035500806 scopus 로고    scopus 로고
    • Expression of the ryanodine receptor isoforms in immune cells
    • 11673493
    • E Hosoi C Nishizaki KL Gallagher, et al. 2001 Expression of the ryanodine receptor isoforms in immune cells J Immunol 167 4887 4894 11673493
    • (2001) J Immunol , vol.167 , pp. 4887-4894
    • Hosoi, E.1    Nishizaki, C.2    Gallagher, K.L.3
  • 40
    • 0038420722 scopus 로고    scopus 로고
    • Differential functional interaction of two Vesl/Homer protein isoforms with ryanodine receptor type 1: A novel mechanism for control of intracellular calcium signaling
    • DOI 10.1016/S0143-4160(03)00082-4
    • SY Hwang J Wei JH Westhoff, et al. 2003 Differential functional interaction of two Vesl/Homer protein isoforms with ryanodine receptor type 1: a novel mechanism for control of intracellular calcium signaling Cell Calcium 34 177 184 10.1016/S0143-4160(03)00082-4 12810060 (Pubitemid 36798401)
    • (2003) Cell Calcium , vol.34 , Issue.2 , pp. 177-184
    • Hwang, S.-Y.1    Wei, J.2    Westhoff, J.H.3    Duncan, R.S.4    Ozawa, F.5    Volpe, P.6    Inokuchi, K.7    Koulen, P.8
  • 41
    • 0348048791 scopus 로고    scopus 로고
    • Activity-inducible protein Homer1a/Vesl-1S promotes redistribution of postsynaptic protein Homer1c/Vesl-1L in cultured rat hippocampal neurons
    • DOI 10.1016/j.neulet.2003.09.082
    • Y Inoue N Honkura A Kato, et al. 2004 Activity-inducible protein Homer1a/Vesl-1S promotes redistribution of postsynaptic protein Homer1c/Vesl-1L in cultured rat hippocampal neurons Neurosci Lett 354 143 147 10.1016/j.neulet.2003.09.082 14698459 (Pubitemid 38032854)
    • (2004) Neuroscience Letters , vol.354 , Issue.2 , pp. 143-147
    • Inoue, Y.1    Honkura, N.2    Kato, A.3    Ogawa, S.4    Udo, H.5    Inokuchi, K.6    Sugiyama, H.7
  • 42
    • 0036073345 scopus 로고    scopus 로고
    • Contributions of protein kinase A anchoring proteins to compartmentation of cAMP signaling in the heart
    • DOI 10.1124/mol.62.2.193
    • MS Kapiloff 2002 Contributions of protein kinase A anchoring proteins to compartmentation of cAMP signaling in the heart Mol Pharmacol 62 193 199 10.1124/mol.62.2.193 12130668 (Pubitemid 34804096)
    • (2002) Molecular Pharmacology , vol.62 , Issue.2 , pp. 193-199
    • Kapiloff, M.S.1
  • 43
    • 0030755738 scopus 로고    scopus 로고
    • Vesl, a gene encoding VASP/Ena family related protein, is upregulated during seizure, long-term potentiation and synaptogenesis
    • DOI 10.1016/S0014-5793(97)00775-8, PII S0014579397007758
    • A Kato F Ozawa Y Saitoh, et al. 1997 vesl, a gene encoding VASP/Ena family related protein, is upregulated during seizure, long-term potentiation and synaptogenesis FEBS Lett 412 183 189 10.1016/S0014-5793(97)00775-8 9257717 (Pubitemid 27310027)
    • (1997) FEBS Letters , vol.412 , Issue.1 , pp. 183-189
    • Kato, A.1    Ozawa, F.2    Saitoh, Y.3    Hirai, K.4    Inokuchi, K.5
  • 44
    • 33748174699 scopus 로고    scopus 로고
    • Endothelin-1 activates Homer 1alpha expression via mitogen-activated protein kinase in cardiac myocytes
    • 16786172
    • T Kawamoto K Togi R Yamauchi, et al. 2006 Endothelin-1 activates Homer 1alpha expression via mitogen-activated protein kinase in cardiac myocytes Int J Mol Med 18 193 196 16786172
    • (2006) Int J Mol Med , vol.18 , pp. 193-196
    • Kawamoto, T.1    Togi, K.2    Yamauchi, R.3
  • 45
    • 36349037017 scopus 로고    scopus 로고
    • v1.3 L-type calcium channel with ryanodine receptor type 2 in the rat hippocampus
    • DOI 10.1074/jbc.M701418200
    • S Kim HM Yun JH Baik, et al. 2007 Functional interaction of neuronal Cav1.3 L-type calcium channel with ryanodine receptor type 2 in the rat hippocampus J Biol Chem 282 32877 32889 10.1074/jbc.M701418200 17823125 (Pubitemid 350159320)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.45 , pp. 32877-32889
    • Kim, S.1    Yun, H.-M.2    Baik, J.-H.3    Kwang, C.C.4    Nah, S.-Y.5    Rhim, H.6
  • 46
    • 0033635186 scopus 로고    scopus 로고
    • Gating of store-operated channels by conformational coupling to ryanodine receptors
    • 10.1016/S1097-2765(00)00041-1 10983988
    • KI Kiselyov DM Shin Y Wang, et al. 2000 Gating of store-operated channels by conformational coupling to ryanodine receptors Mol Cell 6 421 431 10.1016/S1097-2765(00)00041-1 10983988
    • (2000) Mol Cell , vol.6 , pp. 421-431
    • Kiselyov, K.I.1    Shin, D.M.2    Wang, Y.3
  • 47
    • 54449100812 scopus 로고    scopus 로고
    • Novel role of calpain-3 in the triad-associated protein complex regulating calcium release in skeletal muscle
    • 10.1093/hmg/ddn223 18676612
    • I Kramerova E Kudryashova B Wu, et al. 2008 Novel role of calpain-3 in the triad-associated protein complex regulating calcium release in skeletal muscle Hum Mol Genet 17 3271 3280 10.1093/hmg/ddn223 18676612
    • (2008) Hum Mol Genet , vol.17 , pp. 3271-3280
    • Kramerova, I.1    Kudryashova, E.2    Wu, B.3
  • 49
    • 33748297537 scopus 로고    scopus 로고
    • Regulation of NFAT activation: A potential therapeutic target for immunosuppression
    • 10.1016/j.molcel.2006.03.017 16951543
    • M Lee J Park 2006 Regulation of NFAT activation: a potential therapeutic target for immunosuppression Mol Cells 22 1 7 10.1016/j.molcel.2006.03.017 16951543
    • (2006) Mol Cells , vol.22 , pp. 1-7
    • Lee, M.1    Park, J.2
  • 50
    • 33744524661 scopus 로고    scopus 로고
    • Functional coupling between TRPC3 and RyR1 regulates the expressions of key triadic proteins
    • DOI 10.1074/jbc.M600981200
    • EH Lee G Cherednichenko IN Pessah, et al. 2006 Functional coupling between TRPC3 and RyR1 regulates the expressions of key triadic proteins J Biol Chem 281 10042 10048 10.1074/jbc.M600981200 16484216 (Pubitemid 43864538)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.15 , pp. 10042-10048
    • Eun, H.L.1    Cherednichenko, G.2    Pessah, I.N.3    Allen, P.D.4
  • 51
    • 33745839333 scopus 로고    scopus 로고
    • Interplay between intra- and extracellular calcium ions
    • 16819293
    • EH Lee H do Kim PD Allen 2006 Interplay between intra- and extracellular calcium ions Mol Cells 21 315 329 16819293
    • (2006) Mol Cells , vol.21 , pp. 315-329
    • Lee, E.H.1    Do Kim, H.2    Allen, P.D.3
  • 52
    • 50349096542 scopus 로고    scopus 로고
    • Signaling for vesicle mobilization and synaptic plasticity
    • 10.1007/s12035-008-8014-3 18446451
    • ES Levitan 2008 Signaling for vesicle mobilization and synaptic plasticity Mol Neurobiol 37 39 43 10.1007/s12035-008-8014-3 18446451
    • (2008) Mol Neurobiol , vol.37 , pp. 39-43
    • Levitan, E.S.1
  • 53
    • 0033083405 scopus 로고    scopus 로고
    • 2+-release channel function
    • DOI 10.1042/0264-6021:3370345
    • 2+-release channel function Biochem J 337 Pt 3 345 361 10.1042/0264-6021:3370345 9895277 (Pubitemid 29082347)
    • (1999) Biochemical Journal , vol.337 , Issue.3 , pp. 345-361
    • Mackrill, J.J.1
  • 54
    • 0034640113 scopus 로고    scopus 로고
    • PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): Defective regulation in failing hearts
    • 10.1016/S0092-8674(00)80847-8 10830164
    • SO Marx S Reiken Y Hisamatsu, et al. 2000 PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts Cell 101 365 376 10.1016/S0092-8674(00)80847-8 10830164
    • (2000) Cell , vol.101 , pp. 365-376
    • Marx, S.O.1    Reiken, S.2    Hisamatsu, Y.3
  • 55
    • 34548188753 scopus 로고    scopus 로고
    • Targeting and retention of type 1 ryanodine receptors to the endoplasmic reticulum
    • DOI 10.1074/jbc.M702457200
    • G Meur AK Parker FV Gergely, et al. 2007 Targeting and retention of type 1 ryanodine receptors to the endoplasmic reticulum J Biol Chem 282 23096 23103 10.1074/jbc.M702457200 17526491 (Pubitemid 47311957)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.32 , pp. 23096-23103
    • Meur, G.1    Parker, A.K.T.2    Gergely, F.V.3    Taylor, C.W.4
  • 57
    • 45549109503 scopus 로고    scopus 로고
    • Phosphorylation of Homer3 by calcium/calmodulin-dependent kinase II regulates a coupling state of its target molecules in Purkinje cells
    • 10.1523/JNEUROSCI.4738-07.2008 18480293
    • A Mizutani Y Kuroda A Futatsugi, et al. 2008 Phosphorylation of Homer3 by calcium/calmodulin-dependent kinase II regulates a coupling state of its target molecules in Purkinje cells J Neurosci 28 5369 5382 10.1523/JNEUROSCI.4738-07. 2008 18480293
    • (2008) J Neurosci , vol.28 , pp. 5369-5382
    • Mizutani, A.1    Kuroda, Y.2    Futatsugi, A.3
  • 58
    • 0037155903 scopus 로고    scopus 로고
    • The ankyrin-B C-terminal domain determines activity of ankyrin-B/G chimeras in rescue of abnormal inositol 1,4,5-trisphosphate and ryanodine receptor distribution in ankyrin-B (-/-) neonatal cardiomyocytes
    • DOI 10.1074/jbc.M110958200
    • PJ Mohler AO Gramolini V Bennett 2002 The ankyrin-B C-terminal domain determines activity of ankyrin-B/G chimeras in rescue of abnormal inositol 1, 4, 5-trisphosphate and ryanodine receptor distribution in ankyrin-B (-/-) neonatal cardiomyocytes J Biol Chem 277 10599 10607 10.1074/jbc.M110958200 11781319 (Pubitemid 34968184)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.12 , pp. 10599-10607
    • Mohler, P.J.1    Gramolini, A.O.2    Bennett, V.3
  • 59
    • 0035868325 scopus 로고    scopus 로고
    • Molecular interaction of dihydropyridine receptors with type-1 ryanodine receptors in rat brain
    • DOI 10.1042/0264-6021:3540597
    • J Mouton I Marty M Villaz, et al. 2001 Molecular interaction of dihydropyridine receptors with type-1 ryanodine receptors in rat brain Biochem J 354 597 603 10.1042/0264-6021:3540597 11237864 (Pubitemid 32269723)
    • (2001) Biochemical Journal , vol.354 , Issue.3 , pp. 597-603
    • Mouton, J.1    Marty, I.2    Villaz, M.3    Feltz, A.4    Maulet, Y.5
  • 60
    • 44649183401 scopus 로고    scopus 로고
    • Auxiliary Ca(2+) channel subunits: Lessons learned from muscle
    • 10.1016/j.coph.2008.01.008 18329337
    • GJ Obermair P Tuluc BE Flucher 2008 Auxiliary Ca(2+) channel subunits: lessons learned from muscle Curr Opin Pharmacol 8 311 318 10.1016/j.coph.2008. 01.008 18329337
    • (2008) Curr Opin Pharmacol , vol.8 , pp. 311-318
    • Obermair, G.J.1    Tuluc, P.2    Flucher, B.E.3
  • 61
    • 0035894874 scopus 로고    scopus 로고
    • Rapid redistribution of the postsynaptic density protein PSD-Zip45 (Homer 1c) and its differential regulation by NMDA receptors and calcium channels
    • 11739567
    • S Okabe T Urushido D Konno, et al. 2001 Rapid redistribution of the postsynaptic density protein PSD-Zip45 (Homer 1c) and its differential regulation by NMDA receptors and calcium channels J Neurosci 21 9561 9571 11739567
    • (2001) J Neurosci , vol.21 , pp. 9561-9571
    • Okabe, S.1    Urushido, T.2    Konno, D.3
  • 62
    • 0032479445 scopus 로고    scopus 로고
    • Functional defects of a muscle-specific calpain, p94, caused by mutations associated with limb-girdle muscular dystrophy type 2A
    • DOI 10.1074/jbc.273.27.17073
    • Y Ono H Shimada H Sorimachi, et al. 1998 Functional defects of a muscle-specific calpain, p94, caused by mutations associated with limb-girdle muscular dystrophy type 2A J Biol Chem 273 17073 17078 10.1074/jbc.273.27.17073 9642272 (Pubitemid 28311741)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.27 , pp. 17073-17078
    • Ono, Y.1    Shimada, H.2    Sorimach, H.3    Richard, I.4    Saido, T.C.5    Beckmann, J.S.6    Ishiura, S.7    Suzuki, K.8
  • 65
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • DOI 10.1126/science.1083653
    • T Pawson P Nash 2003 Assembly of cell regulatory systems through protein interaction domains Science 300 445 452 10.1126/science.1083653 12702867 (Pubitemid 36444318)
    • (2003) Science , vol.300 , Issue.5618 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 67
    • 67649842123 scopus 로고    scopus 로고
    • In vitro modulation of the cardiac ryanodine receptor activity by Homer1
    • doi:10.1007/s00424-009-0664-0
    • Pouliquin P, Pace SM, Dulhunty AF (2009) In vitro modulation of the cardiac ryanodine receptor activity by Homer1. Pfluggers Arch (in press). doi: 10.1007/s00424-009-0664-0
    • (2009) Pfluggers Arch (In Press
    • Pouliquin, P.1    Pace, S.M.2    Dulhunty, A.F.3
  • 68
    • 0032559585 scopus 로고    scopus 로고
    • Role of ryanodine receptors in the assembly of calcium release units in skeletal muscle
    • DOI 10.1083/jcb.140.4.831
    • F Protasi C Franzini-Armstrong PD Allen 1998 Role of ryanodine receptors in the assembly of calcium release units in skeletal muscle J Cell Biol 140 831 842 10.1083/jcb.140.4.831 9472035 (Pubitemid 28141221)
    • (1998) Journal of Cell Biology , vol.140 , Issue.4 , pp. 831-842
    • Protasi, F.1    Franzini-Armstrong, C.2    Allen, P.D.3
  • 69
    • 0035369784 scopus 로고    scopus 로고
    • 2+ pools in neuronal signalling
    • DOI 10.1016/S0959-4388(00)00212-9
    • R Rizzuto 2001 Intracellular Ca(2+) pools in neuronal signalling Curr Opin Neurobiol 11 306 311 10.1016/S0959-4388(00)00212-9 11399428 (Pubitemid 32524095)
    • (2001) Current Opinion in Neurobiology , vol.11 , Issue.3 , pp. 306-311
    • Rizzuto, R.1
  • 70
    • 46349090290 scopus 로고    scopus 로고
    • The sarcoplasmic reticulum: An organized patchwork of specialized domains
    • DOI 10.1111/j.1600-0854.2008.00717.x
    • D Rossi V Barone E Giacomello, et al. 2008 The sarcoplasmic reticulum: an organized patchwork of specialized domains Traffic 9 1044 1049 10.1111/j.1600-0854.2008.00717.x 18266914 (Pubitemid 351916881)
    • (2008) Traffic , vol.9 , Issue.7 , pp. 1044-1049
    • Rossi, D.1    Barone, V.2    Giacomello, E.3    Cusimano, V.4    Sorrentino, V.5
  • 71
    • 0036382868 scopus 로고    scopus 로고
    • An N-terminal sequence specific for a novel Homer1 isoform controls trafficking of group i metabotropic glutamate receptor in mammalian cells
    • 10.1016/S0006-291X(02)00899-9 12176012
    • H Saito M Kimura A Inanobe, et al. 2002 An N-terminal sequence specific for a novel Homer1 isoform controls trafficking of group I metabotropic glutamate receptor in mammalian cells Biochem Biophys Res Commun 296 523 529 10.1016/S0006-291X(02)00899-9 12176012
    • (2002) Biochem Biophys Res Commun , vol.296 , pp. 523-529
    • Saito, H.1    Kimura, M.2    Inanobe, A.3
  • 73
    • 21644451189 scopus 로고    scopus 로고
    • The foot structure from the type 1 ryanodine receptor is required for functional coupling to store-operated channels
    • DOI 10.1074/jbc.M501487200
    • A Sampieri M Diaz-Munoz A Antaramian, et al. 2005 The foot structure from the type 1 ryanodine receptor is required for functional coupling to store-operated channels J Biol Chem 280 24804 24815 10.1074/jbc.M501487200 15878845 (Pubitemid 40934571)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 24804-24815
    • Sampieri, A.1    Diaz-Munoz, M.2    Antaramian, A.3    Vaca, L.4
  • 74
    • 0038128459 scopus 로고    scopus 로고
    • Subcellular distribution of Homer 1b/c in relation to endoplasmic reticulum and plasma membrane proteins in Purkinje neurons
    • DOI 10.1023/A:1024264025401
    • D Sandona A Scolari K Mikoshiba, et al. 2003 Subcellular distribution of Homer 1b/c in relation to endoplasmic reticulum and plasma membrane proteins in Purkinje neurons Neurochem Res 28 1151 1158 10.1023/A:1024264025401 12834253 (Pubitemid 36734545)
    • (2003) Neurochemical Research , vol.28 , Issue.8 , pp. 1151-1158
    • Sandona, D.1    Scolari, A.2    Mikoshiba, K.3    Volpe, P.4
  • 77
    • 0034044563 scopus 로고    scopus 로고
    • The Shank family of scaffold proteins
    • 10806096
    • M Sheng E Kim 2000 The Shank family of scaffold proteins J Cell Sci 113 Pt 11 1851 1856 10806096
    • (2000) J Cell Sci , vol.113 , Issue.PART 11 , pp. 1851-1856
    • Sheng, M.1    Kim, E.2
  • 78
    • 0036841856 scopus 로고    scopus 로고
    • Ca(2+)-dependent interaction between FKBP12 and calcineurin regulates activity of the Ca(2+) release channel in skeletal muscle
    • 10.1016/S0006-3495(02)75265-X 12414688
    • DW Shin Z Pan A Bandyopadhyay, et al. 2002 Ca(2+)-dependent interaction between FKBP12 and calcineurin regulates activity of the Ca(2+) release channel in skeletal muscle Biophys J 83 2539 2549 10.1016/S0006-3495(02)75265-X 12414688
    • (2002) Biophys J , vol.83 , pp. 2539-2549
    • Shin, D.W.1    Pan, Z.2    Bandyopadhyay, A.3
  • 80
    • 34447531009 scopus 로고    scopus 로고
    • The Homer family proteins
    • DOI 10.1186/gb-2007-8-2-206
    • Y Shiraishi-Yamaguchi T Furuichi 2007 The Homer family proteins Genome Biol 8 206 10.1186/gb-2007-8-2-206 17316461 (Pubitemid 351851022)
    • (2007) Genome Biology , vol.8 , Issue.2 , pp. 206
    • Shiraishi-Yamaguchi, Y.1    Furuichi, T.2
  • 81
    • 0033960760 scopus 로고    scopus 로고
    • Mouse brain and muscle tissues constitutively express high levels of homer proteins
    • DOI 10.1046/j.1432-1327.2000.01078.x
    • MM Soloviev F Ciruela WY Chan, et al. 2000 Mouse brain and muscle tissues constitutively express high levels of Homer proteins Eur J Biochem 267 634 639 10.1046/j.1432-1327.2000.01078.x 10651798 (Pubitemid 30082374)
    • (2000) European Journal of Biochemistry , vol.267 , Issue.3 , pp. 634-639
    • Soloviev, M.M.1    Ciruela, F.2    Chan, W.-Y.3    McIlhinney, R.A.J.4
  • 82
    • 0347986615 scopus 로고    scopus 로고
    • Oligomerization of the cardiac ryanodine receptor C-terminal tail
    • DOI 10.1042/BJ20030597
    • R Stewart S Zissimopoulos FA Lai 2003 Oligomerization of the cardiac ryanodine receptor C-terminal tail Biochem J 376 795 799 10.1042/BJ20030597 12959641 (Pubitemid 38058080)
    • (2003) Biochemical Journal , vol.376 , Issue.3 , pp. 795-799
    • Stewart, R.1    Zissimopoulos, S.2    Lai, F.A.3
  • 85
    • 0032561427 scopus 로고    scopus 로고
    • Isolation of PSD-Zip45, a novel Homer/vesl family protein containing leucine zipper motifs, from rat brain
    • DOI 10.1016/S0014-5793(98)01256-3, PII S0014579398012563
    • J Sun S Tadokoro T Imanaka, et al. 1998 Isolation of PSD-Zip45, a novel Homer/vesl family protein containing leucine zipper motifs, from rat brain FEBS Lett 437 304 308 10.1016/S0014-5793(98)01256-3 9824313 (Pubitemid 28511180)
    • (1998) FEBS Letters , vol.437 , Issue.3 , pp. 304-308
    • Sun, J.1    Tadokoro, S.2    Imanaka, T.3    D. Murakami, S.4    Nakamura, M.5    Kashiwada, K.6    Ko, J.7    Nishida, W.8    Sobue, K.9
  • 87
    • 0035891352 scopus 로고    scopus 로고
    • Sequential docking, molecular differentiation, and positioning of T-tubule/SR junctions in developing mouse skeletal muscle
    • DOI 10.1006/dbio.2001.0437
    • H Takekura BE Flucher C Franzini-Armstrong 2001 Sequential docking, molecular differentiation, and positioning of T-tubule/SR junctions in developing mouse skeletal muscle Dev Biol 239 204 214 10.1006/dbio.2001.0437 11784029 (Pubitemid 33108834)
    • (2001) Developmental Biology , vol.239 , Issue.2 , pp. 204-214
    • Takekura, H.1    Flucher, B.E.2    Franzini-Armstrong, C.3
  • 88
    • 0032192487 scopus 로고    scopus 로고
    • Homer binds a novel proline-rich motif and links group I metabotropic glutamate receptors with IP3 receptors
    • DOI 10.1016/S0896-6273(00)80589-9
    • JC Tu B Xiao JP Yuan, et al. 1998 Homer binds a novel proline-rich motif and links group 1 metabotropic glutamate receptors with IP3 receptors Neuron 21 717 726 10.1016/S0896-6273(00)80589-9 9808459 (Pubitemid 28498781)
    • (1998) Neuron , vol.21 , Issue.4 , pp. 717-726
    • Tu, J.C.1    Xiao, B.2    Yuan, J.P.3    Lanahan, A.A.4    Leoffert, K.5    Li, M.6    Linden, D.J.7    Worley, P.F.8
  • 89
    • 41549143871 scopus 로고    scopus 로고
    • NFAT activation by membrane potential follows a calcium pathway distinct from other activity-related transcription factors in skeletal muscle cells
    • 10.1152/ajpcell.00195.2007 18184878
    • JA Valdes E Gaggero J Hidalgo, et al. 2008 NFAT activation by membrane potential follows a calcium pathway distinct from other activity-related transcription factors in skeletal muscle cells Am J Physiol Cell Physiol 294 C715 C725 10.1152/ajpcell.00195.2007 18184878
    • (2008) Am J Physiol Cell Physiol , vol.294
    • Valdes, J.A.1    Gaggero, E.2    Hidalgo, J.3
  • 90
    • 0037119993 scopus 로고    scopus 로고
    • Involvement of TRPC in the abnormal calcium influx observed in dystrophic (mdx) mouse skeletal muscle fibers
    • DOI 10.1083/jcb.200203091
    • C Vandebrouck D Martin M Colson-Van Schoor, et al. 2002 Involvement of TRPC in the abnormal calcium influx observed in dystrophic (mdx) mouse skeletal muscle fibers J Cell Biol 158 1089 1096 10.1083/jcb.200203091 12235126 (Pubitemid 35052691)
    • (2002) Journal of Cell Biology , vol.158 , Issue.6 , pp. 1089-1096
    • Vandebrouck, C.1    Martin, D.2    Schoor, M.C.-V.3    Debaix, H.4    Gailly, P.5
  • 91
    • 34548632601 scopus 로고    scopus 로고
    • TRP channels
    • 10.1146/annurev.biochem.75.103004.142819 17579562
    • K Venkatachalam C Montell 2007 TRP channels Annu Rev Biochem 76 387 417 10.1146/annurev.biochem.75.103004.142819 17579562
    • (2007) Annu Rev Biochem , vol.76 , pp. 387-417
    • Venkatachalam, K.1    Montell, C.2
  • 92
    • 0036878801 scopus 로고    scopus 로고
    • The endoplasmic reticulum and neuronal calcium signalling
    • DOI 10.1016/S0143416002001896
    • A Verkhratsky 2002 The endoplasmic reticulum and neuronal calcium signalling Cell Calcium 32 393 404 10.1016/S0143416002001896 12543098 (Pubitemid 36175759)
    • (2002) Cell Calcium , vol.32 , Issue.5-6 , pp. 393-404
    • Verkhratsky, A.1
  • 93
    • 0036776098 scopus 로고    scopus 로고
    • Structural organization of the endoplasmic reticulum
    • DOI 10.1093/embo-reports/kvf202
    • GK Voeltz MM Rolls TA Rapoport 2002 Structural organization of the endoplasmic reticulum EMBO Rep 3 944 950 10.1093/embo-reports/kvf202 12370207 (Pubitemid 35256468)
    • (2002) EMBO Reports , vol.3 , Issue.10 , pp. 944-950
    • Voeltz, G.K.1    Rolls, M.M.2    Rapoport, T.A.3
  • 95
    • 33845687465 scopus 로고    scopus 로고
    • 2+ wave propagation in glial cells
    • DOI 10.1016/j.ceca.2006.06.006, PII S0143416006001242
    • 2+ wave propagation in glial cells Cell Calcium 41 155 167 10.1016/j.ceca.2006.06.006 16905188 (Pubitemid 44964458)
    • (2007) Cell Calcium , vol.41 , Issue.2 , pp. 155-167
    • Weerth, S.H.1    Holtzclaw, L.A.2    Russell, J.T.3
  • 97
    • 0041977044 scopus 로고    scopus 로고
    • Vesl/Homer proteins regulate ryanodine receptor type 2 function and intracellular calcium signaling
    • DOI 10.1016/S0143-4160(03)00112-X
    • JH Westhoff SY Hwang RS Duncan, et al. 2003 Vesl/Homer proteins regulate ryanodine receptor type 2 function and intracellular calcium signaling Cell Calcium 34 261 269 10.1016/S0143-4160(03)00112-X 12887973 (Pubitemid 37009934)
    • (2003) Cell Calcium , vol.34 , Issue.3 , pp. 261-269
    • Westhoff, J.H.1    Hwang, S.-Y.2    Duncan, R.S.3    Ozawa, F.4    Volpe, P.5    Inokuchi, K.6    Koulen, P.7
  • 98
    • 61549127939 scopus 로고    scopus 로고
    • Presynaptic ryanodine receptor-CamKII signaling is required for activity-dependent capture of transiting vesicles
    • 18592416
    • MY Wong D Shakiryanova ES Levitan 2009 Presynaptic ryanodine receptor-CamKII signaling is required for activity-dependent capture of transiting vesicles J Mol Neurosci 37 146 150 18592416
    • (2009) J Mol Neurosci , vol.37 , pp. 146-150
    • Wong, M.Y.1    Shakiryanova, D.2    Levitan, E.S.3
  • 99
    • 42449101304 scopus 로고    scopus 로고
    • TRPC3-interacting triadic proteins in skeletal muscle
    • DOI 10.1042/BJ20071504
    • JS Woo H Kim do PD Allen, et al. 2008 TRPC3-interacting triadic proteins in skeletal muscle Biochem J 411 399 405 10.1042/BJ20071504 18215135 (Pubitemid 351580192)
    • (2008) Biochemical Journal , vol.411 , Issue.2 , pp. 399-405
    • Woo, J.S.1    Kim, D.H.2    Allen, P.D.3    Lee, E.H.4
  • 101
    • 18544393408 scopus 로고    scopus 로고
    • Homer regulates the association of group 1 metabotropic glutamate receptors with multivalent complexes of Homer-related, synaptic proteins
    • DOI 10.1016/S0896-6273(00)80588-7
    • B Xiao JC Tu RS Petralia, et al. 1998 Homer regulates the association of group 1 metabotropic glutamate receptors with multivalent complexes of Homer-related, synaptic proteins Neuron 21 707 716 10.1016/S0896-6273(00)80588-7 9808458 (Pubitemid 28498780)
    • (1998) Neuron , vol.21 , Issue.4 , pp. 707-716
    • Xiao, B.1    Tu, J.C.2    Petralia, R.S.3    Yuan, J.P.4    Doan, A.5    Breder, C.D.6    Ruggiero, A.7    Lanahan, A.A.8    Wenthold, R.J.9    Worley, P.F.10
  • 102
    • 41149098918 scopus 로고    scopus 로고
    • Ryanodine receptor arrays: Not just a pretty pattern?
    • 10.1016/j.tcb.2008.02.003 18329877
    • CC Yin LG D'Cruz FA Lai 2008 Ryanodine receptor arrays: not just a pretty pattern? Trends Cell Biol 18 149 156 10.1016/j.tcb.2008.02.003 18329877
    • (2008) Trends Cell Biol , vol.18 , pp. 149-156
    • Yin, C.C.1    D'Cruz, L.G.2    Lai, F.A.3
  • 105
    • 34548644786 scopus 로고    scopus 로고
    • Modulation of the ryanodine receptor and intracellular calcium
    • 10.1146/annurev.biochem.76.053105.094237 17506640
    • R Zalk SE Lehnart AR Marks 2007 Modulation of the ryanodine receptor and intracellular calcium Annu Rev Biochem 76 367 385 10.1146/annurev.biochem.76. 053105.094237 17506640
    • (2007) Annu Rev Biochem , vol.76 , pp. 367-385
    • Zalk, R.1    Lehnart, S.E.2    Marks, A.R.3


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