메뉴 건너뛰기




Volumn 8, Issue 4, 1998, Pages 419-422

Specificity in signaling pathways: Assembly into multimolecular signaling complexes

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; PROTEIN KINASE C;

EID: 0031712741     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(98)80112-3     Document Type: Article
Times cited : (38)

References (39)
  • 1
    • 0031171361 scopus 로고    scopus 로고
    • PDZ domains: targeting signalling molecules to sub-membranous sites
    • CP Pointing C Phillips KE Davis DJ Blake PDZ domains: targeting signalling molecules to sub-membranous sites of special interest Bioessays 19 1997 469 479
    • (1997) Bioessays , vol.19 , pp. 469-479
    • Pointing, CP1    Phillips, C2    Davis, KE3    Blake, DJ4
  • 2
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • T Pawson JT Scott Signaling through scaffold, anchoring, and adaptor proteins of special interest Science 278 1997 2075 2080
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T1    Scott, JT2
  • 3
    • 0030475794 scopus 로고    scopus 로고
    • The transient receptor potential protein (Trp), a putative store-operated Ca2+ channel essential for phosphoinositide-mediated photoreception, forms a signaling complex with NorpA, InaC and InaD
    • A Huber P Sander A Gobert M Bahner R Hermann R Paulsen The transient receptor potential protein (Trp), a putative store-operated Ca2+ channel essential for phosphoinositide-mediated photoreception, forms a signaling complex with NorpA, InaC and InaD EMBO J 15 1996 7036 7045
    • (1996) EMBO J , vol.15 , pp. 7036-7045
    • Huber, A1    Sander, P2    Gobert, A3    Bahner, M4    Hermann, R5    Paulsen, R6
  • 4
    • 0029664550 scopus 로고    scopus 로고
    • Regulation of the TRP Ca2+ channel by INAD in Drosophila photoreceptors
    • BH Shieh MY Zhu Regulation of the TRP Ca2+ channel by INAD in Drosophila photoreceptors Neuron 16 1996 991 998
    • (1996) Neuron , vol.16 , pp. 991-998
    • Shieh, BH1    Zhu, MY2
  • 5
    • 0031037164 scopus 로고    scopus 로고
    • Requirement for the PDZ domain protein, INAD, for localization of the TRP store-operated channel to a signaling complex
    • J Chevesich AJ Kreuz C Montell Requirement for the PDZ domain protein, INAD, for localization of the TRP store-operated channel to a signaling complex Neuron 18 1997 95 105
    • (1997) Neuron , vol.18 , pp. 95-105
    • Chevesich, J1    Kreuz, AJ2    Montell, C3
  • 6
    • 0030856343 scopus 로고    scopus 로고
    • Association of INAD with NORPA is essential for controlled activation and deactivation of Drosophila phototransduction in vivo
    • BH Shieh MY Zhu JK Lee IM Kelly F Bahiraei Association of INAD with NORPA is essential for controlled activation and deactivation of Drosophila phototransduction in vivo of special interest Proc Natl Acad Sci USA 11 1997 12682 12687
    • (1997) Proc Natl Acad Sci USA , vol.11 , pp. 12682-12687
    • Shieh, BH1    Zhu, MY2    Lee, JK3    Kelly, IM4    Bahiraei, F5
  • 7
    • 0030835610 scopus 로고    scopus 로고
    • A multivalent PDZ-domain protein assembles signalling complexes in a G-protein-coupled cascade
    • S Tsunoda J Sierralta Y Sun R Bodner E Suzuki A Becker M Socolich CS Zuker A multivalent PDZ-domain protein assembles signalling complexes in a G-protein-coupled cascade of outstanding interest Nature 388 1997 243 249
    • (1997) Nature , vol.388 , pp. 243-249
    • Tsunoda, S1    Sierralta, J2    Sun, Y3    Bodner, R4    Suzuki, E5    Becker, A6    Socolich, M7    Zuker, CS8
  • 8
    • 0029993728 scopus 로고    scopus 로고
    • LET-23 receptor localization by the cell junction protein LIN-7 during C. elegans vulval induction
    • JS Simske SM Kaech SA Harp SK Kim LET-23 receptor localization by the cell junction protein LIN-7 during C. elegans vulval induction Cell 85 1996 195 204
    • (1996) Cell , vol.85 , pp. 195-204
    • Simske, JS1    Kaech, SM2    Harp, SA3    Kim, SK4
  • 9
    • 0030910976 scopus 로고    scopus 로고
    • Camguk, Lin-2, and CASK: novel membrane-associated guanylate kinase homologs that also contain CaM kinase domains
    • SD Dimitratos DF Woods PJ Bryant Camguk, Lin-2, and CASK: novel membrane-associated guanylate kinase homologs that also contain CaM kinase domains Mech Dev 63 1997 127 130
    • (1997) Mech Dev , vol.63 , pp. 127-130
    • Dimitratos, SD1    Woods, DF2    Bryant, PJ3
  • 10
    • 0030067804 scopus 로고    scopus 로고
    • The C. elegans vulval induction gene lin-2 encodes a member of the MAGUK family of cell junction proteins
    • R Hoskins AF Hajnal SA Harp SK Kim The C. elegans vulval induction gene lin-2 encodes a member of the MAGUK family of cell junction proteins Development 122 1996 97 111
    • (1996) Development , vol.122 , pp. 97-111
    • Hoskins, R1    Hajnal, AF2    Harp, SA3    Kim, SK4
  • 11
    • 0030273003 scopus 로고    scopus 로고
    • PDZs and receptor/channel clustering: rounding up the latest suspects
    • M Sheng PDZs and receptor/channel clustering: rounding up the latest suspects Neuron 17 1996 575 578
    • (1996) Neuron , vol.17 , pp. 575-578
    • Sheng, M1
  • 12
    • 0032524629 scopus 로고    scopus 로고
    • PDZ proteins organize synaptic signaling pathways
    • SE Craven DS Bredt PDZ proteins organize synaptic signaling pathways of special interest Cell 93 1999 495 498
    • (1999) Cell , vol.93 , pp. 495-498
    • Craven, SE1    Bredt, DS2
  • 14
    • 0030612949 scopus 로고    scopus 로고
    • Syanptic clustering of Fasciclin II and Shaker: essential targeting sequences and role of Dlg
    • K Zito RD Fetter CS Goodman EY Isacoff Syanptic clustering of Fasciclin II and Shaker: essential targeting sequences and role of Dlg of special interest Neuron 19 1997 1007 1016
    • (1997) Neuron , vol.19 , pp. 1007-1016
    • Zito, K1    Fetter, RD2    Goodman, CS3    Isacoff, EY4
  • 15
    • 0030900558 scopus 로고    scopus 로고
    • GRIP: a synaptic PDZ domain-containing protein that interact with AMPA receptors
    • H Dong RJ O'Brien ET Fung AA Lanahan PF Worley RL Huganir GRIP: a synaptic PDZ domain-containing protein that interact with AMPA receptors Nature 386 1997 279 284
    • (1997) Nature , vol.386 , pp. 279-284
    • Dong, H1    O'Brien, RJ2    Fung, ET3    Lanahan, AA4    Worley, PF5    Huganir, RL6
  • 16
    • 0030273552 scopus 로고    scopus 로고
    • Binding of the inward rectifier K+ channel Kir 2.3 to PSD-95 is regulated by protein kinase A phosphorylation
    • + channel Kir 2.3 to PSD-95 is regulated by protein kinase A phosphorylation Neuron 17 1996 759 767
    • (1996) Neuron , vol.17 , pp. 759-767
    • Cohen, NA1    Brenman, JE2    Snyder, SH3    Bredt, DS4
  • 17
    • 0030200438 scopus 로고    scopus 로고
    • Heteromultimerization and NMDA receptor clustering activity of Chapsyn-110, a member of the PSD-95 family of proteins
    • E Kim K-O Cho A Rothschild M Sheng Heteromultimerization and NMDA receptor clustering activity of Chapsyn-110, a member of the PSD-95 family of proteins Neuron 17 1996 103 113
    • (1996) Neuron , vol.17 , pp. 103-113
    • Kim, E1    Cho, K-O2    Rothschild, A3    Sheng, M4
  • 18
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • H-C Kornau LT Schenker MB Kennedy PH Seeburg Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95 Science 269 1995 1737 1740
    • (1995) Science , vol.269 , pp. 1737-1740
    • Kornau, H-C1    Schenker, LT2    Kennedy, MB3    Seeburg, PH4
  • 19
    • 0032055396 scopus 로고    scopus 로고
    • Syn-gap: a synaptic rasgap that associates with the PSD-95/SAP90 protein family
    • JH Kim D Liao L-F Lau R Huganir Syn-gap: a synaptic rasgap that associates with the PSD-95/SAP90 protein family Neuron 20 1998 638 691
    • (1998) Neuron , vol.20 , pp. 638-691
    • Kim, JH1    Liao, D2    Lau, L-F3    Huganir, R4
  • 20
    • 0031594886 scopus 로고    scopus 로고
    • Plasma membrane Ca2+ ATPase isoform 4b binds to membrane-associated guanylate kinase (MAGUK) proteins via their PDZ (PSD-95/Dlg/ZO-1) domains
    • 2+ ATPase isoform 4b binds to membrane-associated guanylate kinase (MAGUK) proteins via their PDZ (PSD-95/Dlg/ZO-1) domains J Biol Chem 273 1998 1591 1595
    • (1998) J Biol Chem , vol.273 , pp. 1591-1595
    • Kim, E1    DeMarco, SJ2    Marfatia, SM3    Chishti, AH4    Sheng, M5    Strehler, EE6
  • 21
    • 13344277364 scopus 로고    scopus 로고
    • Interaction of nitric oxid synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domains
    • JE Brenman DS Chao SH Gee AW McGee SE Craven DR Santillano Z Wu F Huang H Xia MF Peters Interaction of nitric oxid synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domains Cell 84 1996 757 767
    • (1996) Cell , vol.84 , pp. 757-767
    • Brenman, JE1    Chao, DS2    Gee, SH3    McGee, AW4    Craven, SE5    Santillano, DR6    Wu, Z7    Huang, F8    Xia, H9    Peters, MF10
  • 22
    • 0030777701 scopus 로고    scopus 로고
    • Synaptic clustering of the cell adhesion molecule Fasciclin II by Disc-Large and its role in the regulation of presynaptic structure
    • U Thomas E Kim S Kuhlendahl YH Koh ED Gundelfinger M Sheng CC Garner V Budnik Synaptic clustering of the cell adhesion molecule Fasciclin II by Disc-Large and its role in the regulation of presynaptic structure of special interest Neuron 19 1997 787 799
    • (1997) Neuron , vol.19 , pp. 787-799
    • Thomas, U1    Kim, E2    Kuhlendahl, S3    Koh, YH4    Gundelfinger, ED5    Sheng, M6    Garner, CC7    Budnik, V8
  • 24
    • 0028882810 scopus 로고
    • Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases
    • + channels by interaction with a family of membrane-associated guanylate kinases Nature 378 1995 85 88
    • (1995) Nature , vol.378 , pp. 85-88
    • Kim, E1    Niethhammer, M2    Rothschild, A3    Jan, YN4    Sheng, M5
  • 25
    • 0028920365 scopus 로고
    • The proliferation of MAP kinase signaling pathways in yeast
    • DE Levin B Errede The proliferation of MAP kinase signaling pathways in yeast Curr Opin Cell Biol 7 1995 197 202
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 197-202
    • Levin, DE1    Errede, B2
  • 26
    • 0031058930 scopus 로고    scopus 로고
    • Pheromone signalling and polarized morphogenesis in yeast
    • E Leberer DY Thomas M Whiteway Pheromone signalling and polarized morphogenesis in yeast Curr Opin Genet Dev 7 1997 59 67
    • (1997) Curr Opin Genet Dev , vol.7 , pp. 59-67
    • Leberer, E1    Thomas, DY2    Whiteway, M3
  • 27
    • 0030450397 scopus 로고    scopus 로고
    • Dimerization of Ste5, a mitogen-activated protein kinase cascade scaffold protein, is required for signal transduction
    • D Yablonski I Marbach A Levitzki Dimerization of Ste5, a mitogen-activated protein kinase cascade scaffold protein, is required for signal transduction Proc Natl Acad Sci USA 93 1996 13864 13869
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13864-13869
    • Yablonski, D1    Marbach, I2    Levitzki, A3
  • 28
    • 0030777328 scopus 로고    scopus 로고
    • Mutational analysis of STE5 in the yeast Saccharomyces cerevisiae: application of a differential interaction trap assay for examining protein—protein interactions
    • C Inouye N Dhillon T Durfee PC Zambryski J Thorner Mutational analysis of STE5 in the yeast Saccharomyces cerevisiae : application of a differential interaction trap assay for examining protein—protein interactions Genetics 147 1997 479 492
    • (1997) Genetics , vol.147 , pp. 479-492
    • Inouye, C1    Dhillon, N2    Durfee, T3    Zambryski, PC4    Thorner, J5
  • 29
    • 0030815533 scopus 로고    scopus 로고
    • Ste5 RING-H2 domain: role in Ste4-promoted oligomerization for yeast pheromone signaling
    • C Inouye N Dhillon J Thorner Ste5 RING-H2 domain: role in Ste4-promoted oligomerization for yeast pheromone signaling Science 278 1997 103 106
    • (1997) Science , vol.278 , pp. 103-106
    • Inouye, C1    Dhillon, N2    Thorner, J3
  • 30
    • 0031932282 scopus 로고    scopus 로고
    • N-Terminal palmitoylation of PSD-95 regulates association with cell membranes and interaction with K+ channel Kv 1.4
    • v 1.4 of special interest Neuron 20 1998 125 134
    • (1998) Neuron , vol.20 , pp. 125-134
    • Topinka, JR1    Bredt, DS2
  • 31
    • 0031932281 scopus 로고    scopus 로고
    • CAPON: a protein associated with neuronal nitric oxide synthase that regulates its interactions with PSD95
    • SR Jaffrey AM Snowman MJL Eliasson NA Cohen SH Snyder CAPON: a protein associated with neuronal nitric oxide synthase that regulates its interactions with PSD95 Neuron 20 1998 115 124
    • (1998) Neuron , vol.20 , pp. 115-124
    • Jaffrey, SR1    Snowman, AM2    Eliasson, MJL3    Cohen, NA4    Snyder, SH5
  • 32
    • 0030774987 scopus 로고    scopus 로고
    • Binding of high-risk human papillomavirus E6 oncoproteins to the human homologue of the Drosophila discs large tumor supressor protein
    • T Kiyono A Hiraiwa M Fujita Y Hayashi T Akiyama M Ishibashi Binding of high-risk human papillomavirus E6 oncoproteins to the human homologue of the Drosophila discs large tumor supressor protein Proc Natl Acad Sci USA 94 1997 11612 11616
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11612-11616
    • Kiyono, T1    Hiraiwa, A2    Fujita, M3    Hayashi, Y4    Akiyama, T5    Ishibashi, M6
  • 33
    • 0030950410 scopus 로고    scopus 로고
    • Binding of human virus oncoproteins to hDlg/SAP97, a mammalian homolog of the Drosophila discs large tumor supressor protein
    • SS Lee RS Weiss RT Javier Binding of human virus oncoproteins to hDlg/SAP97, a mammalian homolog of the Drosophila discs large tumor supressor protein Proc Natl Acad Sci USA 94 1997 6670 6675
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6670-6675
    • Lee, SS1    Weiss, RS2    Javier, RT3
  • 34
    • 0030827949 scopus 로고    scopus 로고
    • Actinin-associated LIM protein: identification of a domain interaction between PDZ and spectrin-like repeat motifs
    • H Xia ST Winokur WL Kuo MR Altherr DS Bredt Actinin-associated LIM protein: identification of a domain interaction between PDZ and spectrin-like repeat motifs J Cell Biol 139 1997 507 515
    • (1997) J Cell Biol , vol.139 , pp. 507-515
    • Xia, H1    Winokur, ST2    Kuo, WL3    Altherr, MR4    Bredt, DS5
  • 35
    • 0030763609 scopus 로고    scopus 로고
    • The PDZ domain of human erythrocyte p55 mediates its binding to the cytoplasmic carboxyl terminus of glycophorin C
    • SM Marfatia JH Morais-Cabral AC Kim O Byron AH Chishti The PDZ domain of human erythrocyte p55 mediates its binding to the cytoplasmic carboxyl terminus of glycophorin C J Biol Chem 272 1997 24191 24197
    • (1997) J Biol Chem , vol.272 , pp. 24191-24197
    • Marfatia, SM1    Morais-Cabral, JH2    Kim, AC3    Byron, O4    Chishti, AH5
  • 36
    • 0028096801 scopus 로고
    • Cloning and characterization of hdlg: the human homologue of the Drosophila discs large tumor supressor binds to protein 4.1
    • RA Lue SM Marfatia D Branton AH Chishti Cloning and characterization of hdlg: the human homologue of the Drosophila discs large tumor supressor binds to protein 4.1 Proc Natl Acad Sci USA 91 1994 9818 9822
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9818-9822
    • Lue, RA1    Marfatia, SM2    Branton, D3    Chishti, AH4
  • 37
    • 0022168490 scopus 로고
    • Stabilizing infrastructure of cell membranes
    • VT Marchesi Stabilizing infrastructure of cell membranes Annu Rev Cell Biol 1 1985 531 561
    • (1985) Annu Rev Cell Biol , vol.1 , pp. 531-561
    • Marchesi, VT1
  • 39
    • 0030921919 scopus 로고    scopus 로고
    • Disulfide-linked head-to-head multimerization in the mechanism of ion channel clustering by PSD-95
    • Y-P Hsueh E Kim M Sheng Disulfide-linked head-to-head multimerization in the mechanism of ion channel clustering by PSD-95 of special interest Neuron 18 1997 803 814
    • (1997) Neuron , vol.18 , pp. 803-814
    • Hsueh, Y-P1    Kim, E2    Sheng, M3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.