메뉴 건너뛰기




Volumn 6, Issue 9, 2008, Pages 2043-2059

A specificity map for the PDZ domain family

Author keywords

[No Author keywords available]

Indexed keywords

PDZ PROTEIN; CAENORHABDITIS ELEGANS PROTEIN; MEMBRANE PROTEIN; PEPTIDE; PROTEOME; SCRIB PROTEIN, HUMAN; TUMOR SUPPRESSOR PROTEIN; VIRUS PROTEIN;

EID: 54749086397     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.0060239     Document Type: Article
Times cited : (386)

References (56)
  • 1
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • Pawson T, Nash P (2003) Assembly of cell regulatory systems through protein interaction domains. Science 300: 445-452.
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 2
    • 0034740693 scopus 로고    scopus 로고
    • Mechanism and role of PDZ domains in signaling complex assembly
    • Harris BZ, Lim WA (2001) Mechanism and role of PDZ domains in signaling complex assembly. J Cell Sci 114: 3219-3231.
    • (2001) J Cell Sci , vol.114 , pp. 3219-3231
    • Harris, B.Z.1    Lim, W.A.2
  • 3
    • 0034916230 scopus 로고    scopus 로고
    • PDZ domains and the organization of supramolecular complexes
    • Sheng M, Sala C (2001) PDZ domains and the organization of supramolecular complexes. Annu Rev Neurosci 24: 1-29.
    • (2001) Annu Rev Neurosci , vol.24 , pp. 1-29
    • Sheng, M.1    Sala, C.2
  • 4
    • 0038795589 scopus 로고    scopus 로고
    • Dlg, Scribble and Lgl in cell polarity, cell proliferation and cancer
    • Humbert P, Russell S, Richardson H (2003) Dlg, Scribble and Lgl in cell polarity, cell proliferation and cancer. Bioessays 25: 542-553.
    • (2003) Bioessays , vol.25 , pp. 542-553
    • Humbert, P.1    Russell, S.2    Richardson, H.3
  • 5
    • 5044224260 scopus 로고    scopus 로고
    • PDZ domain proteins of synapses
    • Kim E, Sheng M (2004) PDZ domain proteins of synapses. Nat Rev Neurosci 5: 771-781.
    • (2004) Nat Rev Neurosci , vol.5 , pp. 771-781
    • Kim, E.1    Sheng, M.2
  • 6
    • 20444445916 scopus 로고    scopus 로고
    • A network of PDZ-containing proteins regulates T cell polarity and morphology during migration and immunological synapse formation
    • Ludford-Menting MJ, Oliaro J, Sacirbegovic F, Cheah ET, Pedersen N, et al. (2005) A network of PDZ-containing proteins regulates T cell polarity and morphology during migration and immunological synapse formation. Immunity 22: 737-748.
    • (2005) Immunity , vol.22 , pp. 737-748
    • Ludford-Menting, M.J.1    Oliaro, J.2    Sacirbegovic, F.3    Cheah, E.T.4    Pedersen, N.5
  • 7
    • 0037174635 scopus 로고    scopus 로고
    • Treatment of ischemic brain damage by perturbing NMDA receptor- PSD-95 protein interactions
    • Aarts M, Liu Y, Liu L, Besshoh S, Arundine M, et al. (2002) Treatment of ischemic brain damage by perturbing NMDA receptor- PSD-95 protein interactions. Science 298: 846-850.
    • (2002) Science , vol.298 , pp. 846-850
    • Aarts, M.1    Liu, Y.2    Liu, L.3    Besshoh, S.4    Arundine, M.5
  • 8
    • 30344455042 scopus 로고    scopus 로고
    • Identification of a bacterial type III effector family with G protein mimicry functions
    • Alto NM, Shao F, Lazar CS, Brost RL, Chua G, et al. (2006) Identification of a bacterial type III effector family with G protein mimicry functions. Cell 124: 133-145.
    • (2006) Cell , vol.124 , pp. 133-145
    • Alto, N.M.1    Shao, F.2    Lazar, C.S.3    Brost, R.L.4    Chua, G.5
  • 9
    • 10444276589 scopus 로고    scopus 로고
    • Making protein interactions druggable: Targeting PDZ domains
    • Dev KK (2004) Making protein interactions druggable: targeting PDZ domains. Nat Rev Drug Discov 3: 1047-1056.
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 1047-1056
    • Dev, K.K.1
  • 10
    • 33646675570 scopus 로고    scopus 로고
    • Molecular biology of human papillomavirus infection and cervical cancer
    • Doorbar J (2006) Molecular biology of human papillomavirus infection and cervical cancer. Clin Sci 110: 525-541.
    • (2006) Clin Sci , vol.110 , pp. 525-541
    • Doorbar, J.1
  • 11
    • 0037421970 scopus 로고    scopus 로고
    • Selective PDZ protein-dependent stimulation of phosphatidylinositol 3-kinase by the adenovirus E4-ORF1 oncoprotein
    • Frese KK, Lee SS, Thomas DL, Latorre IJ, Weiss RS, et al. (2003) Selective PDZ protein-dependent stimulation of phosphatidylinositol 3-kinase by the adenovirus E4-ORF1 oncoprotein. Oncogene 22: 710-721.
    • (2003) Oncogene , vol.22 , pp. 710-721
    • Frese, K.K.1    Lee, S.S.2    Thomas, D.L.3    Latorre, I.J.4    Weiss, R.S.5
  • 12
    • 25444512922 scopus 로고    scopus 로고
    • Deregulation of cell-signaling pathways in HTLV-1 infection
    • Hall WW, Fujii M (2005) Deregulation of cell-signaling pathways in HTLV-1 infection. Oncogene 24: 5965-5975.
    • (2005) Oncogene , vol.24 , pp. 5965-5975
    • Hall, W.W.1    Fujii, M.2
  • 13
    • 33645067624 scopus 로고    scopus 로고
    • Large-scale sequence analysis of avian influenza isolates
    • Obenauer JC, Denson J, Mehta PK, Su X, Mukatira S, et al. (2006) Large-scale sequence analysis of avian influenza isolates. Science 311: 1576-1580.
    • (2006) Science , vol.311 , pp. 1576-1580
    • Obenauer, J.C.1    Denson, J.2    Mehta, P.K.3    Su, X.4    Mukatira, S.5
  • 15
    • 0043092191 scopus 로고    scopus 로고
    • Wnt pathway activation in mesothelioma: Evidence of Dishevelled overexpression and transcriptional activity of beta-catenin
    • Uematsu K, Kanazawa S, You L, He B, Xu Z, et al. (2003) Wnt pathway activation in mesothelioma: evidence of Dishevelled overexpression and transcriptional activity of beta-catenin. Cancer Res 63: 4547-4551.
    • (2003) Cancer Res , vol.63 , pp. 4547-4551
    • Uematsu, K.1    Kanazawa, S.2    You, L.3    He, B.4    Xu, Z.5
  • 16
    • 15644379801 scopus 로고    scopus 로고
    • Recognition of unique carboxyl-terminal motifs by distinct PDZ domains
    • Songyang Z, Fanning AS, Fu C, Xu J, Marfatia SM, et al. (1997) Recognition of unique carboxyl-terminal motifs by distinct PDZ domains. Science 275: 73-77.
    • (1997) Science , vol.275 , pp. 73-77
    • Songyang, Z.1    Fanning, A.S.2    Fu, C.3    Xu, J.4    Marfatia, S.M.5
  • 17
    • 0030895195 scopus 로고    scopus 로고
    • PDZ domain of neuronal nitric oxide synthase recognizes novel C-terminal peptide sequences
    • Stricker NL, Christopherson KS, Yi BA, Schatz PJ, Raab RW, et al. (1997) PDZ domain of neuronal nitric oxide synthase recognizes novel C-terminal peptide sequences. Nat Biotechnol 15: 336-342.
    • (1997) Nat Biotechnol , vol.15 , pp. 336-342
    • Stricker, N.L.1    Christopherson, K.S.2    Yi, B.A.3    Schatz, P.J.4    Raab, R.W.5
  • 18
    • 0035834678 scopus 로고    scopus 로고
    • Distinct binding specificity of the multiple PDZ domains of INADL, a human protein with homology to INAD from Drosophila melanogaster
    • Vaccaro P, Brannetti B, Montecchi-Palazzi L, Philipp S, Helmer Citterich M, et al. (2001) Distinct binding specificity of the multiple PDZ domains of INADL, a human protein with homology to INAD from Drosophila melanogaster. J Biol Chem 276: 42122-42130.
    • (2001) J Biol Chem , vol.276 , pp. 42122-42130
    • Vaccaro, P.1    Brannetti, B.2    Montecchi-Palazzi, L.3    Philipp, S.4    Helmer Citterich, M.5
  • 19
    • 0032522739 scopus 로고    scopus 로고
    • Two distantly positioned PDZ domains mediate multivalent INAD-phospholipase C interactions essential for G protein-coupled signaling
    • van Huizen R, Miller K, Chen DM, Li Y, Lai ZC, et al. (1998) Two distantly positioned PDZ domains mediate multivalent INAD-phospholipase C interactions essential for G protein-coupled signaling. EMBO J 17: 2285-2297.
    • (1998) EMBO J , vol.17 , pp. 2285-2297
    • van Huizen, R.1    Miller, K.2    Chen, D.M.3    Li, Y.4    Lai, Z.C.5
  • 20
    • 33746819780 scopus 로고    scopus 로고
    • Convergent and divergent ligand specificity among PDZ domains of the LAP and zonula occludens (ZO) families
    • Zhang Y, Yeh S, Appleton BA, Held HA, Kausalya PJ, et al. (2006) Convergent and divergent ligand specificity among PDZ domains of the LAP and zonula occludens (ZO) families. J Biol Chem 281: 22299-22311.
    • (2006) J Biol Chem , vol.281 , pp. 22299-22311
    • Zhang, Y.1    Yeh, S.2    Appleton, B.A.3    Held, H.A.4    Kausalya, P.J.5
  • 21
    • 0036289460 scopus 로고    scopus 로고
    • PIP(2)-PDZ domain binding controls the association of syntenin with the plasma membrane
    • Zimmermann P, Meerschaert K, Reekmans G, Leenaerts I, Small JV, et al. (2002) PIP(2)-PDZ domain binding controls the association of syntenin with the plasma membrane. Mol Cell 9: 1215-1225.
    • (2002) Mol Cell , vol.9 , pp. 1215-1225
    • Zimmermann, P.1    Meerschaert, K.2    Reekmans, G.3    Leenaerts, I.4    Small, J.V.5
  • 22
    • 36749070993 scopus 로고    scopus 로고
    • PDZ domains of Par-3 as potential phosphoinositide signaling integrators
    • Wu H, Feng W, Chen J, Chan LN, Huang S, et al. (2007) PDZ domains of Par-3 as potential phosphoinositide signaling integrators. Mol Cell 28: 886-898.
    • (2007) Mol Cell , vol.28 , pp. 886-898
    • Wu, H.1    Feng, W.2    Chen, J.3    Chan, L.N.4    Huang, S.5
  • 23
    • 0033617473 scopus 로고    scopus 로고
    • Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex
    • Hillier BJ, Christopherson KS, Prehoda KE, Bredt DS, Lim WA (1999) Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex. Science 284: 812-815.
    • (1999) Science , vol.284 , pp. 812-815
    • Hillier, B.J.1    Christopherson, K.S.2    Prehoda, K.E.3    Bredt, D.S.4    Lim, W.A.5
  • 24
    • 7544232779 scopus 로고    scopus 로고
    • Internal recognition through PDZ domain plasticity in the Par-6-Pals1 complex
    • Penkert RR, DiVittorio HM, Prehoda KE (2004) Internal recognition through PDZ domain plasticity in the Par-6-Pals1 complex. Nat Struct Mol Biol 11: 1122-1127.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1122-1127
    • Penkert, R.R.1    DiVittorio, H.M.2    Prehoda, K.E.3
  • 26
    • 34547127612 scopus 로고    scopus 로고
    • PDZ domain binding selectivity is optimized across the mouse proteome
    • Stiffler MA, Chen JR, Grantcharova VP, Lei Y, Fuchs D, et al. (2007) PDZ domain binding selectivity is optimized across the mouse proteome. Science 317: 364-369.
    • (2007) Science , vol.317 , pp. 364-369
    • Stiffler, M.A.1    Chen, J.R.2    Grantcharova, V.P.3    Lei, Y.4    Fuchs, D.5
  • 27
    • 0034647505 scopus 로고    scopus 로고
    • Analysis of PDZ domain-ligand interactions using carboxyl-terminal phage display
    • Fuh G, Pisabarro MT, Li Y, Quan C, Lasky LA, et al. (2000) Analysis of PDZ domain-ligand interactions using carboxyl-terminal phage display. J Biol Chem 275: 21486-21491.
    • (2000) J Biol Chem , vol.275 , pp. 21486-21491
    • Fuh, G.1    Pisabarro, M.T.2    Li, Y.3    Quan, C.4    Lasky, L.A.5
  • 28
    • 34250748507 scopus 로고    scopus 로고
    • Identifying specificity profiles for peptide recognition modules from phage-displayed peptide libraries
    • Tonikian R, Zhang Y, Boone C, Sidhu SS (2007) Identifying specificity profiles for peptide recognition modules from phage-displayed peptide libraries. Nat Protoc 2: 1368-1386.
    • (2007) Nat Protoc , vol.2 , pp. 1368-1386
    • Tonikian, R.1    Zhang, Y.2    Boone, C.3    Sidhu, S.S.4
  • 29
    • 0037066692 scopus 로고    scopus 로고
    • The Erbin PDZ domain binds with high affinity and specificity to the carboxyl termini of delta-catenin and ARVCF
    • Laura RP, Witt AS, Held HA, Gerstner R, Deshayes K, et al. (2002) The Erbin PDZ domain binds with high affinity and specificity to the carboxyl termini of delta-catenin and ARVCF. J Biol Chem 277: 12906-12914.
    • (2002) J Biol Chem , vol.277 , pp. 12906-12914
    • Laura, R.P.1    Witt, A.S.2    Held, H.A.3    Gerstner, R.4    Deshayes, K.5
  • 30
    • 34547559252 scopus 로고    scopus 로고
    • Structural and functional analysis of the ligand specificity of the HtrA2/Omi PDZ domain
    • Zhang Y, Appleton BA, Wu P, Wiesmann C, Sidhu SS (2007) Structural and functional analysis of the ligand specificity of the HtrA2/Omi PDZ domain. Protein Sci 16: 1738-1750.
    • (2007) Protein Sci , vol.16 , pp. 1738-1750
    • Zhang, Y.1    Appleton, B.A.2    Wu, P.3    Wiesmann, C.4    Sidhu, S.S.5
  • 34
    • 0025008168 scopus 로고
    • Sequence logos: A new way to display consensus sequences
    • Schneider TD, Stephens RM (1990) Sequence logos: a new way to display consensus sequences. Nucleic Acids Res 18: 6097-6100.
    • (1990) Nucleic Acids Res , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2
  • 35
    • 0030604722 scopus 로고    scopus 로고
    • Crystal structures of a complexed and peptide-free membrane protein-binding domain: Molecular basis of peptide recognition by PDZ
    • Doyle DA, Lee A, Lewis J, Kim E, Sheng M, et al. (1996) Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell 85: 1067-1076.
    • (1996) Cell , vol.85 , pp. 1067-1076
    • Doyle, D.A.1    Lee, A.2    Lewis, J.3    Kim, E.4    Sheng, M.5
  • 36
    • 0037470140 scopus 로고    scopus 로고
    • Origins of PDZ domain ligand specificity: Structure determination and mutagenesis of the Erbin PDZ domain
    • Skelton NJ, Koehler MFT, Zobel K, Wong WL, Yeh S, et al. (2003) Origins of PDZ domain ligand specificity: structure determination and mutagenesis of the Erbin PDZ domain. J Biol Chem 278: 7645-7654.
    • (2003) J Biol Chem , vol.278 , pp. 7645-7654
    • Skelton, N.J.1    Koehler, M.F.T.2    Zobel, K.3    Wong, W.L.4    Yeh, S.5
  • 37
    • 33646909100 scopus 로고    scopus 로고
    • Protein family expansions and biological complexity
    • doi:10.1371/journal.pcbi.0020048
    • Vogel C, Chothia C (2006) Protein family expansions and biological complexity. PLoS Comput Biol 2: e48. doi:10.1371/journal.pcbi.0020048
    • (2006) PLoS Comput Biol , vol.2
    • Vogel, C.1    Chothia, C.2
  • 38
    • 0033593549 scopus 로고    scopus 로고
    • Divergence time estimates for the early history of animal phyla and the origin of plants, animals and fungi
    • Wang DY-C, Kumar S, Hedges SB (1999) Divergence time estimates for the early history of animal phyla and the origin of plants, animals and fungi. Proc R Soc Lond B 266: 163-171.
    • (1999) Proc R Soc Lond B , vol.266 , pp. 163-171
    • Wang, D.Y.-C.1    Kumar, S.2    Hedges, S.B.3
  • 39
    • 35649004472 scopus 로고    scopus 로고
    • Structural and functional analysis of the PDZ domains of human HtrA1 and HtrA3
    • Runyon ST, Zhang Y, Appleton BA, Sazinsky SL, Wu P, et al. (2007) Structural and functional analysis of the PDZ domains of human HtrA1 and HtrA3. Protein Sci 16: 2454-2471.
    • (2007) Protein Sci , vol.16 , pp. 2454-2471
    • Runyon, S.T.1    Zhang, Y.2    Appleton, B.A.3    Sazinsky, S.L.4    Wu, P.5
  • 40
    • 39749109484 scopus 로고    scopus 로고
    • Regulation of a late phase of T cell polarity and effector functions by Crtam
    • Yeh JH, Sidhu SS, Chan AC (2008) Regulation of a late phase of T cell polarity and effector functions by Crtam. Cell 132: 846-859.
    • (2008) Cell , vol.132 , pp. 846-859
    • Yeh, J.H.1    Sidhu, S.S.2    Chan, A.C.3
  • 41
    • 22244455455 scopus 로고    scopus 로고
    • Membrane-associated guanylate kinases regulate adhesion and plasticity at cell junctions
    • Funke L, Dakoji S, Bredt DS (2005) Membrane-associated guanylate kinases regulate adhesion and plasticity at cell junctions. Annu Rev Biochem 74: 219-245.
    • (2005) Annu Rev Biochem , vol.74 , pp. 219-245
    • Funke, L.1    Dakoji, S.2    Bredt, D.S.3
  • 42
    • 0037077294 scopus 로고    scopus 로고
    • In vitro evolution of recognition specificity mediated by SH3 domains reveals target recognition rules
    • Panni S, Dente L, Cesareni G (2002) In vitro evolution of recognition specificity mediated by SH3 domains reveals target recognition rules. J Biol Chem 277: 21666-21674.
    • (2002) J Biol Chem , vol.277 , pp. 21666-21674
    • Panni, S.1    Dente, L.2    Cesareni, G.3
  • 44
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • Lockless SW, Ranganathan R (1999) Evolutionarily conserved pathways of energetic connectivity in protein families. Science 286: 295-299.
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 45
    • 0029993728 scopus 로고    scopus 로고
    • LET-23 receptor localization by the cell junction protein LIN-7 during C. elegans vulval induction
    • Simske JS, Kaech SM, Harp SA, Kim SK (1996) LET-23 receptor localization by the cell junction protein LIN-7 during C. elegans vulval induction. Cell 85: 195-204.
    • (1996) Cell , vol.85 , pp. 195-204
    • Simske, J.S.1    Kaech, S.M.2    Harp, S.A.3    Kim, S.K.4
  • 46
    • 37749037799 scopus 로고    scopus 로고
    • Design, synthesis, and biological activity of a potent Smac mimetic that sensitizes cancer cells to apoptosis by antagonizing IAPs. ACS
    • Zobel K, Wang L, Varfolomeev E, Franklin MC, Elliott LO, et al. (2006) Design, synthesis, and biological activity of a potent Smac mimetic that sensitizes cancer cells to apoptosis by antagonizing IAPs. ACS Chem Biol 1: 525-533.
    • (2006) Chem Biol , vol.1 , pp. 525-533
    • Zobel, K.1    Wang, L.2    Varfolomeev, E.3    Franklin, M.C.4    Elliott, L.O.5
  • 47
    • 0141757323 scopus 로고    scopus 로고
    • Reprogramming control of an allosteric signaling switch through modular recombination
    • Dueber JE, Yeh BJ, Chak K, Lim WA (2003) Reprogramming control of an allosteric signaling switch through modular recombination. Science 301: 1904-1908.
    • (2003) Science , vol.301 , pp. 1904-1908
    • Dueber, J.E.1    Yeh, B.J.2    Chak, K.3    Lim, W.A.4
  • 49
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE: A multiple sequence alignment method with reduced time and space complexity
    • Edgar RC (2004) MUSCLE: a multiple sequence alignment method with reduced time and space complexity. BMC Bioinformatics 5: 113.
    • (2004) BMC Bioinformatics , vol.5 , pp. 113
    • Edgar, R.C.1
  • 53
    • 24044440971 scopus 로고    scopus 로고
    • BiNGO: A Cytoscape plugin to assess overrepresentation of gene ontology categories in biological networks
    • Maere S, Heymans K, Kuiper M (2005) BiNGO: a Cytoscape plugin to assess overrepresentation of gene ontology categories in biological networks. Bioinformatics 21: 3448-3449.
    • (2005) Bioinformatics , vol.21 , pp. 3448-3449
    • Maere, S.1    Heymans, K.2    Kuiper, M.3
  • 54
    • 0242490780 scopus 로고    scopus 로고
    • Cytoscape: A software environment for integrated models of biomolecular interaction networks
    • Shannon P, Markiel A, Ozier O, Baliga NS, Want JT, et al. (2003) Cytoscape: a software environment for integrated models of biomolecular interaction networks. Genome Res 13: 2498-2504.
    • (2003) Genome Res , vol.13 , pp. 2498-2504
    • Shannon, P.1    Markiel, A.2    Ozier, O.3    Baliga, N.S.4    Want, J.T.5
  • 55
    • 33746861956 scopus 로고    scopus 로고
    • Comparative structural analysis of the Erbin PDZ domain and the first PDZ domain of ZO-1. Insights into determinants of PDZ domain specificity
    • Appleton BA, Zhang Y, Wu P, Yin JP, Hunziker W, et al. (2006) Comparative structural analysis of the Erbin PDZ domain and the first PDZ domain of ZO-1. Insights into determinants of PDZ domain specificity. J Biol Chem 281: 22312-22320.
    • (2006) J Biol Chem , vol.281 , pp. 22312-22320
    • Appleton, B.A.1    Zhang, Y.2    Wu, P.3    Yin, J.P.4    Hunziker, W.5
  • 56
    • 0037023712 scopus 로고    scopus 로고
    • SMAC negatively regulates the anti-apoptotic activity of melanoma inhibitor of apoptosis (ML-IAP)
    • Vucic D, Deshayes K, Ackerly H, Pisabarro MT, Kadkhodayan S, et al. (2002) SMAC negatively regulates the anti-apoptotic activity of melanoma inhibitor of apoptosis (ML-IAP). J Biol Chem 277: 12275-12279.
    • (2002) J Biol Chem , vol.277 , pp. 12275-12279
    • Vucic, D.1    Deshayes, K.2    Ackerly, H.3    Pisabarro, M.T.4    Kadkhodayan, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.