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Volumn 26, Issue 8, 2007, Pages 2192-2205

Crystal structures of autoinhibitory PDZ domain of Tamalin: Implications for metabotropic glutamate receptor trafficking regulation

Author keywords

Autoinhibited assembly; Metabotropic glutamate receptor; PDZ domain; Tamalin; Trafficking

Indexed keywords

LIGAND; METABOTROPIC RECEPTOR; MOLECULAR MOTOR; PDZ PROTEIN; SCAFFOLD PROTEIN; TAMALIN; UNCLASSIFIED DRUG;

EID: 34247238159     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/sj.emboj.7601651     Document Type: Article
Times cited : (39)

References (35)
  • 3
    • 14644387575 scopus 로고    scopus 로고
    • Emerging role of homoand heterodimerization in G-protein-coupled receptor biosynthesis and maturation
    • Bulenger S, Marullo S, Bouvier M (2005) Emerging role of homoand heterodimerization in G-protein-coupled receptor biosynthesis and maturation. Trends Pharmacol Sci 26: 131-137
    • (2005) Trends Pharmacol Sci , vol.26 , pp. 131-137
    • Bulenger, S.1    Marullo, S.2    Bouvier, M.3
  • 4
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computational Project n.4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D 50: 760-763
    • Collaborative Computational Project n.4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D 50: 760-763
  • 5
    • 33748146106 scopus 로고    scopus 로고
    • The role of protein interaction motifs in regulating the polarity and clustering of the metabotropic glutamate receptor mGluR1a
    • Das SS, Banker GA (2006) The role of protein interaction motifs in regulating the polarity and clustering of the metabotropic glutamate receptor mGluR1a. J Neurosci 26: 8115-8125
    • (2006) J Neurosci , vol.26 , pp. 8115-8125
    • Das, S.S.1    Banker, G.A.2
  • 6
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods
    • de La Fortelle E, Bricogne G (1997) Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods. Methods Enzymol 276: 472-494
    • (1997) Methods Enzymol , vol.276 , pp. 472-494
    • de La Fortelle, E.1    Bricogne, G.2
  • 8
    • 2342470026 scopus 로고    scopus 로고
    • Identification and functional roles of metabotropic glutamate receptor-interacting proteins
    • Fagni L, Ango F, Perroy J, Bockaert J (2004) Identification and functional roles of metabotropic glutamate receptor-interacting proteins. Semin Cell Dev Biol 15: 289-298
    • (2004) Semin Cell Dev Biol , vol.15 , pp. 289-298
    • Fagni, L.1    Ango, F.2    Perroy, J.3    Bockaert, J.4
  • 9
    • 2342520109 scopus 로고    scopus 로고
    • The tetrameric L27 domain complex as an organization platform for supramolecular assemblies
    • Feng W, Long JF, Fan JS, Suetake T, Zhang M (2004) The tetrameric L27 domain complex as an organization platform for supramolecular assemblies. Nat Struct Mol Biol 11: 475-480
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 475-480
    • Feng, W.1    Long, J.F.2    Fan, J.S.3    Suetake, T.4    Zhang, M.5
  • 10
    • 0037131192 scopus 로고    scopus 로고
    • Regulation of G protein-coupled receptor signaling by scaffold proteins
    • Hall RA, Lefkowitz RJ (2002) Regulation of G protein-coupled receptor signaling by scaffold proteins. Circ Res 91: 672-680
    • (2002) Circ Res , vol.91 , pp. 672-680
    • Hall, R.A.1    Lefkowitz, R.J.2
  • 11
    • 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
  • 13
    • 0037155199 scopus 로고    scopus 로고
    • PDZ domains: Structural modules for protein complex assembly
    • Hung AY, Sheng M (2002) PDZ domains: structural modules for protein complex assembly. J Biol Chem 277: 5699-5702
    • (2002) J Biol Chem , vol.277 , pp. 5699-5702
    • Hung, A.Y.1    Sheng, M.2
  • 14
    • 0348111461 scopus 로고    scopus 로고
    • Crystal structure of the Shank PDZ-ligand complex reveals a class I PDZ interaction and a novel PDZ-PDZ dimerization
    • Im YJ, Lee JH, Park SH, Park SJ, Rho SH, Kang GB, Kim E, Eom SH (2003a) Crystal structure of the Shank PDZ-ligand complex reveals a class I PDZ interaction and a novel PDZ-PDZ dimerization. J Biol Chem 278: 48099-48104
    • (2003) J Biol Chem , vol.278 , pp. 48099-48104
    • Im, Y.J.1    Lee, J.H.2    Park, S.H.3    Park, S.J.4    Rho, S.H.5    Kang, G.B.6    Kim, E.7    Eom, S.H.8
  • 15
    • 0037424515 scopus 로고    scopus 로고
    • Crystal structure of GRIP1 PDZ6-peptide complex reveals the structural basis for class II PDZ target recognition and PDZ domain-mediated multimerization
    • Im YJ, Park SH, Rho SH, Lee JH, Kang GB, Sheng M, Kim E, Eom SH (2003b) Crystal structure of GRIP1 PDZ6-peptide complex reveals the structural basis for class II PDZ target recognition and PDZ domain-mediated multimerization. J Biol Chem 278: 8501-8507
    • (2003) J Biol Chem , vol.278 , pp. 8501-8507
    • Im, Y.J.1    Park, S.H.2    Rho, S.H.3    Lee, J.H.4    Kang, G.B.5    Sheng, M.6    Kim, E.7    Eom, S.H.8
  • 16
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47 (Part 2): 110-119
    • (1991) Acta Crystallogr A , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 17
    • 0035827518 scopus 로고    scopus 로고
    • + exchanger regulatory factor PDZ1 interaction with the carboxyl-terminal region of the cystic fibrosis transmembrane conductance regulator
    • + exchanger regulatory factor PDZ1 interaction with the carboxyl-terminal region of the cystic fibrosis transmembrane conductance regulator. J Biol Chem 276: 19683-19686
    • (2001) J Biol Chem , vol.276 , pp. 19683-19686
    • Karthikeyan, S.1    Leung, T.2    Ladias, J.A.3
  • 18
    • 0034721678 scopus 로고    scopus 로고
    • Signal-processing machines at the postsynaptic density
    • Kennedy MB (2000) Signal-processing machines at the postsynaptic density. Science 290: 750-754
    • (2000) Science , vol.290 , pp. 750-754
    • Kennedy, M.B.1
  • 19
    • 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
  • 20
    • 0037083370 scopus 로고    scopus 로고
    • Tamalin, a PDZ domain-containing protein, links a protein complex formation of group 1 metabotropic glutamate receptors and the guanine nucleotide exchange factor cytohesins
    • Kitano J, Kimura K, Yamazaki Y, Soda T, Shigemoto R, Nakajima Y, Nakanishi S (2002) Tamalin, a PDZ domain-containing protein, links a protein complex formation of group 1 metabotropic glutamate receptors and the guanine nucleotide exchange factor cytohesins. J Neurosci 22: 1280-1289
    • (2002) J Neurosci , vol.22 , pp. 1280-1289
    • Kitano, J.1    Kimura, K.2    Yamazaki, Y.3    Soda, T.4    Shigemoto, R.5    Nakajima, Y.6    Nakanishi, S.7
  • 21
    • 0038013863 scopus 로고    scopus 로고
    • Tamalin is a scaffold protein that interacts with multiple neuronal proteins in distinct modes of protein-protein association
    • Kitano J, Yamazaki Y, Kimura K, Masukado T, Nakajima Y, Nakanishi S (2003) Tamalin is a scaffold protein that interacts with multiple neuronal proteins in distinct modes of protein-protein association. J Biol Chem 278: 14762-14768
    • (2003) J Biol Chem , vol.278 , pp. 14762-14768
    • Kitano, J.1    Yamazaki, Y.2    Kimura, K.3    Masukado, T.4    Nakajima, Y.5    Nakanishi, S.6
  • 22
    • 21444447912 scopus 로고    scopus 로고
    • Postsynaptic scaffold proteins at non-synaptic sites. The role of postsynaptic scaffold proteins in motor-protein-receptor complexes
    • Kneussel M (2005) Postsynaptic scaffold proteins at non-synaptic sites. The role of postsynaptic scaffold proteins in motor-protein-receptor complexes. EMBO Rep 6: 22-27
    • (2005) EMBO Rep , vol.6 , pp. 22-27
    • Kneussel, M.1
  • 24
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss D, Thornton JM (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26: 283-291
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.3    Thornton, J.M.4
  • 25
    • 17644402459 scopus 로고    scopus 로고
    • Transduction of receptor signals by beta-arrestins
    • Lefkowitz RJ, Shenoy SK (2005) Transduction of receptor signals by beta-arrestins. Science 308: 512-517
    • (2005) Science , vol.308 , pp. 512-517
    • Lefkowitz, R.J.1    Shenoy, S.K.2
  • 26
    • 0242551549 scopus 로고    scopus 로고
    • Some assembly required: The development of neuronal synapses
    • Li Z, Sheng M (2003) Some assembly required: the development of neuronal synapses. Nat Rev Mol Cell Biol 4: 833-841
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 833-841
    • Li, Z.1    Sheng, M.2
  • 27
    • 26944496474 scopus 로고    scopus 로고
    • Autoinhibition of X11/Mint scaffold proteins revealed by the closed conformation of the PDZ tandem
    • Long JF, Feng W, Wang R, Chan LN, Ip FC, Xia J, Ip NY, Zhang M (2005) Autoinhibition of X11/Mint scaffold proteins revealed by the closed conformation of the PDZ tandem. Nat Struct Mol Biol 12: 722-728
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 722-728
    • Long, J.F.1    Feng, W.2    Wang, R.3    Chan, L.N.4    Ip, F.C.5    Xia, J.6    Ip, N.Y.7    Zhang, M.8
  • 28
    • 0036662882 scopus 로고    scopus 로고
    • Association of the kinesin superfamily motor protein KIF1Balpha with postsynaptic density-95 (PSD-95), synapse-associated protein-97, and synaptic scaffolding molecule PSD-95/discs large/zona occludens-1 proteins
    • Mok H, Shin H, Kim S, Lee JR, Yoon J, Kim E (2002) Association of the kinesin superfamily motor protein KIF1Balpha with postsynaptic density-95 (PSD-95), synapse-associated protein-97, and synaptic scaffolding molecule PSD-95/discs large/zona occludens-1 proteins. J Neurosci 22: 5253-5258
    • (2002) J Neurosci , vol.22 , pp. 5253-5258
    • Mok, H.1    Shin, H.2    Kim, S.3    Lee, J.R.4    Yoon, J.5    Kim, E.6
  • 29
    • 0034595664 scopus 로고    scopus 로고
    • Interaction of GRASP, a protein encoded by a novel retinoic acid-induced gene, with members of the cytohesin family of guanine nucleotide exchange factors
    • Nevrivy DJ, Peterson VJ, Avram D, Ishmael JE, Hansen SG, Dowell P, Hruby DE, Dawson MI, Leid M (2000) Interaction of GRASP, a protein encoded by a novel retinoic acid-induced gene, with members of the cytohesin family of guanine nucleotide exchange factors. J Biol Chem 275: 16827-16836
    • (2000) J Biol Chem , vol.275 , pp. 16827-16836
    • Nevrivy, D.J.1    Peterson, V.J.2    Avram, D.3    Ishmael, J.E.4    Hansen, S.G.5    Dowell, P.6    Hruby, D.E.7    Dawson, M.I.8    Leid, M.9
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Method Enzymol 276: 307-326
    • (1997) Method Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 31
    • 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
  • 32
    • 0036441510 scopus 로고    scopus 로고
    • Autoinhibitory domains: Modular effectors of cellular regulation
    • Pufall MA, Graves BJ (2002) Autoinhibitory domains: modular effectors of cellular regulation. Annu Rev Cell Dev Biol 18: 421-462
    • (2002) Annu Rev Cell Dev Biol , vol.18 , pp. 421-462
    • Pufall, M.A.1    Graves, B.J.2
  • 33
    • 2942746419 scopus 로고    scopus 로고
    • Caspase activation: Revisiting the induced proximity model
    • Shi Y (2004) Caspase activation: revisiting the induced proximity model. Cell 117: 855-858
    • (2004) Cell , vol.117 , pp. 855-858
    • Shi, Y.1
  • 35
    • 0344413477 scopus 로고    scopus 로고
    • Direct binding of the PDZ domain of Dishevelled to a conserved internal sequence in the C-terminal region of Frizzled
    • Wong HC, Bourdelas A, Krauss A, Lee HJ, Shao Y, Wu D, Mlodzik M, Shi DL, Zheng J (2003) Direct binding of the PDZ domain of Dishevelled to a conserved internal sequence in the C-terminal region of Frizzled. Mol Cell 12: 1251-1260
    • (2003) Mol Cell , vol.12 , pp. 1251-1260
    • Wong, H.C.1    Bourdelas, A.2    Krauss, A.3    Lee, H.J.4    Shao, Y.5    Wu, D.6    Mlodzik, M.7    Shi, D.L.8    Zheng, J.9


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