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Volumn 452, Issue 1, 2014, Pages 130-135

Structure of the GH1 domain of guanylate kinase-associated protein from Rattus norvegicus

Author keywords

GKAP; Helix bundle; Protein structure; Protein protein interaction; Synaptic scaffolding protein; X ray crystallography

Indexed keywords

GUANYLATE KINASE ASSOCIATED PROTEIN; MALTOSE BINDING PROTEIN; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG; GUANYLATE KINASE;

EID: 84907812930     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2014.08.073     Document Type: Article
Times cited : (10)

References (19)
  • 1
    • 0030858386 scopus 로고    scopus 로고
    • Characterization of guanylate kinase-associated protein, a postsynaptic density protein at excitatory synapses that interacts directly with postsynaptic density-95/synapse-associated protein 90
    • S. Naisbitt, E. Kim, R.J. Weinberg, A. Rao, F.C. Yang, A.M. Craig, and M. Sheng Characterization of guanylate kinase-associated protein, a postsynaptic density protein at excitatory synapses that interacts directly with postsynaptic density-95/synapse-associated protein 90 J. Neurosci. 17 1997 5687 5696
    • (1997) J. Neurosci. , vol.17 , pp. 5687-5696
    • Naisbitt, S.1    Kim, E.2    Weinberg, R.J.3    Rao, A.4    Yang, F.C.5    Craig, A.M.6    Sheng, M.7
  • 2
    • 34548436564 scopus 로고    scopus 로고
    • The postsynaptic architecture of excitatory synapses: A more quantitative view
    • M. Sheng, and C.C. Hoogenraad The postsynaptic architecture of excitatory synapses: a more quantitative view Annu. Rev. Biochem. 76 2007 823 847
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 823-847
    • Sheng, M.1    Hoogenraad, C.C.2
  • 3
    • 0031052970 scopus 로고    scopus 로고
    • GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/SAP90 family of channel clustering molecules
    • E. Kim, S. Naisbitt, Y.P. Hsueh, A. Rao, A. Rothschild, A.M. Craig, and M. Sheng GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/SAP90 family of channel clustering molecules J. Cell Biol. 136 1997 669 678
    • (1997) J. Cell Biol. , vol.136 , pp. 669-678
    • Kim, E.1    Naisbitt, S.2    Hsueh, Y.P.3    Rao, A.4    Rothschild, A.5    Craig, A.M.6    Sheng, M.7
  • 4
    • 0032516885 scopus 로고    scopus 로고
    • A novel multiple PDZ domain-containing molecule interacting with N-methyl-d-aspartate receptors and neuronal cell adhesion proteins
    • K. Hirao, Y. Hata, N. Ide, M. Takeuchi, M. Irie, I. Yao, M. Deguchi, A. Toyoda, T.C. Sudhof, and Y. Takai A novel multiple PDZ domain-containing molecule interacting with N-methyl-d-aspartate receptors and neuronal cell adhesion proteins J. Biol. Chem. 273 1998 21105 21110
    • (1998) J. Biol. Chem. , vol.273 , pp. 21105-21110
    • Hirao, K.1    Hata, Y.2    Ide, N.3    Takeuchi, M.4    Irie, M.5    Yao, I.6    Deguchi, M.7    Toyoda, A.8    Sudhof, T.C.9    Takai, Y.10
  • 5
    • 0033165926 scopus 로고    scopus 로고
    • Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin
    • S. Naisbitt, E. Kim, J.C. Tu, B. Xiao, C. Sala, J. Valtschanoff, R.J. Weinberg, P.F. Worley, and M. Sheng Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin Neuron 23 1999 569 582
    • (1999) Neuron , vol.23 , pp. 569-582
    • Naisbitt, S.1    Kim, E.2    Tu, J.C.3    Xiao, B.4    Sala, C.5    Valtschanoff, J.6    Weinberg, R.J.7    Worley, P.F.8    Sheng, M.9
  • 6
    • 0034660288 scopus 로고    scopus 로고
    • Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein
    • S. Naisbitt, J. Valtschanoff, D.W. Allison, C. Sala, E. Kim, A.M. Craig, R.J. Weinberg, and M. Sheng Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein J. Neurosci. 20 2000 4524 4534
    • (2000) J. Neurosci. , vol.20 , pp. 4524-4534
    • Naisbitt, S.1    Valtschanoff, J.2    Allison, D.W.3    Sala, C.4    Kim, E.5    Craig, A.M.6    Weinberg, R.J.7    Sheng, M.8
  • 7
    • 78049499222 scopus 로고    scopus 로고
    • Dlg1 binds GKAP to control dynein association with microtubules, centrosome positioning, and cell polarity
    • J.B. Manneville, M. Jehanno, and S. Etienne-Manneville Dlg1 binds GKAP to control dynein association with microtubules, centrosome positioning, and cell polarity J. Cell Biol. 191 2010 585 598
    • (2010) J. Cell Biol. , vol.191 , pp. 585-598
    • Manneville, J.B.1    Jehanno, M.2    Etienne-Manneville, S.3
  • 9
    • 78149460672 scopus 로고    scopus 로고
    • Degradation of postsynaptic scaffold GKAP and regulation of dendritic spine morphology by the TRIM3 ubiquitin ligase in rat hippocampal neurons
    • A.Y. Hung, C.C. Sung, I.L. Brito, and M. Sheng Degradation of postsynaptic scaffold GKAP and regulation of dendritic spine morphology by the TRIM3 ubiquitin ligase in rat hippocampal neurons PLoS One 5 2010 e9842
    • (2010) PLoS One , vol.5 , pp. 9842
    • Hung, A.Y.1    Sung, C.C.2    Brito, I.L.3    Sheng, M.4
  • 10
    • 84870494059 scopus 로고    scopus 로고
    • GKAP orchestrates activity-dependent postsynaptic protein remodeling and homeostatic scaling
    • S.M. Shin, N. Zhang, J. Hansen, N.Z. Gerges, D.T. Pak, M. Sheng, and S.H. Lee GKAP orchestrates activity-dependent postsynaptic protein remodeling and homeostatic scaling Nat. Neurosci. 15 2012 1655 1666
    • (2012) Nat. Neurosci. , vol.15 , pp. 1655-1666
    • Shin, S.M.1    Zhang, N.2    Hansen, J.3    Gerges, N.Z.4    Pak, D.T.5    Sheng, M.6    Lee, S.H.7
  • 11
    • 84905514204 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of the C-terminal domain of guanylate kinase-associated protein from Rattus norvegicus
    • J. Tong, H. Yang, and Y.J. Im Crystallization and preliminary X-ray crystallographic analysis of the C-terminal domain of guanylate kinase-associated protein from Rattus norvegicus Acta Crystallogr. F Struct. Biol. Commun. 70 2014 949 954
    • (2014) Acta Crystallogr. F Struct. Biol. Commun. , vol.70 , pp. 949-954
    • Tong, J.1    Yang, H.2    Im, Y.J.3
  • 14
    • 0026493924 scopus 로고
    • Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis
    • A.J. Sharff, L.E. Rodseth, J.C. Spurlino, and F.A. Quiocho Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis Biochemistry 31 1992 10657 10663
    • (1992) Biochemistry , vol.31 , pp. 10657-10663
    • Sharff, A.J.1    Rodseth, L.E.2    Spurlino, J.C.3    Quiocho, F.A.4
  • 17
    • 0036118284 scopus 로고    scopus 로고
    • The structural basis of localization and signaling by the focal adhesion targeting domain
    • S.T. Arold, M.K. Hoellerer, and M.E. Noble The structural basis of localization and signaling by the focal adhesion targeting domain Structure 10 2002 319 327
    • (2002) Structure , vol.10 , pp. 319-327
    • Arold, S.T.1    Hoellerer, M.K.2    Noble, M.E.3
  • 19
    • 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
    • Y.J. Im, J.H. Lee, S.H. Park, S.J. Park, S.H. Rho, G.B. Kang, E. Kim, and S.H. Eom Crystal structure of the Shank PDZ-ligand complex reveals a class I PDZ interaction and a novel PDZ-PDZ dimerization J. Biol. Chem. 278 2003 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.