메뉴 건너뛰기




Volumn 289, Issue 20, 2014, Pages 14121-14131

Periaxin and AHNAK nucleoprotein 2 form intertwined homodimers through domain swapping

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEX NETWORKS; DIMERIZATION; NUCLEIC ACIDS; PEPTIDES;

EID: 84901020085     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.554816     Document Type: Article
Times cited : (26)

References (61)
  • 1
    • 84864615365 scopus 로고    scopus 로고
    • Plasticity of PDZ domains in ligand recognition and signaling
    • Ivarsson, Y. (2012) Plasticity of PDZ domains in ligand recognition and signaling. FEBS Lett. 586, 2638-2647
    • (2012) FEBS Lett. , vol.586 , pp. 2638-2647
    • Ivarsson, Y.1
  • 2
    • 77952705907 scopus 로고    scopus 로고
    • PDZ domains and their binding partners: Structure, specificity, and modification
    • Lee, H. J., and Zheng, J. J. (2010) PDZ domains and their binding partners: structure, specificity, and modification. Cell Commun. Signal. 8, 8
    • (2010) Cell Commun. Signal , vol.8 , pp. 8
    • Lee, H.J.1    Zheng, J.J.2
  • 3
    • 0012927828 scopus 로고    scopus 로고
    • PDZ domain proteins: Plug and play
    • Nourry, C., Grant, S. G., and Borg, J. P. (2003) PDZ domain proteins: plug and play Sci. STKE 2003, RE7
    • (2003) Sci. STKE , vol.2003
    • Nourry, C.1    Grant, S.G.2    Borg, J.P.3
  • 4
    • 77954044144 scopus 로고    scopus 로고
    • Interaction prediction and classification of PDZ domains
    • Kalyoncu, S., Keskin, O., and Gursoy, A. (2010) Interaction prediction and classification of PDZ domains. BMC Bioinformatics 11, 357
    • (2010) BMC Bioinformatics , vol.11 , pp. 357
    • Kalyoncu, S.1    Keskin, O.2    Gursoy, A.3
  • 5
    • 0028204901 scopus 로고
    • Periaxin, a novel protein of myelinating Schwann cells with a possible role in axonal ensheathment
    • DOI 10.1016/0896-6273(94)90208-9
    • Gillespie, C. S., Sherman, D. L., Blair, G. E., and Brophy, P. J. (1994) Periaxin, a novel protein of myelinating Schwann cells with a possible role in axonal ensheathment. Neuron 12, 497-508 (Pubitemid 24100883)
    • (1994) Neuron , vol.12 , Issue.3 , pp. 497-508
    • Gillespie, C.S.1    Sherman, D.L.2    Blair, G.E.3    Brophy, P.J.4
  • 6
    • 0029615322 scopus 로고
    • Periaxin expression in myelinating Schwann cells: Modulation by axon-glial interactions and polarized localization during development
    • Scherer, S. S., Xu, Y. T., Bannerman, P. G., Sherman, D. L., and Brophy, P. J. (1995) Periaxin expression in myelinating Schwann cells: modulation by axon-glial interactions and polarized localization during development. Development 121, 4265-4273 (Pubitemid 26007377)
    • (1995) Development , vol.121 , Issue.12 , pp. 4265-4273
    • Scherer, S.S.1    Xu, Y.-T.2    Bannerman, P.G.C.3    Sherman, D.L.4    Brophy, P.J.5
  • 11
    • 80051474267 scopus 로고    scopus 로고
    • Periaxin is required for hexagonal geometry and membrane organization of mature lens fibers
    • Maddala, R., Skiba, N. P., Lalane, R., 3rd., Sherman, D. L., Brophy, P. J., and Rao, P. V. (2011) Periaxin is required for hexagonal geometry and membrane organization of mature lens fibers. Dev. Biol. 357, 179-190
    • (2011) Dev. Biol , vol.357 , pp. 179-190
    • Maddala, R.1    Skiba, N.P.2    Lalane III, R.3    Sherman, D.L.4    Brophy, P.J.5    Rao, P.V.6
  • 13
    • 0032489463 scopus 로고    scopus 로고
    • Two PDZ domain proteins encoded by the murine periaxin gene are the result of alternative intron retention and are differentially targeted in Schwann cells
    • Dytrych, L., Sherman, D. L., Gillespie, C. S., and Brophy, P. J. (1998) Two PDZ domain proteins encoded by the murine periaxin gene are the result of alternative intron retention and are differentially targeted in Schwann cells. J. Biol. Chem. 273, 5794-5800
    • (1998) J. Biol. Chem , vol.273 , pp. 5794-5800
    • Dytrych, L.1    Sherman, D.L.2    Gillespie, C.S.3    Brophy, P.J.4
  • 14
    • 0034968820 scopus 로고    scopus 로고
    • Specific disruption of a Schwann cell dystrophin-related protein complex in a demyelinating neuropathy
    • DOI 10.1016/S0896-6273(01)00327-0
    • Sherman, D. L., Fabrizi, C., Gillespie, C. S., and Brophy, P. J. (2001) Specific disruption of a schwann cell dystrophin-related protein complex in a demyelinating neuropathy. Neuron 30, 677-687 (Pubitemid 32607333)
    • (2001) Neuron , vol.30 , Issue.3 , pp. 677-687
    • Sherman, D.L.1    Fabrizi, C.2    Gillespie C.Stewart3    Brophy, P.J.4
  • 15
    • 84879420924 scopus 로고    scopus 로고
    • Myelin-specific proteins: A structurally diverse group of membrane-interacting molecules
    • Han, H., Myllykoski, M., Ruskamo, S., Wang, C., and Kursula, P. (2013) Myelin-specific proteins: a structurally diverse group of membrane-interacting molecules. Biofactors 39, 233-241
    • (2013) Biofactors , vol.39 , pp. 233-241
    • Han, H.1    Myllykoski, M.2    Ruskamo, S.3    Wang, C.4    Kursula, P.5
  • 16
    • 0026647930 scopus 로고
    • A human gene (AHNAK) encoding an unusually large protein with a 1.2-microns polyionic rod structure
    • Shtivelman, E., Cohen, F. E., and Bishop, J. M. (1992) A human gene (AHNAK) encoding an unusually large protein with a 1.2-microns polyionic rod structure. Proc. Natl. Acad. Sci. U.S.A. 89, 5472-5476
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 5472-5476
    • Shtivelman, E.1    Cohen, F.E.2    Bishop, J.M.3
  • 17
    • 0035968275 scopus 로고    scopus 로고
    • The giant proteinAHNAKis a specific target for the calcium- and zinc-binding S100B protein: Potential implications for Ca2+ homeostasis regulation by S100B
    • Gentil, B. J., Delphin, C., Mbele, G. O., Deloulme, J. C., Ferro, M., Garin, J., and Baudier, J. (2001) The giant proteinAHNAKis a specific target for the calcium- and zinc-binding S100B protein: potential implications for Ca2+ homeostasis regulation by S100B. J. Biol. Chem. 276, 23253-23261
    • (2001) J. Biol. Chem , vol.276 , pp. 23253-23261
    • Gentil, B.J.1    Delphin, C.2    Mbele, G.O.3    Deloulme, J.C.4    Ferro, M.5    Garin, J.6    Baudier, J.7
  • 21
    • 77957684891 scopus 로고    scopus 로고
    • AHNAK1 and AHNAK2 are costameric proteins: AHNAK1 affects transverse skeletal muscle fiber stiffness
    • Marg, A., Haase, H., Neumann, T., Kouno, M., and Morano, I. (2010) AHNAK1 and AHNAK2 are costameric proteins: AHNAK1 affects transverse skeletal muscle fiber stiffness. Biochem. Biophys. Res. Commun. 401, 143-148
    • (2010) Biochem. Biophys. Res. Commun , vol.401 , pp. 143-148
    • Marg, A.1    Haase, H.2    Neumann, T.3    Kouno, M.4    Morano, I.5
  • 22
    • 84880096639 scopus 로고    scopus 로고
    • Preliminary crystallographic analysis of the N-terminal PDZ-like domain of periaxin, an abundant peripheral nerve protein linked to human neuropathies
    • Han, H., and Kursula, P. (2013) Preliminary crystallographic analysis of the N-terminal PDZ-like domain of periaxin, an abundant peripheral nerve protein linked to human neuropathies. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 69, 804-808
    • (2013) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.69 , pp. 804-808
    • Han, H.1    Kursula, P.2
  • 23
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier, F. W. (2005) Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif. 41, 207-234
    • (2005) Protein Expr. Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 24
    • 33645214738 scopus 로고    scopus 로고
    • ATSAS 2.1, a program package for small-angle scattering data analysis
    • Konarev, P. V., Petoukhov, M. V., Volkov, V. V., and Svergun, D. I. (2006) ATSAS 2.1, a program package for small-angle scattering data analysis. J. Appl. Crystallogr. 39, 277-286
    • (2006) J. Appl. Crystallogr , vol.39 , pp. 277-286
    • Konarev, P.V.1    Petoukhov, M.V.2    Volkov, V.V.3    Svergun, D.I.4
  • 26
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • DOI 10.1107/S0021889892001663
    • Svergun, D. I. (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25, 495-503 (Pubitemid 23564996)
    • (1992) Journal of Applied Crystallography , vol.25 , Issue.PART 4 , pp. 495-503
    • Svergun, D.I.1
  • 27
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun, D. I. (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76, 2879-2886 (Pubitemid 29269438)
    • (1999) Biophysical Journal , vol.76 , Issue.6 , pp. 2879-2886
    • Svergun, D.I.1
  • 28
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab initio shape determination in small-angle scattering
    • Franke, D., and Svergun, D. I. (2009) DAMMIF, a program for rapid ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 42, 342-346
    • (2009) J. Appl. Crystallogr , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 29
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from x-ray solution scattering
    • Svergun, D. I., Petoukhov, M. V., and Koch, M. H. (2001) Determination of domain structure of proteins from x-ray solution scattering. Biophys. J. 80, 2946-2953 (Pubitemid 32521666)
    • (2001) Biophysical Journal , vol.80 , Issue.6 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.J.3
  • 30
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • DOI 10.1529/biophysj.105.064154
    • Petoukhov, M. V., and Svergun, D. I. (2005) Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys. J. 89, 1237-1250 (Pubitemid 41099005)
    • (2005) Biophysical Journal , vol.89 , Issue.2 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 31
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • DOI 10.1107/S0021889800014126
    • Kozin, M. B., and Svergun, D. I. (2001) Automated matching of high- and low-resolution structural models. J. Appl. Crystallogr. 34, 33-41 (Pubitemid 32151714)
    • (2001) Journal of Applied Crystallography , vol.34 , Issue.1 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 32
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • DOI 10.1107/S0021889895007047
    • Svergun, D., Barberato, C., and Koch, M. H. J. (1995) CRYSOL-a program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28, 768-773 (Pubitemid 3014671)
    • (1995) Journal of Applied Crystallography , vol.28 , Issue.6 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.3
  • 33
    • 76449099287 scopus 로고    scopus 로고
    • XDS. Acta crystallogr
    • Kabsch, W. (2010) XDS. Acta Crystallogr. D Biol. Crystallogr. 66, 125-132
    • (2010) D Biol. Crystallogr , vol.66 , pp. 125-132
    • Kabsch, W.1
  • 39
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore, L., and Wallace, B. A. (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32, W668-73
    • (2004) Nucleic Acids Res , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 40
    • 38049178969 scopus 로고    scopus 로고
    • Domain swapping within PDZ2 is responsible for dimerization of ZO proteins
    • Fanning, A. S., Lye, M. F., Anderson, J. M., and Lavie, A. (2007) Domain swapping within PDZ2 is responsible for dimerization of ZO proteins. J. Biol. Chem. 282, 37710-37716
    • (2007) J. Biol. Chem , vol.282 , pp. 37710-37716
    • Fanning, A.S.1    Lye, M.F.2    Anderson, J.M.3    Lavie, A.4
  • 41
    • 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
    • DOI 10.1074/jbc.M212263200
    • Im, Y. J., Park, S. H., Rho, S. H., Lee, J. H., Kang, G. B., Sheng, M., Kim, E., and Eom, S. H. (2003) 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 (Pubitemid 36800602)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.10 , 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
  • 42
    • 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
    • DOI 10.1074/jbc.M306919200
    • Im, Y. J., Lee, J. H., Park, S. H., Park, S. J., Rho, S. H., Kang, G. B., Kim, E., and Eom, S. H. (2003) 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 (Pubitemid 37523261)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.48 , 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
  • 43
    • 0034916230 scopus 로고    scopus 로고
    • PDZ domains and the organization of supramolecular complexes
    • DOI 10.1146/annurev.neuro.24.1.1
    • Sheng, M., and Sala, C. (2001) PDZ domains and the organization of supramolecular complexes. Annu. Rev. Neurosci. 24, 1-29 (Pubitemid 32695221)
    • (2001) Annual Review of Neuroscience , vol.24 , pp. 1-29
    • Sheng, M.1    Sala, C.2
  • 44
    • 72449188596 scopus 로고    scopus 로고
    • NADPH oxidase activator p67phox behaves in solution as a multidomain protein with semi-flexible linkers
    • Durand, D., Vivès, C., Cannella, D., Pérez, J., Pebay-Peyroula, E., Vachette, P., and Fieschi, F. (2010) NADPH oxidase activator p67phox behaves in solution as a multidomain protein with semi-flexible linkers. J. Struct. Biol. 169, 45-53
    • (2010) J. Struct. Biol , vol.169 , pp. 45-53
    • Durand, D.1    Vivès, C.2    Cannella, D.3    Pérez, J.4    Pebay-Peyroula, E.5    Vachette, P.6    Fieschi, F.7
  • 45
    • 0035512216 scopus 로고    scopus 로고
    • The current status of structural studies on proteins of the myelin sheath (review)
    • Kursula, P. (2001) The current status of structural studies on proteins of the myelin sheath (review). Int. J. Mol. Med. 8, 475-479
    • (2001) Int. J. Mol. Med , vol.8 , pp. 475-479
    • Kursula, P.1
  • 46
    • 39049155236 scopus 로고    scopus 로고
    • Structural properties of proteins specific to the myelin sheath
    • DOI 10.1007/s00726-006-0479-7
    • Kursula, P. (2008) Structural properties of proteins specific to the myelin sheath. Amino Acids 34, 175-185 (Pubitemid 351238256)
    • (2008) Amino Acids , vol.34 , Issue.2 , pp. 175-185
    • Kursula, P.1
  • 48
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: As domains continue to swap
    • DOI 10.1110/ps.0201402
    • Liu, Y., and Eisenberg, D. (2002) 3D domain swapping: as domains continue to swap. Protein Sci. 11, 1285-1299 (Pubitemid 34547201)
    • (2002) Protein Science , vol.11 , Issue.6 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 49
    • 0030067028 scopus 로고    scopus 로고
    • High-resolution structure of an engineered Cro monomer shows changes in conformation relative to the native dimer
    • DOI 10.1021/bi951958n
    • Albright, R. A., Mossing, M. C., and Matthews, B. W. (1996) High-resolution structure of an engineered Cro monomer shows changes in conformation relative to the native dimer. Biochemistry 35, 735-742 (Pubitemid 26034557)
    • (1996) Biochemistry , vol.35 , Issue.3 , pp. 735-742
    • Albright, R.A.1    Mossing, M.C.2    Matthews, B.W.3
  • 51
    • 24344436818 scopus 로고    scopus 로고
    • NF-κBA;B RelB forms an intertwined homodimer
    • DOI 10.1016/j.str.2005.06.018, PII S0969212605002790
    • Huang, D. B., Vu, D., and Ghosh, G. (2005) NF-κB RelB forms an intertwined homodimer. Structure 13, 1365-1373 (Pubitemid 41262103)
    • (2005) Structure , vol.13 , Issue.9 , pp. 1365-1373
    • Huang, D.-B.1    Vu, D.2    Ghosh, G.3
  • 52
    • 0033617473 scopus 로고    scopus 로고
    • Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex
    • DOI 10.1126/science.284.5415.812
    • Hillier, B. J., Christopherson, K. S., Prehoda, K. E., Bredt, D. S., and Lim, W. A. (1999) Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex. Science 284, 812-815 (Pubitemid 29291348)
    • (1999) Science , vol.284 , Issue.5415 , pp. 812-815
    • Hillier, B.J.1    Christopherson, K.S.2    Prehoda, K.E.3    Bredt, D.S.4    Lim, W.A.5
  • 53
    • 7544232779 scopus 로고    scopus 로고
    • Internal recognition through PDZ domain plasticity in the Par-6-Pals1 complex
    • DOI 10.1038/nsmb839
    • Penkert, R. R., DiVittorio, H. M., and Prehoda, K. E. (2004) Internal recognition through PDZ domain plasticity in the Par-6-Pals1 complex. Nat. Struct. Mol. Biol. 11, 1122-1127 (Pubitemid 39453342)
    • (2004) Nature Structural and Molecular Biology , vol.11 , Issue.11 , pp. 1122-1127
    • Penkert, R.R.1    Divittorio, H.M.2    Prehoda, K.E.3
  • 57
  • 58
    • 83355174042 scopus 로고    scopus 로고
    • The Src homology 3 domain is required for junctional adhesion molecule binding to the third PDZ domain of the scaffolding protein ZO-1
    • Nomme, J., Fanning, A. S., Caffrey, M., Lye, M. F., Anderson, J. M., and Lavie, A. (2011) The Src homology 3 domain is required for junctional adhesion molecule binding to the third PDZ domain of the scaffolding protein ZO-1. J. Biol. Chem. 286, 43352-43360
    • (2011) J. Biol. Chem , vol.286 , pp. 43352-43360
    • Nomme, J.1    Fanning, A.S.2    Caffrey, M.3    Lye, M.F.4    Anderson, J.M.5    Lavie, A.6
  • 59
    • 1642276423 scopus 로고    scopus 로고
    • Cdc42 regulates the Par-6 PDZ domain through an allosteric CRIB-PDZ transition
    • DOI 10.1016/S1097-2765(04)00086-3, PII S1097276504000863
    • Peterson, F. C., Penkert, R. R., Volkman, B. F., and Prehoda, K. E. (2004) Cdc42 regulates the Par-6 PDZ domain through an allosteric CRIB-PDZ transition. Mol. Cell 13, 665-676 (Pubitemid 38368124)
    • (2004) Molecular Cell , vol.13 , Issue.5 , pp. 665-676
    • Peterson, F.C.1    Penkert, R.R.2    Volkman, B.F.3    Prehoda, K.E.4
  • 60
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • DOI 10.1093/bioinformatics/15.4.305
    • Gouet, P., Courcelle, E., Stuart, D. I., and Métoz, F. (1999) ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15, 305-308 (Pubitemid 29213756)
    • (1999) Bioinformatics , vol.15 , Issue.4 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 61


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.