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Volumn 113, Issue 22, 2009, Pages 5385-5393

Structures of the spectrin-ankyrin interaction binding domains

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; SPECTRIN;

EID: 62549129569     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2008-10-184358     Document Type: Article
Times cited : (80)

References (49)
  • 1
    • 0028263839 scopus 로고
    • Mechanical properties of the red cell membrane in relation to molecular structure and genetic defects
    • Mohandas N, Evans E. Mechanical properties of the red cell membrane in relation to molecular structure and genetic defects. Annu Rev Biophys Biomol Struct. 1994;23:787-818. (Pubitemid 24217386)
    • (1994) Annual Review of Biophysics and Biomolecular Structure , vol.23 , pp. 787-818
    • Mohandas, N.1    Evans, E.2
  • 2
    • 0032907043 scopus 로고    scopus 로고
    • Red blood cell membrane disorders
    • DOI 10.1111/j.1365-2141.1999.01130.x
    • Tse WT, Lux SE. Red blood cell membrane disorders. Br J Haematol. 1999;104:2-13. (Pubitemid 29037011)
    • (1999) British Journal of Haematology , vol.104 , Issue.1 , pp. 2-13
    • Tse, W.T.1    Lux, S.E.2
  • 3
    • 0037062586 scopus 로고    scopus 로고
    • Functional characterization of spectrin-actin-binding domains in 4.1 family of proteins
    • Gimm JA, An X, Nunomura W, Mohandas N. Functional characterization of spectrin-actin-binding domains in 4.1 family of proteins. Biochemistry. 2002;41:7275-7282.
    • (2002) Biochemistry , vol.41 , pp. 7275-7282
    • Gimm, J.A.1    An, X.2    Nunomura, W.3    Mohandas, N.4
  • 4
    • 0026806912 scopus 로고
    • Ankyrins. Adaptors between diverse plasma membrane proteins and the cytoplasm
    • Bennett V. Ankyrins. Adaptors between diverse plasma membrane proteins and the cytoplasm. J Biol Chem. 1992;267:8703-8706.
    • (1992) J Biol Chem , vol.267 , pp. 8703-8706
    • Bennett, V.1
  • 5
    • 0035933904 scopus 로고    scopus 로고
    • Regulation of the Glycophorin C-Protein 4.1 Membrane-to-Skeleton Bridge and Evaluation of Its Contribution to Erythrocyte Membrane Stability
    • DOI 10.1074/jbc.M100604200
    • Chang SH, Low PS. Regulation of the glycophorin C-protein 4.1 membrane-to-skeleton bridge and evaluation of its contribution to erythrocyte membrane stability. J Biol Chem. 2001;276:22223-22230. (Pubitemid 37410891)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.25 , pp. 22223-22230
    • Chang, S.H.1    Low, P.S.2
  • 6
    • 0021272595 scopus 로고
    • Erythrocyte spectrin is comprised of many homologous triple helical segments
    • Speicher DW, Marchesi VT. Erythrocyte spectrin is comprised of many homologous triple helical segments. Nature. 1984;311:177-180.
    • (1984) Nature , vol.311 , pp. 177-180
    • Speicher, D.W.1    Marchesi, V.T.2
  • 7
    • 0037138385 scopus 로고    scopus 로고
    • The spectrin repeat: A structural platform for cytoskeletal protein assemblies
    • DOI 10.1016/S0014-5793(01)03304-X, PII S001457930103304X
    • Djinovic-Carugo K, Gautel M, Ylanne J, Young P. The spectrin repeat: a structural platform for cytoskeletal protein assemblies. FEBS Lett. 2002;513:119-123. (Pubitemid 34242988)
    • (2002) FEBS Letters , vol.513 , Issue.1 , pp. 119-123
    • Djinovic-Carugo, K.1    Gautel, M.2    Ylanne, J.3    Young, P.4
  • 8
    • 33846332690 scopus 로고    scopus 로고
    • Structural Analysis of the Plakin Domain of Bullous Pemphigoid Antigen1 (BPAG1) Suggests that Plakins Are Members of the Spectrin Superfamily
    • DOI 10.1016/j.jmb.2006.11.036, PII S0022283606015762
    • Jefferson JJ, Ciatto C, Shapiro L, Liem RK. Structural analysis of the plakin domain of bullous pemphigoid antigen1 (BPAG1) suggests that plakins are members of the spectrin superfamily. J Mol Biol. 2007;366:244-257. (Pubitemid 46123339)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.1 , pp. 244-257
    • Jefferson, J.J.1    Ciatto, C.2    Shapiro, L.3    Liem, R.K.H.4
  • 9
    • 34247222123 scopus 로고    scopus 로고
    • The Structure of a Tandem Pair of Spectrin Repeats of Plectin Reveals a Modular Organization of the Plakin Domain
    • DOI 10.1016/j.jmb.2007.02.090, PII S0022283607003087
    • Sonnenberg A, Rojas AM, de Pereda JM. The structure of a tandem pair of spectrin repeats of plectin reveals a modular organization of the plakin domain. J Mol Biol. 2007;368:1379-1391. (Pubitemid 46617599)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.5 , pp. 1379-1391
    • Sonnenberg, A.1    Rojas, A.M.2    De Pereda, J.M.3
  • 10
    • 0037623278 scopus 로고    scopus 로고
    • Comprehensive analysis of all triple helical repeats in beta-spectrins reveals patterns of selective evolutionary conservation
    • Baines AJ. Comprehensive analysis of all triple helical repeats in beta-spectrins reveals patterns of selective evolutionary conservation. Cell Mol Biol Lett. 2003;8:195-214.
    • (2003) Cell Mol Biol Lett , vol.8 , pp. 195-214
    • Baines, A.J.1
  • 11
    • 17444415361 scopus 로고    scopus 로고
    • Spectrin, alpha-actinin, and dystrophin
    • Broderick MJ, Winder SJ. Spectrin, alpha-actinin, and dystrophin. Adv Protein Chem. 2005;70:203-246.
    • (2005) Adv Protein Chem , vol.70 , pp. 203-246
    • Broderick, M.J.1    Winder, S.J.2
  • 12
    • 0026754234 scopus 로고
    • The complete sequence of Drosophila beta-spectrin reveals supra-motifs comprising eight 106-residue segments
    • Byers TJ, Brandin E, Lue RA, Winograd E, Branton D. The complete sequence of Drosophila beta-spectrin reveals supra-motifs comprising eight 106-residue segments. Proc Natl Acad Sci U S A. 1992;89:6187-6191.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 6187-6191
    • Byers, T.J.1    Brandin, E.2    Lue, R.A.3    Winograd, E.4    Branton, D.5
  • 13
    • 0033588277 scopus 로고    scopus 로고
    • Structure of the alpha-actinin rod: Molecular basis for cross-linking of actin filaments
    • DOI 10.1016/S0092-8674(00)81981-9
    • Djinović-Carugo K, Young P, Gautel M, Saraste M. Molecular basis for cross-linking of actin filaments: structure of the alpha-actinin rod. Cell. 1999;98:537-546. (Pubitemid 29402490)
    • (1999) Cell , vol.98 , Issue.4 , pp. 537-546
    • Djinovic-Carugo, K.1    Young, P.2    Gautel, M.3    Saraste, M.4
  • 14
    • 0033588274 scopus 로고    scopus 로고
    • Structures of two repeats of spectrin suggest models of flexibility
    • DOI 10.1016/S0092-8674(00)81980-7
    • Grum VL, Li D, MacDonald RI, Mondragón A. Structures of two repeats of spectrin suggest models of flexibility. Cell. 1999;98:523-535. (Pubitemid 29402489)
    • (1999) Cell , vol.98 , Issue.4 , pp. 523-535
    • Grum, V.L.1    Li, D.2    MacDonald, R.I.3    Mondragon, A.4
  • 15
    • 1842450320 scopus 로고    scopus 로고
    • Structural insights into the stability and flexibility of unusual erythroid spectrin repeats
    • DOI 10.1016/j.str.2004.02.022, PII S0969212604000644
    • Kusunoki H, MacDonald RI, Mondragón A. Structural insights into the stability and flexibility of unusual erythroid spectrin repeats. Structure. 2004;12:645-656. (Pubitemid 38447167)
    • (2004) Structure , vol.12 , Issue.4 , pp. 645-656
    • Kusunoki, H.1    MacDonald, R.I.2    Mondragon, A.3
  • 16
    • 7444232111 scopus 로고    scopus 로고
    • Independent movement, dimerization and stability of tandem repeats of chicken brain alpha-spectrin
    • DOI 10.1016/j.jmb.2004.09.019, PII S0022283604011489
    • Kusunoki H, Minasov G, MacDonald RI, Mondragón A. Independent movement, dimerization and stability of tandem repeats of chicken brain alpha-spectrin. J Mol Biol. 2004;344:495-511. (Pubitemid 39441220)
    • (2004) Journal of Molecular Biology , vol.344 , Issue.2 , pp. 495-511
    • Kusunoki, H.1    Minasov, G.2    MacDonald, R.I.3    Mondragon, A.4
  • 17
    • 0034933167 scopus 로고    scopus 로고
    • Crystal structure of the alpha-actinin rod reveals an extensive torsional twist
    • DOI 10.1016/S0969-2126(01)00619-0, PII S0969212601006190
    • Ylänne J, Scheffzek K, Young P, Saraste M. Crystal structure of the alpha-actinin rod reveals an extensive torsional twist. Structure. 2001;9:597-604. (Pubitemid 32695584)
    • (2001) Structure , vol.9 , Issue.7 , pp. 597-604
    • Ylänne, J.1    Scheffzek, K.2    Young, P.3    Saraste, M.4
  • 18
    • 0028985712 scopus 로고
    • A new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier
    • Kordeli E, Lambert S, Bennett V. Ankyrin G: a new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier. J Biol Chem. 1995;270:2352-2359.
    • (1995) J Biol Chem , vol.270 , pp. 2352-2359
    • Kordeli, E.1    Lambert, S.2    Bennett, V.3    Ankyrin, G.4
  • 19
    • 0023196746 scopus 로고
    • Regulatory domains of erythrocyte ankyrin
    • Hall TG, Bennett V. Regulatory domains of erythrocyte ankyrin. J Biol Chem. 1987;262:10537-10545.
    • (1987) J Biol Chem , vol.262 , pp. 10537-10545
    • Hall, T.G.1    Bennett, V.2
  • 20
    • 33744902323 scopus 로고    scopus 로고
    • Cardiac ankyrins: Essential components for development and maintenance of excitable membrane domains in heart
    • Cunha SR, Mohler PJ. Cardiac ankyrins: essential components for development and maintenance of excitable membrane domains in heart. Cardiovasc Res. 2006;71:22-29.
    • (2006) Cardiovasc Res , vol.71 , pp. 22-29
    • Cunha, S.R.1    Mohler, P.J.2
  • 21
    • 0037011104 scopus 로고    scopus 로고
    • Crystal structure of a 12 ANK repeat stack from human ankyrinR
    • DOI 10.1093/emboj/cdf651
    • Michaely P, Tomchick DR, Machius M, Anderson RG. Crystal structure of a 12 ANK repeat stack from human ankyrinR. EMBO J. 2002;21:6387-6396. (Pubitemid 35448417)
    • (2002) EMBO Journal , vol.21 , Issue.23 , pp. 6387-6396
    • Michaely, P.1    Tomchick, D.R.2    Machius, M.3    Anderson, R.G.W.4
  • 23
    • 2442706456 scopus 로고    scopus 로고
    • The ankyrin repeat as molecular architecture for protein recognition
    • DOI 10.1110/ps.03554604
    • Mosavi LK, Cammett TJ, Desrosiers DC, Peng Z-y. The ankyrin repeat as molecular architecture for protein recognition. Protein Sci. 2004;13:1435-1448. (Pubitemid 38669232)
    • (2004) Protein Science , vol.13 , Issue.6 , pp. 1435-1448
    • Mosavi, L.K.1    Cammett, T.J.2    Desrosiers, D.C.3    Peng, Z.-Y.4
  • 25
    • 45449118896 scopus 로고    scopus 로고
    • The 22.5 kDa spectrin-binding domain of ankyrinR binds spectrin with high affinity and changes the spectrin distribution in cells in vivo
    • Kolondra A, Grzybek M, Chorzalska A, Sikorski AF. The 22.5 kDa spectrin-binding domain of ankyrinR binds spectrin with high affinity and changes the spectrin distribution in cells in vivo. Protein Expr Purif. 2008;60:157-164.
    • (2008) Protein Expr Purif , vol.60 , pp. 157-164
    • Kolondra, A.1    Grzybek, M.2    Chorzalska, A.3    Sikorski, A.F.4
  • 26
    • 4544252325 scopus 로고    scopus 로고
    • 2-spectrin to an intracellular compartment in neonatal cardiomyocytes
    • DOI 10.1074/jbc.M406018200
    • Mohler PJ, Yoon W, Bennett V. Ankyrin-B targets beta2-spectrin to an intracellular compartment in neonatal cardiomyocytes. J Biol Chem. 2004;279:40185-40193. (Pubitemid 39258294)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.38 , pp. 40185-40193
    • Mohler, P.J.1    Yoon, W.2    Bennett, V.3
  • 28
    • 0025995618 scopus 로고
    • Ankyrin binds to the 15th repetitive unit of erythroid and nonerythroid beta-spectrin
    • Kennedy SP, Warren SL, Forget BG, Morrow JS. Ankyrin binds to the 15th repetitive unit of erythroid and nonerythroid beta-spectrin. J Cell Biol. 1991;115:267-277.
    • (1991) J Cell Biol , vol.115 , pp. 267-277
    • Kennedy, S.P.1    Warren, S.L.2    Forget, B.G.3    Morrow, J.S.4
  • 29
    • 0021689392 scopus 로고
    • Brain ankyrin. a membrane-associated protein with binding sites for spectrin, tubulin, and the cytoplasmic domain of the erythrocyte anion channel
    • Davis JQ, Bennett V. Brain ankyrin: a membrane-associated protein with binding sites for spectrin, tubulin, and the cytoplasmic domain of the erythrocyte anion channel. J Biol Chem. 1984;259:13550-13559. (Pubitemid 15221833)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.21 , pp. 13550-13559
    • Davis, J.Q.1    Bennett, V.2
  • 30
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr Sect D Biol Crystallogr. 1994;50:760-763.
    • (1994) Acta Crystallogr Sect D Biol Crystallogr , vol.50 , pp. 760-763
  • 31
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Crystallogr. 1993;26:795-800.
    • (1993) J Appl Crystallogr , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 36
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams PD, Grosse-Kunstleve RW, Hung LW, et al. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr D Biol Crystallogr. 2002;58:1948-1954.
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , pp. 1948-1954
    • Adams, P.D.1    Grosse-Kunstleve, R.W.2    Hung, L.W.3
  • 39
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm L, Sander C. Mapping the protein universe. Science. 1996;273:595-603.
    • (1996) Science , vol.273 , pp. 595-603
    • Holm, L.1    Sander, C.2
  • 40
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • DOI 10.1107/S0907444904026460
    • Krissinel E, Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr. 2004;60:2256-2268. (Pubitemid 41742778)
    • (2004) Acta Crystallographica Section D: Biological Crystallography , vol.60 , Issue.12 I , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 41
    • 0034192541 scopus 로고    scopus 로고
    • Drosophila beta spectrin functions independently of alpha spectrin to polarize the Na,K ATPase in epithelial cells
    • DOI 10.1083/jcb.149.3.647
    • Dubreuil RR, Wang P, Dahl S, Lee J, Goldstein LS. Drosophila beta spectrin functions independently of alpha spectrin to polarize the Na,K ATPase in epithelial cells. J Cell Biol. 2000;149:647-656. (Pubitemid 30252398)
    • (2000) Journal of Cell Biology , vol.149 , Issue.3 , pp. 647-656
    • Dubreuil, R.R.1    Wang, P.2    Dahl, S.3    Lee, J.4    Goldstein, L.S.B.5
  • 42
    • 0036754181 scopus 로고    scopus 로고
    • The spectrin-ankyrin skeleton controls CD45 surface display and interleukin-2 production
    • DOI 10.1016/S1074-7613(02)00396-5
    • Pradhan D, Morrow JS. The spectrin-ankyrin skeleton controls CD45 surface display and interleukin-2 production. Immunity. 2002;17:303-315. (Pubitemid 35279551)
    • (2002) Immunity , vol.17 , Issue.3 , pp. 303-315
    • Pradhan, D.1    Morrow, J.S.2
  • 43
    • 0242464931 scopus 로고    scopus 로고
    • Ankyrin-B mutation causes type 4 long-QT cardiac arrhythmia and sudden cardiac death
    • Mohler PJ, Schott J-J, Gramolini AO, et al. Ankyrin-B mutation causes type 4 long-QT cardiac arrhythmia and sudden cardiac death. Nature. 2003;421:634-639.
    • (2003) Nature , vol.421 , pp. 634-639
    • Mohler, P.J.1    Schott, J.-J.2    Gramolini, A.O.3
  • 44
    • 0023030826 scopus 로고
    • Identification of ZO-1: A high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia
    • Stevenson BR, Siliciano JD, Mooseker MS, Goodenough DA. Identification of ZO-1: a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia. J Cell Biol. 1986;103:755-766.
    • (1986) J Cell Biol , vol.103 , pp. 755-766
    • Stevenson, B.R.1    Siliciano, J.D.2    Mooseker, M.S.3    Goodenough, D.A.4
  • 45
    • 0030915704 scopus 로고    scopus 로고
    • Improved R-factors for diffraction data analysis in macromolecular crystallography
    • DOI 10.1038/nsb0497-269
    • Diederichs K, Karplus PA. Improved R-factors for diffraction data analysis in macromolecular crystallography. Nat Struct Biol. 1997;4:269-275. (Pubitemid 27157198)
    • (1997) Nature Structural Biology , vol.4 , Issue.4 , pp. 269-275
    • Diederichs, K.1    Karplus, P.A.2
  • 48
    • 0032451030 scopus 로고    scopus 로고
    • Hematologically important mutations: Spectrin and ankyrin variants in hereditary spherocytosis
    • DOI 10.1006/bcmd.1998.0217
    • Gallagher PG, Forget BG. Hematologically important mutations: spectrin and ankyrin variants in hereditary spherocytosis. Blood Cells Mol Dis. 1998;24:539-543. (Pubitemid 29086936)
    • (1998) Blood Cells, Molecules, and Diseases , vol.24 , Issue.4 , pp. 539-543
    • Gallagher, P.G.1    Forget, B.G.2
  • 49
    • 33847314248 scopus 로고    scopus 로고
    • 2-spectrin collaborate in biogenesis of lateral membrane of human bronchial epithelial cells
    • DOI 10.1074/jbc.M608921200
    • Kizhatil K, Yoon W, Mohler PJ, Davis LH, Hoffman JA, Bennett V. Ankyrin-G and beta2-spectrin collaborate in biogenesis of lateral membrane of human bronchial epithelial cells. J Biol Chem. 2007;282:2029-2037. (Pubitemid 47076710)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.3 , pp. 2029-2037
    • Kizhatil, K.1    Yoon, W.2    Mohler, P.J.3    Davis, L.H.4    Hoffman, J.A.5    Bennett, V.6


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