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Volumn 67, Issue 16, 2010, Pages 2679-2683

Do we already know how spectrin attracts ankyrin?

Author keywords

Ankyrin; Membrane skeleton; Protein structure; Protein protein interactions; Spectrin

Indexed keywords

ANKYRIN; SPECTRIN;

EID: 77955717867     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-010-0371-1     Document Type: Short Survey
Times cited : (13)

References (28)
  • 1
    • 70349254604 scopus 로고    scopus 로고
    • Adducin forms a bridge between the erythrocyte membrane and its cytoskeleton and regulates membrane cohesion
    • 10.1182/blood-2009-02-203216 1:CAS:528:DC%2BD1MXhtFWgsbfF 19567882
    • WA Anong T Franco H Chu TL Weis EE Devlin DM Bodine X An N Mohandas PS Low 2009 Adducin forms a bridge between the erythrocyte membrane and its cytoskeleton and regulates membrane cohesion Blood 114 1904 1912 10.1182/blood-2009-02-203216 1:CAS:528:DC%2BD1MXhtFWgsbfF 19567882
    • (2009) Blood , vol.114 , pp. 1904-1912
    • Anong, W.A.1    Franco, T.2    Chu, H.3    Weis, T.L.4    Devlin, E.E.5    Bodine, D.M.6    An, X.7    Mohandas, N.8    Low, P.S.9
  • 2
    • 0034958883 scopus 로고    scopus 로고
    • Spectrin and ankyrin-based pathways: Metazoan inventions for integrating cells into tissues
    • 1:CAS:528:DC%2BD3MXlt1Ohsrg%3D 11427698
    • V Bennett AJ Baines 2001 Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues Physiol Rev 81 1353 1392 1:CAS:528:DC%2BD3MXlt1Ohsrg%3D 11427698
    • (2001) Physiol Rev , vol.81 , pp. 1353-1392
    • Bennett, V.1    Baines, A.J.2
  • 3
    • 0033880909 scopus 로고    scopus 로고
    • Spectrin tethers and mesh in the biosynthetic pathway
    • 1:CAS:528:DC%2BD3cXlt1Gnt78%3D
    • MA DeMatteis JS Morrow 2000 Spectrin tethers and mesh in the biosynthetic pathway J Cell Sci 113 2331 2343 1:CAS:528:DC%2BD3cXlt1Gnt78%3D
    • (2000) J Cell Sci , vol.113 , pp. 2331-2343
    • Dematteis, M.A.1    Morrow, J.S.2
  • 4
    • 38049048081 scopus 로고    scopus 로고
    • Organizing the fluid membrane bilayer: Diseases linked to spectrin and ankyrin
    • 10.1016/j.molmed.2007.11.005 1:CAS:528:DC%2BD1cXptleiug%3D%3D 18083066
    • V Bennett J Healy 2008 Organizing the fluid membrane bilayer: diseases linked to spectrin and ankyrin Trends Mol Med 14 28 36 10.1016/j.molmed.2007.11. 005 1:CAS:528:DC%2BD1cXptleiug%3D%3D 18083066
    • (2008) Trends Mol Med , vol.14 , pp. 28-36
    • Bennett, V.1    Healy, J.2
  • 5
    • 0036447290 scopus 로고    scopus 로고
    • Towards a complete atomic structure of spectrin family proteins
    • 10.1006/jsbi.2002.4465 1:CAS:528:DC%2BD38XksVygs7c%3D 12064945
    • MJF Broderick SJ Winder 2002 Towards a complete atomic structure of spectrin family proteins J Struct Biol 137 184 193 10.1006/jsbi.2002.4465 1:CAS:528:DC%2BD38XksVygs7c%3D 12064945
    • (2002) J Struct Biol , vol.137 , pp. 184-193
    • Broderick, M.J.F.1    Winder, S.J.2
  • 6
    • 7444232111 scopus 로고    scopus 로고
    • Independent movement, dimerization and stability of tandem repeats of chicken brain a-spectrin
    • 10.1016/j.jmb.2004.09.019 1:CAS:528:DC%2BD2cXptFOnsL4%3D 15522301
    • H Kusunoki G Minasov RI MacDonald A Mondragón 2004 Independent movement, dimerization and stability of tandem repeats of chicken brain a-spectrin J Mol Biol 344 495 511 10.1016/j.jmb.2004.09.019 1:CAS:528: DC%2BD2cXptFOnsL4%3D 15522301
    • (2004) J Mol Biol , vol.344 , pp. 495-511
    • Kusunoki, H.1    Minasov, G.2    MacDonald, R.I.3    Mondragón, A.4
  • 7
    • 33744512202 scopus 로고    scopus 로고
    • Conformational stabilities of the structural repeats of erythroid spectrin and their functional implications
    • 10.1074/jbc.M513725200 1:CAS:528:DC%2BD28Xjt1Knsb0%3D 16476728
    • X An X Guo X Zhang AJ Baines G Debnath D Moyo M Salomao N Bhasin C Johnson D Discher WB Gratzer N Mohandas 2006 Conformational stabilities of the structural repeats of erythroid spectrin and their functional implications J Biol Chem 281 10527 10532 10.1074/jbc.M513725200 1:CAS:528:DC%2BD28Xjt1Knsb0%3D 16476728
    • (2006) J Biol Chem , vol.281 , pp. 10527-10532
    • An, X.1    Guo, X.2    Zhang, X.3    Baines, A.J.4    Debnath, G.5    Moyo, D.6    Salomao, M.7    Bhasin, N.8    Johnson, C.9    Discher, D.10    Gratzer, W.B.11    Mohandas, N.12
  • 8
    • 0037623278 scopus 로고    scopus 로고
    • Comprehensive analysis of all triple helical repeats in beta-spectrins reveals patterns of selective evolutionary conservation
    • 1:CAS:528:DC%2BD3sXjvVegur4%3D 12655374
    • A Baines 2003 Comprehensive analysis of all triple helical repeats in beta-spectrins reveals patterns of selective evolutionary conservation Cell Mol Biol Lett 8 195 214 1:CAS:528:DC%2BD3sXjvVegur4%3D 12655374
    • (2003) Cell Mol Biol Lett , vol.8 , pp. 195-214
    • Baines, A.1
  • 9
    • 0035224375 scopus 로고    scopus 로고
    • Application of genetic semihomology algorithm to theoretical studies on various protein families
    • 1:CAS:528:DC%2BD3MXjs1Smu7o%3D 11440172
    • J Leluk B Hanus-Lorenz AF Sikorski 2001 Application of genetic semihomology algorithm to theoretical studies on various protein families Acta Biochim Pol 48 21 33 1:CAS:528:DC%2BD3MXjs1Smu7o%3D 11440172
    • (2001) Acta Biochim Pol , vol.48 , pp. 21-33
    • Leluk, J.1    Hanus-Lorenz, B.2    Sikorski, A.F.3
  • 10
    • 0037138385 scopus 로고    scopus 로고
    • The spectrin repeat: A structural platform for cytoskeletal protein assemblies
    • 10.1016/S0014-5793(01)03304-X 1:CAS:528:DC%2BD38XitFejtb0%3D 11911890
    • K Djinovic-Carugo M Gautel J Ylänne P Young 2002 The spectrin repeat: a structural platform for cytoskeletal protein assemblies FEBS Lett 513 119 123 10.1016/S0014-5793(01)03304-X 1:CAS:528:DC%2BD38XitFejtb0%3D 11911890
    • (2002) FEBS Lett , vol.513 , pp. 119-123
    • Djinovic-Carugo, K.1    Gautel, M.2    Ylänne, J.3    Young, P.4
  • 12
    • 0025995618 scopus 로고
    • Ankyrin binds to the 15th repetitive unit of erythroid and nonerythroid beta-spectrin
    • 10.1083/jcb.115.1.267 1:CAS:528:DyaK3MXmt1Kntrc%3D 1833409
    • SP Kennedy SL Warren BG Forget JS Morrow 1991 Ankyrin binds to the 15th repetitive unit of erythroid and nonerythroid beta-spectrin J Cell Biol 115 267 277 10.1083/jcb.115.1.267 1:CAS:528:DyaK3MXmt1Kntrc%3D 1833409
    • (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
  • 13
    • 47249140034 scopus 로고    scopus 로고
    • Molecular epitopes of the ankyrin-spectrin interaction
    • 10.1021/bi702525z 1:CAS:528:DC%2BD1cXntlKqs7g%3D 18563915
    • JJ Ipsaro L Huang L Gutierrez RI MacDonald 2008 Molecular epitopes of the ankyrin-spectrin interaction Biochemistry 47 7452 7464 10.1021/bi702525z 1:CAS:528:DC%2BD1cXntlKqs7g%3D 18563915
    • (2008) Biochemistry , vol.47 , pp. 7452-7464
    • Ipsaro, J.J.1    Huang, L.2    Gutierrez, L.3    MacDonald, R.I.4
  • 14
    • 4544326907 scopus 로고    scopus 로고
    • Mapping of an ankyrin-sensitive, phosphatidylethanolamine/ phosphatidylcholine mono- and bi-layer binding site in erythroid beta-spectrin
    • 10.1042/BJ20040358 1:CAS:528:DC%2BD2cXmvVOntL0%3D 15171729
    • A Hryniewicz-Jankowska E Bok P Dubielecka A Chorzalska W Diakowski A Jezierski M Lisowski AF Sikorski 2004 Mapping of an ankyrin-sensitive, phosphatidylethanolamine/phosphatidylcholine mono- and bi-layer binding site in erythroid beta-spectrin Biochem J 382 677 685 10.1042/BJ20040358 1:CAS:528:DC%2BD2cXmvVOntL0%3D 15171729
    • (2004) Biochem J , vol.382 , pp. 677-685
    • Hryniewicz-Jankowska, A.1    Bok, E.2    Dubielecka, P.3    Chorzalska, A.4    Diakowski, W.5    Jezierski, A.6    Lisowski, M.7    Sikorski, A.F.8
  • 15
    • 34249018580 scopus 로고    scopus 로고
    • Structural insight into an ankyrin-sensitive lipid-binding site of erythroid β-spectrin
    • 10.1080/09687860601102427 1:CAS:528:DC%2BD2sXls1Shu7o%3D 17520478
    • A Czogalla AR Jaszewski W Diakowski E Bok A Jezierski AF Sikorski 2007 Structural insight into an ankyrin-sensitive lipid-binding site of erythroid β-spectrin Mol Membr Biol 24 215 224 10.1080/09687860601102427 1:CAS:528:DC%2BD2sXls1Shu7o%3D 17520478
    • (2007) Mol Membr Biol , vol.24 , pp. 215-224
    • Czogalla, A.1    Jaszewski, A.R.2    Diakowski, W.3    Bok, E.4    Jezierski, A.5    Sikorski, A.F.6
  • 16
    • 0033588274 scopus 로고    scopus 로고
    • Structures of two repeats of spectrin suggest models of flexibility
    • 10.1016/S0092-8674(00)81980-7 1:CAS:528:DyaK1MXlslWmtr8%3D 10481916
    • VL Grum D Li RI MacDonald A Mondragon 1999 Structures of two repeats of spectrin suggest models of flexibility Cell 98 523 535 10.1016/S0092-8674(00) 81980-7 1:CAS:528:DyaK1MXlslWmtr8%3D 10481916
    • (1999) Cell , vol.98 , pp. 523-535
    • Grum, V.L.1    Li, D.2    MacDonald, R.I.3    Mondragon, A.4
  • 17
    • 54049121344 scopus 로고    scopus 로고
    • Phospholipid-induced structural changes to an erythroid beta spectrin ankyrin-dependent lipid-binding site
    • 10.1016/j.bbamem.2008.07.020 1:CAS:528:DC%2BD1cXht12rsb7E 18721795
    • A Czogalla K Grzymajło A Jezierski AF Sikorski 2008 Phospholipid-induced structural changes to an erythroid beta spectrin ankyrin-dependent lipid-binding site Biochim Biophys Acta 1778 2612 2620 10.1016/j.bbamem.2008.07.020 1:CAS:528:DC%2BD1cXht12rsb7E 18721795
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 2612-2620
    • Czogalla, A.1    Grzymajło, K.2    Jezierski, A.3    Sikorski, A.F.4
  • 18
    • 65449178092 scopus 로고    scopus 로고
    • Localization and structure of the ankyrin-binding site on beta2-spectrin
    • 10.1074/jbc.M809245200 1:CAS:528:DC%2BD1MXislWqsrw%3D 19098307
    • L Davis K Abdi M Machius C Brautigam DR Tomchick V Bennett P Michaely 2009 Localization and structure of the ankyrin-binding site on beta2-spectrin J Biol Chem 284 6982 6987 10.1074/jbc.M809245200 1:CAS:528:DC%2BD1MXislWqsrw%3D 19098307
    • (2009) J Biol Chem , vol.284 , pp. 6982-6987
    • Davis, L.1    Abdi, K.2    MacHius, M.3    Brautigam, C.4    Tomchick, D.R.5    Bennett, V.6    Michaely, P.7
  • 19
    • 62549129569 scopus 로고    scopus 로고
    • Structures of the spectrin-ankyrin interaction binding domains
    • 10.1182/blood-2008-10-184358 1:CAS:528:DC%2BD1MXntVertLs%3D 19141864
    • JJ Ipsaro L Huang A Mondragón 2009 Structures of the spectrin-ankyrin interaction binding domains Blood 113 5385 5393 10.1182/blood-2008-10-184358 1:CAS:528:DC%2BD1MXntVertLs%3D 19141864
    • (2009) Blood , vol.113 , pp. 5385-5393
    • Ipsaro, J.J.1    Huang, L.2    Mondragón, A.3
  • 20
    • 67049164963 scopus 로고    scopus 로고
    • The structure of the ankyrin-binding site of beta-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties
    • 10.1182/blood-2008-10-184291 1:CAS:528:DC%2BD1MXntVertLo%3D 19168783
    • PR Stabach I Simonović MA Ranieri MS Aboodi TA Steitz M Simonović JS Morrow 2009 The structure of the ankyrin-binding site of beta-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties Blood 113 5377 5384 10.1182/blood-2008-10-184291 1:CAS:528:DC%2BD1MXntVertLo%3D 19168783
    • (2009) Blood , vol.113 , pp. 5377-5384
    • Stabach, P.R.1    Simonović, I.2    Ranieri, M.A.3    Aboodi, M.S.4    Steitz, T.A.5    Simonović, M.6    Morrow, J.S.7
  • 21
    • 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
    • 10.1016/j.pep.2008.04.002 1:CAS:528:DC%2BD1cXns1ahsLY%3D 18495489
    • A Kolondra M Grzybek A Chorzalska AF Sikorski 2008 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 60 157 164 10.1016/j.pep.2008.04.002 1:CAS:528:DC%2BD1cXns1ahsLY%3D 18495489
    • (2008) Protein Expr Purif , vol.60 , pp. 157-164
    • Kolondra, A.1    Grzybek, M.2    Chorzalska, A.3    Sikorski, A.F.4
  • 22
    • 62549095266 scopus 로고    scopus 로고
    • Autoinhibition of UNC5b revealed by the cytoplasmic domain structure of the receptor
    • 10.1016/j.molcel.2009.02.016 1:CAS:528:DC%2BD1MXltFSms7Y%3D 19328064
    • R Wang Z Wei H Jin H Wu C Yu W Wen L-N Chan Z Wen M Zhang 2009 Autoinhibition of UNC5b revealed by the cytoplasmic domain structure of the receptor Mol Cell 33 692 703 10.1016/j.molcel.2009.02.016 1:CAS:528: DC%2BD1MXltFSms7Y%3D 19328064
    • (2009) Mol Cell , vol.33 , pp. 692-703
    • Wang, R.1    Wei, Z.2    Jin, H.3    Wu, H.4    Yu, C.5    Wen, W.6    Chan, L.-N.7    Wen, Z.8    Zhang, M.9
  • 23
    • 72949086465 scopus 로고    scopus 로고
    • Fluorescence approach to evaluating conformational changes upon binding of β-spectrin ankyrin-binding domain mutants with the lipid bilayer
    • 10.4149/gpb-2009-03-283 20037194
    • G Paździor A Chorzalska A Czogalla T Borowik AF Sikorski M Langner 2009 Fluorescence approach to evaluating conformational changes upon binding of β-spectrin ankyrin-binding domain mutants with the lipid bilayer Gen Physiol Biophys 28 283 293 10.4149/gpb-2009-03-283 20037194
    • (2009) Gen Physiol Biophys , vol.28 , pp. 283-293
    • Paździor, G.1    Chorzalska, A.2    Czogalla, A.3    Borowik, T.4    Sikorski, A.F.5    Langner, M.6
  • 24
    • 65849359061 scopus 로고    scopus 로고
    • Mapping of the lipid-binding and stability properties of the central rod domain of human dystrophin
    • 10.1016/j.jmb.2009.04.025 1:CAS:528:DC%2BD1MXms1aitb8%3D 19379759
    • S Legardinier C Raguénès-Nicol C Tascon C Rocher S Hardy JF Hubert E Le Rumeur 2009 Mapping of the lipid-binding and stability properties of the central rod domain of human dystrophin J Mol Biol 389 546 558 10.1016/j.jmb.2009.04.025 1:CAS:528:DC%2BD1MXms1aitb8%3D 19379759
    • (2009) J Mol Biol , vol.389 , pp. 546-558
    • Legardinier, S.1    Raguénès-Nicol, C.2    Tascon, C.3    Rocher, C.4    Hardy, S.5    Hubert, J.F.6    Le Rumeur, E.7
  • 25
    • 77953239491 scopus 로고    scopus 로고
    • Structural basis for spectrin recognition by ankyrin
    • Doi:10.1182/blood-2009-11-255604
    • Ipsaro JJ, Mondragón A (2010) Structural basis for spectrin recognition by ankyrin. Blood Doi: 10.1182/blood-2009-11-255604
    • (2010) Blood
    • Ipsaro, J.J.1    Mondragón, A.2
  • 26
    • 76749133529 scopus 로고    scopus 로고
    • Ankyrin recognizes both surface character and shape of the 14-15 di-repeat of β-spectrin
    • 10.1016/j.bbrc.2010.01.046 1:CAS:528:DC%2BC3cXit1Ohtb0%3D 20079712
    • PJ La-Borde PR Stabach I Siminović JS Morrow M Siminović 2010 Ankyrin recognizes both surface character and shape of the 14-15 di-repeat of β-spectrin Biochem Biophys Res Commun 392 490 494 10.1016/j.bbrc.2010. 01.046 1:CAS:528:DC%2BC3cXit1Ohtb0%3D 20079712
    • (2010) Biochem Biophys Res Commun , vol.392 , pp. 490-494
    • La-Borde, P.J.1    Stabach, P.R.2    Siminović, I.3    Morrow, J.S.4    Siminović, M.5
  • 27
    • 77954699179 scopus 로고    scopus 로고
    • Crystal structure and functional interpretation of the erythrocyte spectrin tetramerization domain complex
    • doi:10.1182/blood-2010-01-261396
    • Ipsaro JJ, Harper SL, Messick TE, Marmorstein R, Mondragón A, Speicher DW (2010) Crystal structure and functional interpretation of the erythrocyte spectrin tetramerization domain complex. Blood. doi: 10.1182/blood-2010-01-261396
    • (2010) Blood
    • Ipsaro, J.J.1    Harper, S.L.2    Messick, T.E.3    Marmorstein, R.4    Mondragón, A.5    Speicher, D.W.6
  • 28
    • 0027938023 scopus 로고
    • Molecular maps of red cell deformation: Hidden elasticity and in situ connectivity
    • 10.1126/science.7973655 1:CAS:528:DyaK2cXmvFOku78%3D 7973655
    • DE Discher N Mohandas EA Evans 1994 Molecular maps of red cell deformation: hidden elasticity and in situ connectivity Science 266 1032 1035 10.1126/science.7973655 1:CAS:528:DyaK2cXmvFOku78%3D 7973655
    • (1994) Science , vol.266 , pp. 1032-1035
    • Discher, D.E.1    Mohandas, N.2    Evans, E.A.3


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