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Volumn 15, Issue 3, 2010, Pages 406-423

The effect of the lipid-binding site of the ankyrin-binding domain of erythroid β-spectrin on the properties of natural membranes and skeletal structures

Author keywords

Ankyrin binding domain; Membrane skeleton properties; Resealed ghosts; Spectrin lipid interactions; Transmembrane protein aggregation

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ANKYRIN; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; NERVE CELL ADHESION MOLECULE; NERVE CELL ADHESION MOLECULE L1; SPECTRIN; SPECTRIN BETA SUBUNIT; UNCLASSIFIED DRUG; UVOMORULIN; ACTIN; CADHERIN; RECOMBINANT PROTEIN;

EID: 77956910211     PISSN: 14258153     EISSN: 16891392     Source Type: Journal    
DOI: 10.2478/s11658-010-0012-6     Document Type: Article
Times cited : (12)

References (35)
  • 1
    • 0014411415 scopus 로고
    • Selective solubilization of a protein component of the red cell membrane
    • Marchesi, V. T. and Steers, Jr E. Selective solubilization of a protein component of the red cell membrane. Science159 (1968) 203-204.
    • (1968) Science , vol.159 , pp. 203-204
    • Marchesi, V.T.1    Steers Jr., E.2
  • 2
    • 0006791435 scopus 로고
    • Identification of a spectrin-like protein in nonerythroid cells
    • Goodman, S. R., Zagon, I. S. and Kulikowski, R. R. Identification of a spectrin-like protein in nonerythroid cells. Proc. Natl Acad. Sci. USA78 (1981) 7570-7574.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 7570-7574
    • Goodman, S.R.1    Zagon, I.S.2    Kulikowski, R.R.3
  • 3
    • 0033880909 scopus 로고    scopus 로고
    • Spectrin tethers and mesh in the biosynthetic pathway
    • De Matteis, M. A. and Morrow, J. S. Spectrin tethers and mesh in the biosynthetic pathway. J. Cell Sci. 113 (2000) 2331-2343.
    • (2000) J. Cell Sci. , vol.113 , pp. 2331-2343
    • de Matteis, M.A.1    Morrow, J.S.2
  • 4
    • 14044267645 scopus 로고    scopus 로고
    • SH3 domain of spectrin participates in the activation of Rac in specialized calpain-induced integrin signaling complexes
    • Bialkowska, K., Saido, T. C. and Fox, J. E. B. SH3 domain of spectrin participates in the activation of Rac in specialized calpain-induced integrin signaling complexes. J. Cell Sci. 118 (2005) 381-395.
    • (2005) J. Cell Sci. , vol.118 , pp. 381-395
    • Bialkowska, K.1    Saido, T.C.2    Fox, J.E.B.3
  • 5
    • 0037470058 scopus 로고    scopus 로고
    • c-Src binds αII Spectrin's Src Homology 3 (SH3) domain and blocks calpain susceptibility by phosphorylating Tyr1176*
    • Nedrelow, J. H., Cianci, C. D. and Morrow, J. S. c-Src binds αII Spectrin's Src Homology 3 (SH3) domain and blocks calpain susceptibility by phosphorylating Tyr1176*. J. Biol. Chem. 278 (2003) 7735-7741.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7735-7741
    • Nedrelow, J.H.1    Cianci, C.D.2    Morrow, J.S.3
  • 6
    • 0034958883 scopus 로고    scopus 로고
    • Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues
    • Bennett, V. and Baines, A. J. Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues. Physiol. Rev. 81 (2001) 1353-1392.
    • (2001) Physiol. Rev. , vol.81 , pp. 1353-1392
    • Bennett, V.1    Baines, A.J.2
  • 8
    • 0028263839 scopus 로고
    • Mechanical properties of the red cell membrane in relation to molecular structure and genetic defects
    • Mohandas, N. and Evans, E. Mechanical properties of the red cell membrane in relation to molecular structure and genetic defects. Annu. Rev. Biophys. Biomol. Struct. 23 (1994) 787-818.
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 787-818
    • Mohandas, N.1    Evans, E.2
  • 10
    • 0017370212 scopus 로고
    • Selective association of spectrin with the cytoplasmic surface of Human erythrocyte plasma membranes. Quantitative determination with purified (32P)spectrin
    • Bennett, V. and Branton, D. Selective association of spectrin with the cytoplasmic surface of Human erythrocyte plasma membranes. Quantitative determination with purified (32P)spectrin. J. Biol. Chem. 252 (1977) 2753-2763.
    • (1977) J. Biol. Chem. , vol.252 , pp. 2753-2763
    • Bennett, V.1    Branton, D.2
  • 11
    • 0018759538 scopus 로고
    • The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes
    • Bennett, V. and Stenbuck, P. J. The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes. Nature280 (1979) 468-473.
    • (1979) Nature , vol.280 , pp. 468-473
    • Bennett, V.1    Stenbuck, P.J.2
  • 12
    • 0346761425 scopus 로고
    • Syndeins: the spectrin-binding protein(s) of the human erythrocyte membrane
    • Yu, J. and Goodman, S. R. Syndeins: the spectrin-binding protein(s) of the human erythrocyte membrane. Proc. Natl Acad. Sci. USA76 (1979) 2340-2344.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 2340-2344
    • Yu, J.1    Goodman, S.R.2
  • 13
    • 0028944110 scopus 로고
    • Identification of the membrane attachment sites for protein 4.1 in the human erythrocyte
    • Hemming, N. J., Anstee, D. J., Staricoff, M. A., Tanner, M. J. A. and Mohandas, N. Identification of the membrane attachment sites for protein 4. 1 in the human erythrocyte. J. Biol. Chem. 270 (1995) 5360-5366.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5360-5366
    • Hemming, N.J.1    Anstee, D.J.2    Staricoff, M.A.3    Tanner, M.J.A.4    Mohandas, N.5
  • 15
    • 0038491423 scopus 로고    scopus 로고
    • Rh-RhAG/ankyrin-R, a new interaction site between the membrane bilayer and the red cell skeleton, is impaired by Rh(null)-associated mutation
    • Nicolas, V., Le van Kim, C., Gane, P., Birkenmeier, C., Cartron, J. P., Colin, Y. and Mouro-Chanteloup, I. Rh-RhAG/ankyrin-R, a new interaction site between the membrane bilayer and the red cell skeleton, is impaired by Rh(null)-associated mutation. J. Biol. Chem. 278 (2003) 25526-25533.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25526-25533
    • Nicolas, V.1    Le van Kim, C.2    Gane, P.3    Birkenmeier, C.4    Cartron, J.P.5    Colin, Y.6    Mouro-Chanteloup, I.7
  • 17
    • 70349254604 scopus 로고    scopus 로고
    • Adducin forms a bridge between the erythrocyte membrane and its cytoskeleton and regulates membrane cohesion
    • Anong, W. A., Franco, T., Chu, H., Weis, T. L., Devlin, E. E., Bodine, D. M., An, X. Mohandas, N. and Low, P. S. Adducin forms a bridge between the erythrocyte membrane and its cytoskeleton and regulates membrane cohesion. Blood114 (2009) 1904-1912. doi 10. 1182/blood-2009-02-203216. DOI 10. 1182/blood-2009-02-203216.
    • (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
  • 18
    • 33846274937 scopus 로고    scopus 로고
    • The molecular basis of hereditary red cell membrane disorders
    • Delaunay, J. The molecular basis of hereditary red cell membrane disorders. Blood Rev. 21 (2007) 1-20.
    • (2007) Blood Rev. , vol.21 , pp. 1-20
    • Delaunay, J.1
  • 19
    • 0345832247 scopus 로고    scopus 로고
    • Phosphatidylserine binding sites in erythroid spectrin: Location and implications for membrane stability
    • An, X., Guo, X., Sum, H., Morrow, J., Gratzer, W. and Mohandas, N. Phosphatidylserine binding sites in erythroid spectrin: Location and implications for membrane stability. Biochemistry43 (2004) 310-315.
    • (2004) Biochemistry , vol.43 , pp. 310-315
    • An, X.1    Guo, X.2    Sum, H.3    Morrow, J.4    Gratzer, W.5    Mohandas, N.6
  • 21
    • 0028215013 scopus 로고
    • Ankyrin inhibits binding of erythrocyte spectrin to phospholipid vesicles
    • Białkowska, K., Zembro., A. and Sikorski, A. F. Ankyrin inhibits binding of erythrocyte spectrin to phospholipid vesicles. Biochim. Biophys. Acta1191 (1994) 21-26.
    • (1994) Biochim. Biophys. Acta , vol.1191 , pp. 21-26
    • Białkowska, K.1    Zembro, A.2    Sikorski, A.F.3
  • 22
    • 1942423758 scopus 로고    scopus 로고
    • Membrane interaction of erythroid spectrin: surface-density dependent high-affinity binding to phosphatidylethanolamine
    • Ray, S. and Chakrabarti, A. Membrane interaction of erythroid spectrin: surface-density dependent high-affinity binding to phosphatidylethanolamine. Mol. Membr. Biol. 21 (2004) 93-100.
    • (2004) Mol. Membr. Biol. , vol.21 , pp. 93-100
    • Ray, S.1    Chakrabarti, A.2
  • 25
    • 0025995618 scopus 로고
    • Ankyrin binds to the 15th repetitive unit of erythroid and nonerythroid beta-spectrin
    • Kennedy, S. P., Warren, S. L., Forget, B. G. and Morrow, J. S. Ankyrin binds to the 15th repetitive unit of erythroid and nonerythroid beta-spectrin. J. Cell. Biol. 115 (1991) 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
  • 26
    • 0015481306 scopus 로고
    • Factors controlling the resealing of the membrane of human erythrocyte ghosts after hypotonic hemolysis
    • Bodemann, H. and Passow, H. Factors controlling the resealing of the membrane of human erythrocyte ghosts after hypotonic hemolysis. J. Membr. Biol. 8 (1972) 1-26.
    • (1972) J. Membr. Biol. , vol.8 , pp. 1-26
    • Bodemann, H.1    Passow, H.2
  • 27
    • 0016360444 scopus 로고
    • Preparation of impermeable ghosts and inside-out vesicles from Human erythrocyte membranes
    • Steck, T. L. and Kant, J. A. Preparation of impermeable ghosts and inside-out vesicles from Human erythrocyte membranes. Methods Enzymol. 31 (1974) 172-180.
    • (1974) Methods Enzymol. , vol.31 , pp. 172-180
    • Steck, T.L.1    Kant, J.A.2
  • 29
    • 0037133206 scopus 로고    scopus 로고
    • Identification of a functional role for lipid asymmetry in biological membranes: Phosphatidylserine-skeletal protein interactions modulate membrane stability
    • Manno, S., Takakuwa, Y. and Mohandas, N. Identification of a functional role for lipid asymmetry in biological membranes: Phosphatidylserine-skeletal protein interactions modulate membrane stability. Proc. Natl. Acad. Sci. USA99 (2002) 1943-1948.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1943-1948
    • Manno, S.1    Takakuwa, Y.2    Mohandas, N.3
  • 30
    • 0028917316 scopus 로고
    • Expression of functional domains of betaG spectrin disrupts epithelial morphology in cultured cells
    • Hu, R. J., Moorthy, S. and Bennett, V. Expression of functional domains of betaG spectrin disrupts epithelial morphology in cultured cells. J. Cell Biol. 128 (1995) 1069-1080.
    • (1995) J. Cell Biol. , vol.128 , pp. 1069-1080
    • Hu, R.J.1    Moorthy, S.2    Bennett, V.3
  • 31
    • 0039247377 scopus 로고    scopus 로고
    • Interactions of Spectrins with Membrane Intrinsic Domain
    • Sikorski, A. F. and Białkowska, K. Interactions of Spectrins with Membrane Intrinsic Domain. Cell. Mol. Biol. Lett. 1 (1996) 97-104.
    • (1996) Cell. Mol. Biol. Lett. , vol.1 , pp. 97-104
    • Sikorski, A.F.1    Białkowska, K.2
  • 32
    • 62549129569 scopus 로고    scopus 로고
    • Structures of the spectrin-ankyrin interaction binding domains
    • Ipsaro, J. J., Huang, L. and Mondragon, A. Structures of the spectrin-ankyrin interaction binding domains. Blood113 (2009) 5385-5393.
    • (2009) Blood , vol.113 , pp. 5385-5393
    • Ipsaro, J.J.1    Huang, L.2    Mondragon, A.3
  • 34
    • 54049121344 scopus 로고    scopus 로고
    • Phospholipid-induced structural changes to an erythroid beta spectrin ankyrin-dependent lipid-binding site
    • Czogalla, A., Grzymajło, K, Jezierski, A. and Sikorski, A. F. Phospholipid-induced structural changes to an erythroid beta spectrin ankyrin-dependent lipid-binding site. Biochim. Biophys. Acta1778 (2008) 2612-2620.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 2612-2620
    • Czogalla, A.1    Grzymajło, K.2    Jezierski, A.3    Sikorski, A.F.4
  • 35
    • 67049164963 scopus 로고    scopus 로고
    • The structure of the ankyrin-binding site of b-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties
    • Stabach, P. R., Simonovic, I., Ranieri, M. A., Abodi, M. S., Steitz, T. A., Simonovic, M. and Morrow, J. S. The structure of the ankyrin-binding site of b-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties. Blood113 (2009) 5377-5384.
    • (2009) Blood , vol.113 , pp. 5377-5384
    • Stabach, P.R.1    Simonovic, I.2    Ranieri, M.A.3    Abodi, M.S.4    Steitz, T.A.5    Simonovic, M.6    Morrow, J.S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.