메뉴 건너뛰기




Volumn 87, Issue 2, 2004, Pages 1215-1226

Structure of human annexin A6 at the air-water interface and in a membrane-bound state

Author keywords

[No Author keywords available]

Indexed keywords

ANNEXIN; ANNEXIN A6A; ANNEXIN A6B; CALPHOBINDIN II; LIPID; UNCLASSIFIED DRUG;

EID: 4143070134     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.103.038240     Document Type: Article
Times cited : (23)

References (58)
  • 1
    • 0029792781 scopus 로고    scopus 로고
    • Similarity in calcium channel activity of annexin V and matrix vesicles in planar lipid bilayers
    • Arispe, N., E. Rojas, B. R. Genge, L. N. Y. Wu, and R. E. Wuthier. 1996. Similarity in calcium channel activity of annexin V and matrix vesicles in planar lipid bilayers. Biophys. J. 71:1764-1775.
    • (1996) Biophys. J. , vol.71 , pp. 1764-1775
    • Arispe, N.1    Rojas, E.2    Genge, B.R.3    Wu, L.N.Y.4    Wuthier, R.E.5
  • 2
    • 0032497382 scopus 로고    scopus 로고
    • Crystal structure of bovine annexin VI in a calcium-bound state
    • Avila-Sakar, A. J., C. E. Creutz, and R. H. Kretsinger. 1998. Crystal structure of bovine annexin VI in a calcium-bound state. Biochim. Biophys. Acta. 1387:103-116.
    • (1998) Biochim. Biophys. Acta , vol.1387 , pp. 103-116
    • Avila-Sakar, A.J.1    Creutz, C.E.2    Kretsinger, R.H.3
  • 3
    • 0033912329 scopus 로고    scopus 로고
    • Membrane-bound 3D structures reveal the intrinsic flexibility of annexin VI
    • Avila-Sakar, A. J., R. H. Kretsinger, and C. E. Creutz. 2000. Membrane-bound 3D structures reveal the intrinsic flexibility of annexin VI. J. Struct. Biol. 130:54-62.
    • (2000) J. Struct. Biol. , vol.130 , pp. 54-62
    • Avila-Sakar, A.J.1    Kretsinger, R.H.2    Creutz, C.E.3
  • 6
    • 0032548810 scopus 로고    scopus 로고
    • Acid-induced equilibrium unfolding of annexin V wild type shows two intermediate states
    • Beermann, B. B., H. J. Hinz, A. Hofmann, and R. Huber. 1998. Acid-induced equilibrium unfolding of annexin V wild type shows two intermediate states. FEBS Lett. 423:265-269.
    • (1998) FEBS Lett. , vol.423 , pp. 265-269
    • Beermann, B.B.1    Hinz, H.J.2    Hofmann, A.3    Huber, R.4
  • 7
    • 0034667431 scopus 로고    scopus 로고
    • 2+-dependent interaction of annexin V with phospholipid membranes: A combined study using fluorescence techniques, microelectrophoresis and infrared spectroscopy
    • 2+-dependent interaction of annexin V with phospholipid membranes: a combined study using fluorescence techniques, microelectrophoresis and infrared spectroscopy. Phys. Chem. Chem. Phys. 2:4615-4623.
    • (2000) Phys. Chem. Chem. Phys. , vol.2 , pp. 4615-4623
    • Binder, H.1    Kohler, G.2    Arnold, K.3    Zschornig, O.4
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 0001679310 scopus 로고    scopus 로고
    • Optical constant determination in the infrared of uniaxially oriented monolayers from transmittance and reflectance measurements
    • Buffeteau, T., D. Blaudez, E. Pere, and B. Desbat. 1999. Optical constant determination in the infrared of uniaxially oriented monolayers from transmittance and reflectance measurements. J. Phys. Chem. B. 103:5020-5027.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 5020-5027
    • Buffeteau, T.1    Blaudez, D.2    Pere, E.3    Desbat, B.4
  • 11
    • 0027203361 scopus 로고
    • A rapid and efficient purification method for recombinant annexin V for biophysical studies
    • Burger, A., R. Berendes, D. Voges, R. Huber, and P. Demange. 1993. A rapid and efficient purification method for recombinant annexin V for biophysical studies. FEBS Lett. 329:25-28.
    • (1993) FEBS Lett. , vol.329 , pp. 25-28
    • Burger, A.1    Berendes, R.2    Voges, D.3    Huber, R.4    Demange, P.5
  • 12
    • 0034646288 scopus 로고    scopus 로고
    • Annexin XII E105K crystal structure: Identification of a pH-dependent switch for mutant hexamerization
    • Cartailler, J. P., H. T. Haigler, and H. Luecke. 2000. Annexin XII E105K crystal structure: identification of a pH-dependent switch for mutant hexamerization. Biochemistry. 39:2475-2483.
    • (2000) Biochemistry , vol.39 , pp. 2475-2483
    • Cartailler, J.P.1    Haigler, H.T.2    Luecke, H.3
  • 13
    • 0037012958 scopus 로고    scopus 로고
    • Secondary structure of spiralin in solution, at the air-water interface, and in interaction with lipid monolayers
    • Castano, S., D. Blaudez, B. Desbat, J. Dufourcq, and H. Wroblewski. 2002. Secondary structure of spiralin in solution, at the air-water interface, and in interaction with lipid monolayers. Biochim. Biophys. Acta. 1562:45-56.
    • (2002) Biochim. Biophys. Acta , vol.1562 , pp. 45-56
    • Castano, S.1    Blaudez, D.2    Desbat, B.3    Dufourcq, J.4    Wroblewski, H.5
  • 15
    • 0030048902 scopus 로고    scopus 로고
    • In situ study by polarization-modulated Fourier transform infrared spectroscopy of the structure and orientation of lipids and amphipathic peptides at the air-water interface
    • Cornut, L., B. Desbat, J. M. Turlet, and J. Dufourcq. 1996. In situ study by polarization-modulated Fourier transform infrared spectroscopy of the structure and orientation of lipids and amphipathic peptides at the air-water interface. Biophys. J. 70:305-312.
    • (1996) Biophys. J. , vol.70 , pp. 305-312
    • Cornut, L.1    Desbat, B.2    Turlet, J.M.3    Dufourcq, J.4
  • 16
    • 0034721869 scopus 로고    scopus 로고
    • Selective degradation of annexins by chaperone-mediated autophagy
    • Cuervo, A. M., A. V. Gomes, J. A. Barnes, and J. F. Dice. 2000. Selective degradation of annexins by chaperone-mediated autophagy. J. Biol. Chem. 275:33329-33335.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33329-33335
    • Cuervo, A.M.1    Gomes, A.V.2    Barnes, J.A.3    Dice, J.F.4
  • 19
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: From structure to function
    • Gerke, V., and S. E. Moss. 2002. Annexins: from structure to function. Physiol. Rev. 82:331-371.
    • (2002) Physiol. Rev. , vol.82 , pp. 331-371
    • Gerke, V.1    Moss, S.E.2
  • 20
    • 0035319319 scopus 로고    scopus 로고
    • Acidic pH-induced folding of annexin VI is a prerequisite for its insertion into lipid bilayers and formation of ion channels by the protein molecules
    • Golczak, M., A. Kicinska, J. Bandorowicz-Pikula, R. Buchet, A. Szewczyk, and S. Pikula. 2001a. Acidic pH-induced folding of annexin VI is a prerequisite for its insertion into lipid bilayers and formation of ion channels by the protein molecules. FASEB J. 15:1083-1085.
    • (2001) FASEB J. , vol.15 , pp. 1083-1085
    • Golczak, M.1    Kicinska, A.2    Bandorowicz-Pikula, J.3    Buchet, R.4    Szewczyk, A.5    Pikula, S.6
  • 21
    • 0035805190 scopus 로고    scopus 로고
    • Conformational states of annexin VI in solution induced by acidic pH
    • Golczak, M., A. Kirilenko, J. Bandorowicz-Pikula, and S. Pikula. 2001b. Conformational states of annexin VI in solution induced by acidic pH. FEBS Lett. 496:49-54.
    • (2001) FEBS Lett. , vol.496 , pp. 49-54
    • Golczak, M.1    Kirilenko, A.2    Bandorowicz-Pikula, J.3    Pikula, S.4
  • 22
    • 0034810737 scopus 로고    scopus 로고
    • N- and C-terminal halves of human annexin VI differ in ability to form low pH-induced ion channels
    • Golczak, M., A. Kirilenko, J. Bandorowicz-Pikula, and S. Pikula. 2001c. N- and C-terminal halves of human annexin VI differ in ability to form low pH-induced ion channels. Biochem. Biophys. Res. Commun. 284:785-791.
    • (2001) Biochem. Biophys. Res. Commun. , vol.284 , pp. 785-791
    • Golczak, M.1    Kirilenko, A.2    Bandorowicz-Pikula, J.3    Pikula, S.4
  • 23
    • 0034721867 scopus 로고    scopus 로고
    • Annexin VI stimulates endocytosis and is involved in the trafficking of low density lipoprotein to the prelysosomal compartment
    • Grewal, T., J. Heeren, D. Mewawala, T. Schnitgerhans, D. Wendt, G. Salomon, C. Enrich, U. Beisiegel, and S. Jackle. 2000. Annexin VI stimulates endocytosis and is involved in the trafficking of low density lipoprotein to the prelysosomal compartment. J. Biol. Chem. 275:33806-33813.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33806-33813
    • Grewal, T.1    Heeren, J.2    Mewawala, D.3    Schnitgerhans, T.4    Wendt, D.5    Salomon, G.6    Enrich, C.7    Beisiegel, U.8    Jackle, S.9
  • 24
    • 0034678130 scopus 로고    scopus 로고
    • ARF1 regulates pH-dependent COP functions in the early endocytic pathway
    • Gu, F., and J. Gruenberg. 2000. ARF1 regulates pH-dependent COP functions in the early endocytic pathway. J. Biol. Chem. 275:8154-8160.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8154-8160
    • Gu, F.1    Gruenberg, J.2
  • 28
  • 31
    • 0027848910 scopus 로고
    • Brewster angle microscopy. A new method of visualizing the spreading of Meibomian lipids
    • Kaercher, T., D. Honig, and D. Mobius. 1993-1994. Brewster angle microscopy. A new method of visualizing the spreading of Meibomian lipids. Int. Ophthalmol. 17:341-348.
    • (1993) Int. Ophthalmol. , vol.17 , pp. 341-348
    • Kaercher, T.1    Honig, D.2    Mobius, D.3
  • 32
    • 0036229987 scopus 로고    scopus 로고
    • GTP-induced membrane binding and ion channel activity of annexin VI: Is annexin VI a GTP biosensor?
    • Kirilenko, A., M. Golczak, S. Pikula, R. Buchet, and J. Bandorowicz-Pikula. 2002. GTP-induced membrane binding and ion channel activity of annexin VI: is annexin VI a GTP biosensor? Biophys. J. 82:2737-2745.
    • (2002) Biophys. J. , vol.82 , pp. 2737-2745
    • Kirilenko, A.1    Golczak, M.2    Pikula, S.3    Buchet, R.4    Bandorowicz-Pikula, J.5
  • 33
    • 0038233899 scopus 로고    scopus 로고
    • Annexin V interaction with phosphatidylserine-containing vesicles at low and neutral pH
    • Kohler, G., U. Hering, O. Zschornig, and K. Arnold. 1997. Annexin V interaction with phosphatidylserine-containing vesicles at low and neutral pH. Biochemistry. 36:8189-8194.
    • (1997) Biochemistry , vol.36 , pp. 8189-8194
    • Kohler, G.1    Hering, U.2    Zschornig, O.3    Arnold, K.4
  • 34
    • 0037137178 scopus 로고    scopus 로고
    • Determining the membrane topology of proteins: Insertion pathway of a transmembrane helix of annexin 12
    • Ladokhin, A. S., J. M. Isas, H. T. Haigler, and S. H. White. 2002. Determining the membrane topology of proteins: insertion pathway of a transmembrane helix of annexin 12. Biochemistry. 41:13617-13626.
    • (2002) Biochemistry , vol.41 , pp. 13617-13626
    • Ladokhin, A.S.1    Isas, J.M.2    Haigler, H.T.3    White, S.H.4
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 37
    • 0032564344 scopus 로고    scopus 로고
    • A transmembrane form of annexin XII detected by site-directed spin labeling
    • Langen, R., J. M. Isas, W. L. Hubbell, and H. T. Haigler. 1998a. A transmembrane form of annexin XII detected by site-directed spin labeling. Proc. Natl. Acad. Sci. USA. 95:14060-14065.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14060-14065
    • Langen, R.1    Isas, J.M.2    Hubbell, W.L.3    Haigler, H.T.4
  • 38
    • 0032575512 scopus 로고    scopus 로고
    • Membrane-mediated assembly of annexins studied by site-directed spin labeling
    • Langen, R., J. M. Isas, H. Luecke, H. T. Haigler, and W. L. Hubbell. 1998b. Membrane-mediated assembly of annexins studied by site-directed spin labeling. J. Biol. Chem. 273:22453-22457.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22453-22457
    • Langen, R.1    Isas, J.M.2    Luecke, H.3    Haigler, H.T.4    Hubbell, W.L.5
  • 39
    • 0000235168 scopus 로고    scopus 로고
    • The behaviour of membrane proteins in monolayers at the gas-water interface: Comparison between photosystem II, rhodopsin and bacteriorhodopsin
    • Lavoie, H., J. Gallant, M. Grandbois, D. Blaudez, B. Desbat, F. Boucher, and C. Saless. 1999. The behaviour of membrane proteins in monolayers at the gas-water interface: comparison between photosystem II, rhodopsin and bacteriorhodopsin. Mat. Sci. Eng. C-Bio. S. 10:147-154.
    • (1999) Mat. Sci. Eng. C-Bio. S , vol.10 , pp. 147-154
    • Lavoie, H.1    Gallant, J.2    Grandbois, M.3    Blaudez, D.4    Desbat, B.5    Boucher, F.6    Saless, C.7
  • 40
    • 0028846237 scopus 로고
    • Crystal structure of the annexin XII hexamer and implications for bilayer insertion
    • Luecke, H., B. T. Chang, W. S. Mailliard, D. D. Schlaepfer, and H. T. Haigler. 1995. Crystal structure of the annexin XII hexamer and implications for bilayer insertion. Nature (Lond.). 378:512-515.
    • (1995) Nature (Lond.) , vol.378 , pp. 512-515
    • Luecke, H.1    Chang, B.T.2    Mailliard, W.S.3    Schlaepfer, D.D.4    Haigler, H.T.5
  • 41
    • 0035782667 scopus 로고    scopus 로고
    • Trimers, dimers of trimers, and trimers of trimers are common building blocks of annexin A5 two-dimensional crystals
    • Oling, F., W. Bergsma-Schutter, and A. Brisson. 2001. Trimers, dimers of trimers, and trimers of trimers are common building blocks of annexin A5 two-dimensional crystals. J. Struct. Biol. 133:55-63.
    • (2001) J. Struct. Biol. , vol.133 , pp. 55-63
    • Oling, F.1    Bergsma-Schutter, W.2    Brisson, A.3
  • 42
    • 0031931006 scopus 로고    scopus 로고
    • Annexin VI defines an apical endocytic compartment in rat liver hepatocytes
    • Ortega, D., A. Pol, M. Biermer, S. Jackle, and C. Enrich. 1998. Annexin VI defines an apical endocytic compartment in rat liver hepatocytes. J. Cell Sci. 111:261-269.
    • (1998) J. Cell Sci. , vol.111 , pp. 261-269
    • Ortega, D.1    Pol, A.2    Biermer, M.3    Jackle, S.4    Enrich, C.5
  • 43
    • 4143135647 scopus 로고    scopus 로고
    • Acidic pH-induced ion channels formed by annexin VI-transformation from soluble to membrane integral protein
    • J. Bandorowicz-Pikula, editor. Kluwer Academic/Plenum Publishers, New York, NY, and Landes Bioscience, Georgetown, TX
    • Pikula, S. 2003. Acidic pH-induced ion channels formed by annexin VI-transformation from soluble to membrane integral protein. In Annexins: Biological Importance and Annexin-Related Pathologies. J. Bandorowicz-Pikula, editor. Kluwer Academic/Plenum Publishers, New York, NY, and Landes Bioscience, Georgetown, TX. 182-195.
    • (2003) Annexins: Biological Importance and Annexin-Related Pathologies , pp. 182-195
    • Pikula, S.1
  • 44
    • 0030700638 scopus 로고    scopus 로고
    • Identification of cytoskeleton-associated proteins in isolated rat liver endosomes
    • Pol, A., D. Ortega, and C. Enrich. 1997. Identification of cytoskeleton-associated proteins in isolated rat liver endosomes. Biochem. J. 327:741-746.
    • (1997) Biochem. J. , vol.327 , pp. 741-746
    • Pol, A.1    Ortega, D.2    Enrich, C.3
  • 45
    • 0034713256 scopus 로고    scopus 로고
    • Late endocytic compartments are major sites of annexin VI localization in NRK fibroblasts and polarized WIF-B hepatoma cells
    • Pons, M., G. Ihrke, S. Koch, M. Biermer, A. Pol, T. Grewal, S. Jackle, and C. Enrich. 2000. Late endocytic compartments are major sites of annexin VI localization in NRK fibroblasts and polarized WIF-B hepatoma cells. Exp. Cell Res. 257:33-47.
    • (2000) Exp. Cell Res. , vol.257 , pp. 33-47
    • Pons, M.1    Ihrke, G.2    Koch, S.3    Biermer, M.4    Pol, A.5    Grewal, T.6    Jackle, S.7    Enrich, C.8
  • 46
    • 0035840266 scopus 로고    scopus 로고
    • Evidence for the involvement of annexin 6 in the trafficking between the endocytic compartment and lysosomes
    • Pons, M., T. Grewal, E. Rius, T. Schnitgerhans, S. Jackle, and C. Enrich. 2001a. Evidence for the involvement of annexin 6 in the trafficking between the endocytic compartment and lysosomes. Exp. Cell Res. 269:13-22.
    • (2001) Exp. Cell Res. , vol.269 , pp. 13-22
    • Pons, M.1    Grewal, T.2    Rius, E.3    Schnitgerhans, T.4    Jackle, S.5    Enrich, C.6
  • 47
    • 0035854784 scopus 로고    scopus 로고
    • Activation of Raf-1 is defective in annexin 6 overexpressing Chinese hamster ovary cells
    • Pons, M., F. Tebar, M. Kirchhoff, S. Peiro, I. de Diego, T. Grewal, and C. Enrich. 2001b. Activation of Raf-1 is defective in annexin 6 overexpressing Chinese hamster ovary cells. FEBS Lett. 501:69-73.
    • (2001) FEBS Lett. , vol.501 , pp. 69-73
    • Pons, M.1    Tebar, F.2    Kirchhoff, M.3    Peiro, S.4    De Diego, I.5    Grewal, T.6    Enrich, C.7
  • 48
    • 0014468553 scopus 로고
    • Formation and properties of thin-walled phospholipids vesicles
    • Reeves, J. P., and R. M. Dowben. 1969. Formation and properties of thin-walled phospholipids vesicles. J. Cell. Physiol. 73:49-60.
    • (1969) J. Cell. Physiol. , vol.73 , pp. 49-60
    • Reeves, J.P.1    Dowben, R.M.2
  • 49
    • 17344378494 scopus 로고    scopus 로고
    • Structure and dynamics of annexin 12 bound to a planar lipid bilayer
    • Epub 2003 Oct 29
    • Risse, T., W. L. Hubbell, J. M. Isas, and H. T. Haigler. 2003. Structure and dynamics of annexin 12 bound to a planar lipid bilayer. Phys. Rev. Lett. 91:188101. Epub 2003 Oct 29.
    • (2003) Phys. Rev. Lett. , vol.91 , pp. 188101
    • Risse, T.1    Hubbell, W.L.2    Isas, J.M.3    Haigler, H.T.4
  • 50
    • 0033524425 scopus 로고    scopus 로고
    • Fourier transform infrared linked analysis of conformational changes in annexin V upon membrane binding
    • Silvestro, L., and P. H. Axelsen. 1999. Fourier transform infrared linked analysis of conformational changes in annexin V upon membrane binding. Biochemistry. 38:113-121.
    • (1999) Biochemistry , vol.38 , pp. 113-121
    • Silvestro, L.1    Axelsen, P.H.2
  • 52
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 54
    • 0037423193 scopus 로고    scopus 로고
    • 2+ influx regulates growth plate chondrocyte maturation and apoptosis
    • 2+ influx regulates growth plate chondrocyte maturation and apoptosis. J. Biol. Chem. 278:3762-3769.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3762-3769
    • Wang, W.1    Xu, J.2    Kirsch, T.3
  • 55
    • 0032321726 scopus 로고    scopus 로고
    • Protein folding in membranes: Determining energetics of peptide-bilayer interactions
    • White, S. H., W. C. Wimley, A. S. Ladokhin, and K. Hristova. 1998. Protein folding in membranes: determining energetics of peptide-bilayer interactions. Methods Enzymol. 295:62-87.
    • (1998) Methods Enzymol. , vol.295 , pp. 62-87
    • White, S.H.1    Wimley, W.C.2    Ladokhin, A.S.3    Hristova, K.4
  • 58
    • 0034839237 scopus 로고    scopus 로고
    • Association of annexin 2 with recycling endosomes requires either calcium- or cholesterol-stabilized membrane domains
    • Zeuschner, D., W. Stoorvogel, and V. Gerke. 2001. Association of annexin 2 with recycling endosomes requires either calcium- or cholesterol-stabilized membrane domains. Eur. J. Cell Biol. 80:499-507.
    • (2001) Eur. J. Cell Biol. , vol.80 , pp. 499-507
    • Zeuschner, D.1    Stoorvogel, W.2    Gerke, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.