메뉴 건너뛰기




Volumn 110, Issue 2, 1997, Pages 221-228

Identification and characterization of a novel type of annexin-membrane interaction: Ca2+ is not required for the association of annexin II with early endosomes

Author keywords

Ca2+ phospholipid binding protein; Endocytosis; Membrane cytoskeleton interaction

Indexed keywords

CALCIUM ION; LIPOCORTIN 2;

EID: 0031038664     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (96)

References (43)
  • 1
    • 0024390672 scopus 로고
    • A role for calpactin in calcium dependent exocytosis in adrenal chromaffin cells
    • Ali, S. M., Geisow, M. J. and Burgoyne, R. D. (1989). A role for calpactin in calcium dependent exocytosis in adrenal chromaffin cells. Nature 340, 313-315.
    • (1989) Nature , vol.340 , pp. 313-315
    • Ali, S.M.1    Geisow, M.J.2    Burgoyne, R.D.3
  • 2
    • 0029869843 scopus 로고    scopus 로고
    • An endosomal βCOP is involved in the pH-dependent formation of transport vesicles destined for late endosomes
    • Aniento, F., Gu, F., Parton, R. G. and Gruenberg, J. (1996). An endosomal βCOP is involved in the pH-dependent formation of transport vesicles destined for late endosomes. J. Cell Biol. 133, 29-41.
    • (1996) J. Cell Biol. , vol.133 , pp. 29-41
    • Aniento, F.1    Gu, F.2    Parton, R.G.3    Gruenberg, J.4
  • 3
    • 0027183815 scopus 로고
    • A guide to the use of pore-forming toxins for controlled permeabilization of cell membranes
    • Bhakdi, S., Weller, U., Walev, I., Martin, E., Jonas, D. and Palmer, M. (1993). A guide to the use of pore-forming toxins for controlled permeabilization of cell membranes. Med. Microbiol. Immunol. 182, 167-175.
    • (1993) Med. Microbiol. Immunol. , vol.182 , pp. 167-175
    • Bhakdi, S.1    Weller, U.2    Walev, I.3    Martin, E.4    Jonas, D.5    Palmer, M.6
  • 4
    • 0025678441 scopus 로고
    • Protein-protein recognition via short amphiphilic helices; a mutational analysis of the binding site of annexin II for p 11
    • Becker, T., Weber, K. and Johnsson, N. (1990). Protein-protein recognition via short amphiphilic helices; a mutational analysis of the binding site of annexin II for p 11. EMBO J. 9, 4207-4213.
    • (1990) EMBO J. , vol.9 , pp. 4207-4213
    • Becker, T.1    Weber, K.2    Johnsson, N.3
  • 5
    • 0025029828 scopus 로고
    • Microtubule- and motor-dependent fusion in vitro between apical and basolateral endocytic vesicles from MDCK cells
    • Bomsel, M., Parton, R., Kurznetsov, S. A., Schroer, T. A. and Gruenberg, J. (1990). Microtubule- and motor-dependent fusion in vitro between apical and basolateral endocytic vesicles from MDCK cells. Cell 62, 719-731.
    • (1990) Cell , vol.62 , pp. 719-731
    • Bomsel, M.1    Parton, R.2    Kurznetsov, S.A.3    Schroer, T.A.4    Gruenberg, J.5
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein dye-binding
    • Bradford, M. M. (1976). A rapid and sensitive method for 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
  • 7
    • 0022517260 scopus 로고
    • A cell free system to study reassembly of the nuclear envelope at the end of mitosis
    • Burke, B. and Gerace, L. (1986). A cell free system to study reassembly of the nuclear envelope at the end of mitosis. Cell 44, 639-652.
    • (1986) Cell , vol.44 , pp. 639-652
    • Burke, B.1    Gerace, L.2
  • 8
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen, C. and Okayama, H. (1987). High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7, 2745-2752.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 9
    • 0026452240 scopus 로고
    • The annexins and exocytosis
    • Creutz, C. E. (1992). The annexins and exocytosis. Science 258, 924-931.
    • (1992) Science , vol.258 , pp. 924-931
    • Creutz, C.E.1
  • 10
    • 0023818448 scopus 로고
    • Aggregation of chromaffin granules by calpactin at micromolar levels of calcium
    • Drust, D. S. and Creutz, C. E. (1988). Aggregation of chromaffin granules by calpactin at micromolar levels of calcium. Nature 331, 88-91.
    • (1988) Nature , vol.331 , pp. 88-91
    • Drust, D.S.1    Creutz, C.E.2
  • 12
    • 0021299594 scopus 로고
    • Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein from brush borders; calcium-dependent binding to nonerythroid spectrin and F-actin
    • Gerke, V. and Weber, K. (1984). Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein from brush borders; calcium-dependent binding to nonerythroid spectrin and F-actin. EMBO J. 3, 227-233.
    • (1984) EMBO J. , vol.3 , pp. 227-233
    • Gerke, V.1    Weber, K.2
  • 13
    • 0011829734 scopus 로고
    • Evolutionary conservation and three-dimensional folding of the tyrosine kinase substrate annexin II
    • (ed. S. E. Moss), Portland Press, London
    • Gerke, V. (1992). Evolutionary conservation and three-dimensional folding of the tyrosine kinase substrate annexin II. In The Annexins (ed. S. E. Moss), pp. 47-59. Portland Press, London.
    • (1992) The Annexins , pp. 47-59
    • Gerke, V.1
  • 14
    • 0011112272 scopus 로고    scopus 로고
    • Annexins and membrane traffic
    • (ed. B. A. Seaton). Landes Science Publishers, Georgetown, TX (in press)
    • Gerke, V. (1996). Annexins and membrane traffic. In Annexins: Molecular Structure to Cell Function (ed. B. A. Seaton). Landes Science Publishers, Georgetown, TX (in press).
    • (1996) Annexins: Molecular Structure to Cell Function
    • Gerke, V.1
  • 15
    • 0022928659 scopus 로고
    • 2+-binding by the 36-kDa tyrosine kinase substrate (calpactin) and its 33-kDa core
    • 2+-binding by the 36-kDa tyrosine kinase substrate (calpactin) and its 33-kDa core. J. Biol. Chem. 261, 7247-7252.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7247-7252
    • Glenney J.R., Jr.1
  • 16
    • 0025974686 scopus 로고
    • Rab5 controls early endosome fusion in vitro
    • Gorvel, J. P., Chavrier, P., Zerial, M. and Gruenberg, J. (1991). rab5 controls early endosome fusion in vitro. Cell 64, 915-925.
    • (1991) Cell , vol.64 , pp. 915-925
    • Gorvel, J.P.1    Chavrier, P.2    Zerial, M.3    Gruenberg, J.4
  • 17
    • 0027158668 scopus 로고
    • Annexins in membrane transport
    • Gruenberg, J. and Emans, N. (1993). Annexins in membrane transport. Trends Cell Biol. 3, 224-227.
    • (1993) Trends Cell Biol. , vol.3 , pp. 224-227
    • Gruenberg, J.1    Emans, N.2
  • 19
    • 0030899412 scopus 로고    scopus 로고
    • Specific release of membrane hound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol
    • in press
    • Harder, T., Kellner, R., Parton, R. G. and Gruenberg, J. (1997). Specific release of membrane hound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol. Mol. Biol. Cell (in press).
    • (1997) Mol. Biol. Cell
    • Harder, T.1    Kellner, R.2    Parton, R.G.3    Gruenberg, J.4
  • 21
    • 0025000276 scopus 로고
    • The crystal and molecular structure of human annexin V, an anticoagulant calcium, membrane binding protein
    • Huber, R., Römisch, J. and Paques, E. P. (1990). The crystal and molecular structure of human annexin V, an anticoagulant calcium, membrane binding protein. EMBO J. 9, 3867-3874.
    • (1990) EMBO J. , vol.9 , pp. 3867-3874
    • Huber, R.1    Römisch, J.2    Paques, E.P.3
  • 22
    • 0000259584 scopus 로고
    • Annexin V: Crystal structure and its implications on function
    • (ed. S. E. Moss), Portland Press, London
    • Huber, R., Berendes, R., Burger, A., Luecke, H. and Karshikov, A. (1992). Annexin V: crystal structure and its implications on function. In The Annexins (ed. S. E. Moss), pp. 105-124. Portland Press, London.
    • (1992) The Annexins , pp. 105-124
    • Huber, R.1    Berendes, R.2    Burger, A.3    Luecke, H.4    Karshikov, A.5
  • 23
    • 0022491787 scopus 로고
    • Binding sites for calcium, lipid and p11 on p36, the substrate of retroviral tyrosine-specitic protein kinases
    • Johnsson, N., Vanderkerckhove, J., van Damme, J. and Weber, K. (1986). Binding sites for calcium, lipid and p11 on p36, the substrate of retroviral tyrosine-specitic protein kinases. FEBS Lett. 198, 361-364.
    • (1986) FEBS Lett. , vol.198 , pp. 361-364
    • Johnsson, N.1    Vanderkerckhove, J.2    Van Damme, J.3    Weber, K.4
  • 24
    • 0024062670 scopus 로고
    • p36, the major cytoplasmic substrate of src tyrosine protein kinase, binds to its p11 subunit via a short amino-terminal amphiphatic helix
    • Johnsson, N., Marriott, G. and Weber, K. (1988). p36, the major cytoplasmic substrate of src tyrosine protein kinase, binds to its p11 subunit via a short amino-terminal amphiphatic helix. EMBO J. 7, 2435-3442.
    • (1988) EMBO J. , vol.7 , pp. 2435-3442
    • Johnsson, N.1    Marriott, G.2    Weber, K.3
  • 27
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A. (1985). Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Nat. Acad. Sci. USA 82, 488-492.
    • (1985) Proc. Nat. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 28
    • 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 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0016430638 scopus 로고
    • Refinement of the structure of carp muscle calcium-binding parvalbumin by model building and difference Fourier analysis
    • Moews, P. C. and Kretsinger, R. H. (1975). Refinement of the structure of carp muscle calcium-binding parvalbumin by model building and difference Fourier analysis. J. Mol. Biol. 91, 6645-6653.
    • (1975) J. Mol. Biol. , vol.91 , pp. 6645-6653
    • Moews, P.C.1    Kretsinger, R.H.2
  • 32
    • 0025117429 scopus 로고
    • Conformational change and localization of calpactin I complex involved in exocytosis as revealed by quick-freeze, deep-etch electron microscopy and immunocytochemistry
    • Nakata, T., Sobue, K. and Hirokawa, N. (1990). Conformational change and localization of calpactin I complex involved in exocytosis as revealed by quick-freeze, deep-etch electron microscopy and immunocytochemistry. J. Cell Biol. 110, 13-25.
    • (1990) J. Cell Biol. , vol.110 , pp. 13-25
    • Nakata, T.1    Sobue, K.2    Hirokawa, N.3
  • 33
    • 0023897690 scopus 로고
    • The submembraneous location of p11 and its interaction with the p36 substrate of pp60 src kinase in situ
    • Osborn, M., Johnsson, N., Wehland, J. and Weber, K. (1988). The submembraneous location of p11 and its interaction with the p36 substrate of pp60 src kinase in situ. Exp. Cell Res. 175, 81-96.
    • (1988) Exp. Cell Res. , vol.175 , pp. 81-96
    • Osborn, M.1    Johnsson, N.2    Wehland, J.3    Weber, K.4
  • 34
    • 0028324464 scopus 로고
    • Annexins: The problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins
    • Raynal, P. and Pollard, H. B. (1994). Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins. Biochim. Biophys. Acta 1197, 63-93.
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 63-93
    • Raynal, P.1    Pollard, H.B.2
  • 36
    • 0026063254 scopus 로고
    • The participation of annexin II (calpactin I) in calcium-evoked exocytosis requires protein kinase C
    • Sarafian, T., Pradel, L. A., Henry, J. P., Aunis, D. and Bader, M. F. (1991). The participation of annexin II (calpactin I) in calcium-evoked exocytosis requires protein kinase C. J. Cell Biol. 114, 1135-1147.
    • (1991) J. Cell Biol. , vol.114 , pp. 1135-1147
    • Sarafian, T.1    Pradel, L.A.2    Henry, J.P.3    Aunis, D.4    Bader, M.F.5
  • 37
    • 0028233432 scopus 로고
    • Annexin structure and membrane interactions: A molecular perspective
    • Swairjo, M. A. and Seaton, B. A. (1994). Annexin structure and membrane interactions: a molecular perspective. Annu. Rev. Biophys. Biomol. Struct. 23, 193-213.
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 193-213
    • Swairjo, M.A.1    Seaton, B.A.2
  • 38
    • 0025797231 scopus 로고
    • Characterization of a discontinuous epitope on annexin II by site-directed mutagenesis
    • Thiel, C., Weber, K. and Gerke, V. (1991). Characterization of a discontinuous epitope on annexin II by site-directed mutagenesis. FEBS Lett. 285, 59-62.
    • (1991) FEBS Lett. , vol.285 , pp. 59-62
    • Thiel, C.1    Weber, K.2    Gerke, V.3
  • 40
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocuellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. and Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocuellulose sheets: procedure and some applications. Proc. Nat. Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Nat. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 41
    • 0003001809 scopus 로고
    • Annexin II: Interaction with p11
    • (ed. S. E. Moss), Portland Press, London
    • Weber, K. (1992). Annexin II: interaction with p11. In The Annexins (ed. S. E. Moss), pp. 61-68. Portland Press, London.
    • (1992) The Annexins , pp. 61-68
    • Weber, K.1
  • 43
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of proteins in dilute solution in the presence of detergents and lipids
    • Wessel, D. and Flügge, U. J. (1984). A method for the quantitative recovery of proteins in dilute solution in the presence of detergents and lipids. Anal. Biochem. 138, 141-143.
    • (1984) Anal. Biochem. , vol.138 , pp. 141-143
    • Wessel, D.1    Flügge, U.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.