메뉴 건너뛰기




Volumn 2, Issue 10, 2007, Pages

The p11/S100A10 light chain of annexin A2 is dispensable for annexin A2 association to endosomes and functions in endosomal transport

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CALCIUM BINDING PROTEIN; LIPOCORTIN 2; LIPOSOME; MEMBRANE PROTEIN; PHOSPHOLIPID BINDING PROTEIN; PROTEIN S 100; PROTEIN S 100A10; SMALL INTERFERING RNA; ANXA2 PROTEIN, HUMAN; CALCIUM; GLYCOPROTEIN; S100 CALCIUM BINDING PROTEIN A10; UNCLASSIFIED DRUG;

EID: 42549145897     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0001118     Document Type: Article
Times cited : (57)

References (36)
  • 2
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: From structure to function
    • Gerke V, Moss SE (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
  • 3
    • 3242877433 scopus 로고    scopus 로고
    • Annexins-unique membrane binding proteins with diverse functions
    • Rescher U, Gerke V (2004) Annexins-unique membrane binding proteins with diverse functions. J Cell Sci 117: 2631-2639.
    • (2004) J Cell Sci , vol.117 , pp. 2631-2639
    • Rescher, U.1    Gerke, V.2
  • 4
    • 0021299594 scopus 로고
    • Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders; calcium-dependent binding to non-erythroid spectrin and F-actin
    • Gerke V, Weber K (1984) Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders; calcium-dependent binding to non-erythroid spectrin and F-actin. Embo J 3: 227-233.
    • (1984) Embo J , vol.3 , pp. 227-233
    • Gerke, V.1    Weber, K.2
  • 5
    • 0022406556 scopus 로고
    • Phosphorylation of p36 in vitro with pp60src. Regulation by Ca2+ and phospholipid
    • Glenney JR Jr (1985) Phosphorylation of p36 in vitro with pp60src. Regulation by Ca2+ and phospholipid. FEBS Lett 192: 79-82.
    • (1985) FEBS Lett , vol.192 , pp. 79-82
    • Glenney Jr, J.R.1
  • 6
    • 0022755882 scopus 로고
    • The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo
    • Gould KL, Woodgett JR, Isacke GM, Hunter T (1986) The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo. Mol Cell Biol 6: 2738-2744.
    • (1986) Mol Cell Biol , vol.6 , pp. 2738-2744
    • Gould, K.L.1    Woodgett, J.R.2    Isacke, G.M.3    Hunter, T.4
  • 7
    • 0026633683 scopus 로고
    • S100P, a novel Ca(2+)-binding protein from human placenta. cDNA cloning, recombinant protein expression and Ca2+ binding properties
    • Becker T, Gerke V, Kube E, Weber K (1992) S100P, a novel Ca(2+)-binding protein from human placenta. cDNA cloning, recombinant protein expression and Ca2+ binding properties. Eur J Biochem 207: 541-547.
    • (1992) Eur J Biochem , vol.207 , pp. 541-547
    • Becker, T.1    Gerke, V.2    Kube, E.3    Weber, K.4
  • 9
    • 0032924354 scopus 로고    scopus 로고
    • The crystal structure of a complex of p11 with die annexin II N-terminal peptide
    • Rety S, Sopkova J, Renouard M, Osterloh D, Gerke V, et al. (1999) The crystal structure of a complex of p11 with die annexin II N-terminal peptide. Nat Struct Biol 6: 89-95.
    • (1999) Nat Struct Biol , vol.6 , pp. 89-95
    • Rety, S.1    Sopkova, J.2    Renouard, M.3    Osterloh, D.4    Gerke, V.5
  • 10
    • 0027094236 scopus 로고
    • The tight association of the tyrosine kinase substrate annexin II with the submembranous cytoskeleton depends on intact p11- and Ca(2+)-Lding sites
    • Thiel C, Osborn M, Gerke V (1992) The tight association of the tyrosine kinase substrate annexin II with the submembranous cytoskeleton depends on intact p11- and Ca(2+)-Lding sites. J Cell Sci 103(Pt 3): 733-742.
    • (1992) J Cell Sci , vol.103 , Issue.PART 3 , pp. 733-742
    • Thiel, C.1    Osborn, M.2    Gerke, V.3
  • 11
    • 0027426724 scopus 로고
    • The subcellular distribution of early endosomes is affected by the annexin II2p11(2) complex
    • Harder T, Gerke V (1993) The subcellular distribution of early endosomes is affected by the annexin II2p11(2) complex. J Cell Biol 123: 1119-1132.
    • (1993) J Cell Biol , vol.123 , pp. 1119-1132
    • Harder, T.1    Gerke, V.2
  • 12
    • 0344012479 scopus 로고    scopus 로고
    • The annexin 2/S100A10 complex controls the distribution of transferrin receptor-containing recycling endosomes
    • Zobiack N, Rescher U, Ludwig C, Zeuschner D, Gerke V (2003) The annexin 2/S100A10 complex controls the distribution of transferrin receptor-containing recycling endosomes. Mol Biol Cell 14: 4896-4908.
    • (2003) Mol Biol Cell , vol.14 , pp. 4896-4908
    • Zobiack, N.1    Rescher, U.2    Ludwig, C.3    Zeuschner, D.4    Gerke, V.5
  • 14
    • 1842784049 scopus 로고    scopus 로고
    • The biogenesis of multivesicular endosomes
    • Gruenberg J, Stenmark H (2004) The biogenesis of multivesicular endosomes. Nat Rev Mol Cell Biol 5: 317-323.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 317-323
    • Gruenberg, J.1    Stenmark, H.2
  • 15
    • 0037926403 scopus 로고    scopus 로고
    • Annexin II regulates multivesicular endosome biogenesis in the degradation pathway of animal cells
    • Mayran N, Parton RG, Gruenberg J (2003) Annexin II regulates multivesicular endosome biogenesis in the degradation pathway of animal cells. Embo J 22: 3242-3253.
    • (2003) Embo J , vol.22 , pp. 3242-3253
    • Mayran, N.1    Parton, R.G.2    Gruenberg, J.3
  • 16
    • 0027457754 scopus 로고
    • Annexin II is a major component of fusogenic endosomal vesicles
    • Emans N, Gorvel JP, Walter C, Gerke V, Kellner R, et al. (1993) Annexin II is a major component of fusogenic endosomal vesicles. J Cell Biol 120: 1357-1369.
    • (1993) J Cell Biol , vol.120 , pp. 1357-1369
    • Emans, N.1    Gorvel, J.P.2    Walter, C.3    Gerke, V.4    Kellner, R.5
  • 17
    • 0031038664 scopus 로고    scopus 로고
    • Identification and characterization of a novel type of annexin-membrane interaction: Ca2+ is not required for the association of annexin II with early endosomes
    • Jost M, Zeuschner D, Seemann J, Weber K, Gerke V (1997) Identification and characterization of a novel type of annexin-membrane interaction: Ca2+ is not required for the association of annexin II with early endosomes. J Cell Sci 110(Pt 2): 221-228.
    • (1997) J Cell Sci , vol.110 , Issue.PART 2 , pp. 221-228
    • Jost, M.1    Zeuschner, D.2    Seemann, J.3    Weber, K.4    Gerke, V.5
  • 18
    • 0030899412 scopus 로고    scopus 로고
    • Specific release of membrane-bound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol
    • Harder T, Kellner R, Parton RG, Gruenberg J (1997) Specific release of membrane-bound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol. Mol Biol Cell 8: 533-545.
    • (1997) Mol Biol Cell , vol.8 , pp. 533-545
    • Harder, T.1    Kellner, R.2    Parton, R.G.3    Gruenberg, J.4
  • 19
    • 0034471239 scopus 로고    scopus 로고
    • Intact Ca(2+)-binding sites are required for targeting of annexin 1 to endosomal membranes in living HeLa cells
    • Rescher U, Zobiack N, Gerke V (2000) Intact Ca(2+)-binding sites are required for targeting of annexin 1 to endosomal membranes in living HeLa cells. J Cell Sci 113(Pt 22) 3931-3938.
    • (2000) J Cell Sci , vol.113 , Issue.PART 22 , pp. 3931-3938
    • Rescher, U.1    Zobiack, N.2    Gerke, V.3
  • 20
    • 0027730175 scopus 로고
    • Cytoplasmic dynein-dependent vesicular transport from early to late endosomes
    • Aniento F, Emans N, Griffiths G, Gruenberg J (1993) Cytoplasmic dynein-dependent vesicular transport from early to late endosomes. J Cell Biol 123: 1373-1387.
    • (1993) J Cell Biol , vol.123 , pp. 1373-1387
    • Aniento, F.1    Emans, N.2    Griffiths, G.3    Gruenberg, J.4
  • 21
    • 0023801519 scopus 로고
    • A discontinuous epitope on p36, the major substrate of src tyrosine-protein-kinase, brings the phosphorylation site into the neighbourhood of a consensus sequence for Ca2+/lipid-binding proteins
    • Johnsson N, Johnsson K, Weber K (1988) A discontinuous epitope on p36, the major substrate of src tyrosine-protein-kinase, brings the phosphorylation site into the neighbourhood of a consensus sequence for Ca2+/lipid-binding proteins. FEBS Lett 236: 201-204.
    • (1988) FEBS Lett , vol.236 , pp. 201-204
    • Johnsson, N.1    Johnsson, K.2    Weber, K.3
  • 22
    • 0023897690 scopus 로고
    • The submembranous location of p11 and its interaction with the p36 substrate of pp60 src kinase in situ
    • Osborn M, Johnsson N, Wehland J, Weber K (1988) The submembranous 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
  • 23
    • 0025797231 scopus 로고
    • Characterization of a discontinuous epitope on annexin II by site-directed mutagenesis
    • Thiel C, Weber K, 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
  • 24
    • 0034208540 scopus 로고    scopus 로고
    • Both calmodulin and the unconventional myosin Myr4 regulate membrane trafficking along the recycling pathway of MDCK cells
    • Huber LA, Fialka I, Paiha K, Hunziker W, Sacks DB, et al. (2000) Both calmodulin and the unconventional myosin Myr4 regulate membrane trafficking along the recycling pathway of MDCK cells. Traffic 1: 494-503.
    • (2000) Traffic , vol.1 , pp. 494-503
    • Huber, L.A.1    Fialka, I.2    Paiha, K.3    Hunziker, W.4    Sacks, D.B.5
  • 26
    • 0141433284 scopus 로고    scopus 로고
    • (20103) PI3P signaling regulates receptor sorting but not transport in the endosomal pathway
    • Petiot A, Faure J, Stenmark H, Gruenberg J (20103) PI3P signaling regulates receptor sorting but not transport in the endosomal pathway. J Cell Biol 162: 971-979.
    • J Cell Biol , vol.162 , pp. 971-979
    • Petiot, A.1    Faure, J.2    Stenmark, H.3    Gruenberg, J.4
  • 27
    • 0026452240 scopus 로고
    • The annexins and exocytosis
    • Creutz CE (1992) The annexins and exocytosis. Science 258: 924-931.
    • (1992) Science , vol.258 , pp. 924-931
    • Creutz, C.E.1
  • 28
    • 0035943011 scopus 로고    scopus 로고
    • Annexin 2 has an essential role in actin-baied macropinocytic rocketing
    • Merrifield CJ, Recher U, Almers W, Proust J, Gerke V, et al. (2001) Annexin 2 has an essential role in actin-baied macropinocytic rocketing. Curr Biol 11: 1136-1141.
    • (2001) Curr Biol , vol.11 , pp. 1136-1141
    • Merrifield, C.J.1    Recher, U.2    Almers, W.3    Proust, J.4    Gerke, V.5
  • 29
    • 0347753248 scopus 로고    scopus 로고
    • AHNAK interaction with the annexin 2/S100A10 complex regulates cell membrane cytoarchitecture
    • Benaud C, Gentil BJ, Assard N, Court M, Garin J, et al. (2004) AHNAK interaction with the annexin 2/S100A10 complex regulates cell membrane cytoarchitecture. J Cell Biol 164: 133-144.
    • (2004) J Cell Biol , vol.164 , pp. 133-144
    • Benaud, C.1    Gentil, B.J.2    Assard, N.3    Court, M.4    Garin, J.5
  • 30
    • 0030849323 scopus 로고    scopus 로고
    • Annexin I targets S100C to early endosomes
    • Seemann J, Weber K, Gerke V (1997) Annexin I targets S100C to early endosomes. FEBS Let 413: 185-190.
    • (1997) FEBS Let , vol.413 , pp. 185-190
    • Seemann, J.1    Weber, K.2    Gerke, V.3
  • 31
    • 0025678441 scopus 로고
    • Protein-protein recognition via short amphiphilic helices; a mutational analysis of the binding site of annexin II for p11
    • Becker T, Weber K, Johnsson N (1990) Protein-protein recognition via short amphiphilic helices; a mutational analysis of the binding site of annexin II for p11. Embo J 9: 4207-4213.
    • (1990) Embo J , vol.9 , pp. 4207-4213
    • Becker, T.1    Weber, K.2    Johnsson, N.3
  • 32
    • 0024062670 scopus 로고
    • p36, the major cytoplasmic substrate of src tyrosine protein kinase, binds to its p11 regulatory subunit via a short amino-terminal amphiphatic helix
    • Johnsson N, Marriott G, Weber K (1988) p36, the major cytoplasmic substrate of src tyrosine protein kinase, binds to its p11 regulatory subunit via a short amino-terminal amphiphatic helix. Embo J 7: 2435-2442.
    • (1988) Embo J , vol.7 , pp. 2435-2442
    • Johnsson, N.1    Marriott, G.2    Weber, K.3
  • 33
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • McMahon HT, Gallop JL (2005) Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature 438: 590-596.
    • (2005) Nature , vol.438 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 34
    • 11144353714 scopus 로고    scopus 로고
    • Annexin 2 binding to phosphatidylinositol 4,5-bisphosphate on endocytic vesicles is regulated by the stress response pathway
    • Hayes MJ, Merrifield CJ, Shan D, Ayala-Sanmartin J, Schorey CD, et al. (2004) Annexin 2 binding to phosphatidylinositol 4,5-bisphosphate on endocytic vesicles is regulated by the stress response pathway. J Biol Chem 279: 14157-14164.
    • (2004) J Biol Chem , vol.279 , pp. 14157-14164
    • Hayes, M.J.1    Merrifield, C.J.2    Shan, D.3    Ayala-Sanmartin, J.4    Schorey, C.D.5
  • 35
    • 3242887228 scopus 로고    scopus 로고
    • Annexin 2 is a phosphatidylinositol (4,5)-bisphosphate binding protein recruited to actin assembly sites at cellular membranes
    • Rescher U, Ruhe D, Ludwig C, Zobiack N, Gerke V (2004) Annexin 2 is a phosphatidylinositol (4,5)-bisphosphate binding protein recruited to actin assembly sites at cellular membranes. J Cell Sci 117: 3473-3480.
    • (2004) J Cell Sci , vol.117 , pp. 3473-3480
    • Rescher, U.1    Ruhe, D.2    Ludwig, C.3    Zobiack, N.4    Gerke, V.5
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.