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Volumn 455, Issue 4, 2008, Pages 575-582

S100A10/p11: Family, friends and functions

Author keywords

Cytosolic calcium; Ion channel modulation; Receptor; Transport; TRP channels

Indexed keywords

AMINO ACID; LIPOCORTIN 2;

EID: 36349028713     PISSN: 00316768     EISSN: 14322013     Source Type: Journal    
DOI: 10.1007/s00424-007-0313-4     Document Type: Review
Times cited : (158)

References (57)
  • 2
    • 0013844612 scopus 로고
    • A soluble protein characteristic of the nervous system
    • Moore B (1965) A soluble protein characteristic of the nervous system. Biochem Biophys Res Commun 19:739-744
    • (1965) Biochem Biophys Res Commun , vol.19 , pp. 739-744
    • Moore, B.1
  • 3
    • 4444371768 scopus 로고    scopus 로고
    • S100 proteins in mouse and man: From evolution to function and pathology (including an update of the nomenclature)
    • Marenholz I, Heizmann CW, Fritz G (2004) S100 proteins in mouse and man: from evolution to function and pathology (including an update of the nomenclature). Biochem Biophys Res Commun 322:1111-1122
    • (2004) Biochem Biophys Res Commun , vol.322 , pp. 1111-1122
    • Marenholz, I.1    Heizmann, C.W.2    Fritz, G.3
  • 4
    • 0034995073 scopus 로고    scopus 로고
    • S100: A multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles
    • Donato R (2001) S100: a multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles. Int J Biochem Cell Biol 33:637-668
    • (2001) Int J Biochem Cell Biol , vol.33 , pp. 637-668
    • Donato, R.1
  • 6
    • 33744782044 scopus 로고    scopus 로고
    • Calcium-dependent and -independent interactions of the S100 protein family
    • Santamaria-Kisiel L, Rintala-Dempsey AC, Shaw GS (2006) Calcium-dependent and -independent interactions of the S100 protein family. Biochem J 396:201-214
    • (2006) Biochem J , vol.396 , pp. 201-214
    • Santamaria-Kisiel, L.1    Rintala-Dempsey, A.C.2    Shaw, G.S.3
  • 7
    • 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
  • 8
    • 0022157945 scopus 로고
    • The regulatory chain in the p36-kd substrate complex of viral tyrosine-specific protein kinases is related in sequence to the S-100 protein of glial cells
    • Gerke V, Weber K (1985) The regulatory chain in the p36-kd substrate complex of viral tyrosine-specific protein kinases is related in sequence to the S-100 protein of glial cells. EMBO J 4:2917-2920
    • (1985) EMBO J , vol.4 , pp. 2917-2920
    • Gerke, V.1    Weber, K.2
  • 9
    • 0001171815 scopus 로고
    • Amino-terminal sequence of p36 and associated p10: Identification of the site of tyrosine phosphorylation and homology with S-100
    • Glenney JR Jr, Tack BF (1985) Amino-terminal sequence of p36 and associated p10: identification of the site of tyrosine phosphorylation and homology with S-100. Proc Natl Acad Sci USA 82:7884-7888
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 7884-7888
    • Glenney Jr., J.R.1    Tack, B.F.2
  • 10
    • 0023645241 scopus 로고
    • CDNA sequence and tissue distribution of the mRNA for bovine and murine p11, the S100-related light chain of the protein-tyrosine kinase substrate p36 (calpactin I)
    • Saris CJ, Kristensen T, D'Eustachio P, Hicks LJ, Noonan DJ, Hunter T, Tack BF (1987) cDNA sequence and tissue distribution of the mRNA for bovine and murine p11, the S100-related light chain of the protein-tyrosine kinase substrate p36 (calpactin I). J Biol Chem 262:10663-10671
    • (1987) J Biol Chem , vol.262 , pp. 10663-10671
    • Saris, C.J.1    Kristensen, T.2    D'Eustachio, P.3    Hicks, L.J.4    Noonan, D.J.5    Hunter, T.6    Tack, B.F.7
  • 11
    • 0023600206 scopus 로고
    • The calpactin light chain is tightly linked to the cytoskeletal form of calpactin I: Studies using monoclonal antibodies to calpactin subunits
    • Zokas L, Glenney JR Jr (1987) The calpactin light chain is tightly linked to the cytoskeletal form of calpactin I: studies using monoclonal antibodies to calpactin subunits. J Cell Biol 105:2111-2121
    • (1987) J Cell Biol , vol.105 , pp. 2111-2121
    • Zokas, L.1    Glenney Jr., J.R.2
  • 12
    • 0026523298 scopus 로고
    • Cloning and characterization of the human gene encoding p11: Structural similarity to other members of the S-100 gene family
    • Harder T, Kube E, Gerke V (1992) Cloning and characterization of the human gene encoding p11: structural similarity to other members of the S-100 gene family. Gene 113:269-274
    • (1992) Gene , vol.113 , pp. 269-274
    • Harder, T.1    Kube, E.2    Gerke, V.3
  • 14
    • 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.1
  • 16
    • 0026623542 scopus 로고
    • Protein-protein interaction studied by site-directed mutagenesis. Characterization of the annexin II-binding site on p11, a member of the S100 protein family
    • Kube E, Becker T, Weber K, Gerke V (1992) Protein-protein interaction studied by site-directed mutagenesis. Characterization of the annexin II-binding site on p11, a member of the S100 protein family. J Biol Chem 267:14175-14182
    • (1992) J Biol Chem , vol.267 , pp. 14175-14182
    • Kube, E.1    Becker, T.2    Weber, K.3    Gerke, V.4
  • 19
    • 0025041899 scopus 로고
    • 2+/lipid binding proteins (annexins, calpactins, lipocortins) and its complex with P11; Molecular aspects
    • 2+/lipid binding proteins (annexins, calpactins, lipocortins) and its complex with P11; molecular aspects. Prog Clin Biol Res 349:123-133
    • (1990) Prog Clin Biol Res , vol.349 , pp. 123-133
    • Johnsson, N.1    Gerke, V.2    Weber, K.3
  • 20
    • 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
  • 21
    • 0031565732 scopus 로고    scopus 로고
    • Structural analysis of junctions formed between lipid membranes and several annexins by cryo-electron microscopy
    • Lambert O, Gerke V, Bader MF, Porte F, Brisson A (1997) Structural analysis of junctions formed between lipid membranes and several annexins by cryo-electron microscopy. J Mol Biol 272:42-55
    • (1997) J Mol Biol , vol.272 , pp. 42-55
    • Lambert, O.1    Gerke, V.2    Bader, M.F.3    Porte, F.4    Brisson, A.5
  • 22
    • 4544231736 scopus 로고    scopus 로고
    • The molecular arrangement of membrane-bound annexin A2-S100A10 tetramer as revealed by scanning force microscopy
    • Menke M, Ross M, Gerke V, Steinem C (2004) The molecular arrangement of membrane-bound annexin A2-S100A10 tetramer as revealed by scanning force microscopy. Chembiochem 5:1003-1006
    • (2004) Chembiochem , vol.5 , pp. 1003-1006
    • Menke, M.1    Ross, M.2    Gerke, V.3    Steinem, C.4
  • 23
    • 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
  • 25
    • 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
  • 27
    • 33646570263 scopus 로고    scopus 로고
    • Regulation of actin dynamics by annexin 2
    • Hayes MJ, Shao D, Bailly M, Moss SE (2006) Regulation of actin dynamics by annexin 2. EMBO J 25:1816-1826
    • (2006) EMBO J , vol.25 , pp. 1816-1826
    • Hayes, M.J.1    Shao, D.2    Bailly, M.3    Moss, S.E.4
  • 28
    • 33846270032 scopus 로고    scopus 로고
    • PTEN-mediated apical segregation of phosphoinositides controls epithelial morphogenesis through Cdc42
    • Martin-Belmonte F, Gassama A, Datta A, Yu W, Rescher U, Gerke V, Mostov K (2007) PTEN-mediated apical segregation of phosphoinositides controls epithelial morphogenesis through Cdc42. Cell 128:383-397
    • (2007) Cell , vol.128 , pp. 383-397
    • Martin-Belmonte, F.1    Gassama, A.2    Datta, A.3    Yu, W.4    Rescher, U.5    Gerke, V.6    Mostov, K.7
  • 29
    • 0030022110 scopus 로고    scopus 로고
    • Annexin II up-regulates cellular levels of p11 protein by a post-translational mechanisms
    • Pt 1
    • Puisieux A, Ji J, Ozturk M (1996) Annexin II up-regulates cellular levels of p11 protein by a post-translational mechanisms. Biochem J 313(Pt 1):51-55
    • (1996) Biochem J , vol.313 , pp. 51-55
    • Puisieux, A.1    Ji, J.2    Ozturk, M.3
  • 30
  • 31
    • 0842303212 scopus 로고    scopus 로고
    • Identification of binding domains in the sodium channel Na(V)1.8 intracellular N-terminal region and annexin II light chain p11
    • Poon WY, Malik-Hall M, Wood JN, Okuse K (2004) Identification of binding domains in the sodium channel Na(V)1.8 intracellular N-terminal region and annexin II light chain p11. FEBS Lett 558:114-118
    • (2004) FEBS Lett , vol.558 , pp. 114-118
    • Poon, W.Y.1    Malik-Hall, M.2    Wood, J.N.3    Okuse, K.4
  • 32
    • 0037009441 scopus 로고    scopus 로고
    • P11, an annexin II subunit, an auxiliary protein associated with the background K + channel, TASK-1
    • Girard C, Tinel N, Terrenoire C, Romey G, Lazdunski M, Borsotto M (2002) p11, an annexin II subunit, an auxiliary protein associated with the background K + channel, TASK-1. EMBO J 21:4439-4448
    • (2002) EMBO J , vol.21 , pp. 4439-4448
    • Girard, C.1    Tinel, N.2    Terrenoire, C.3    Romey, G.4    Lazdunski, M.5    Borsotto, M.6
  • 35
    • 33644688683 scopus 로고    scopus 로고
    • Annexin II light chain p11 promotes functional expression of acid-sensing ion channel ASIC1a
    • Donier E, Rugiero F, Okuse K, Wood JN (2005) Annexin II light chain p11 promotes functional expression of acid-sensing ion channel ASIC1a. J Biol Chem 280:38666-38672
    • (2005) J Biol Chem , vol.280 , pp. 38666-38672
    • Donier, E.1    Rugiero, F.2    Okuse, K.3    Wood, J.N.4
  • 37
    • 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, Delphin C, Baudier J (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    Delphin, C.6    Baudier, J.7
  • 39
    • 0036789972 scopus 로고    scopus 로고
    • The membrane trafficking protein calpactin forms a complex with bluetongue virus protein NS3 and mediates virus release
    • Beaton AR, Rodriguez J, Reddy YK, Roy P (2002) The membrane trafficking protein calpactin forms a complex with bluetongue virus protein NS3 and mediates virus release. Proc Natl Acad Sci USA 99:13154-13159
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13154-13159
    • Beaton, A.R.1    Rodriguez, J.2    Reddy, Y.K.3    Roy, P.4
  • 40
    • 0036479735 scopus 로고    scopus 로고
    • Annexin II: A plasminogen-plasminogen activator co-receptor
    • Kim J, Hajjar KA (2002) Annexin II: a plasminogen-plasminogen activator co-receptor. Front Biosci 7:d341-d348
    • (2002) Front Biosci , vol.7
    • Kim, J.1    Hajjar, K.A.2
  • 41
    • 17444366177 scopus 로고    scopus 로고
    • S100A10, annexin A2, and annexin a2 heterotetramer as candidate plasminogen receptors
    • Kwon M, MacLeod TJ, Zhang Y, Waisman DM (2005) S100A10, annexin A2, and annexin a2 heterotetramer as candidate plasminogen receptors. Front Biosci 10:300-325
    • (2005) Front Biosci , vol.10 , pp. 300-325
    • Kwon, M.1    MacLeod, T.J.2    Zhang, Y.3    Waisman, D.M.4
  • 42
    • 6344241866 scopus 로고    scopus 로고
    • An annexin 2 phosphorylation switch mediates p11-dependent translocation of annexin 2 to the cell surface
    • Deora AB, Kreitzer G, Jacovina AT, Hajjar KA (2004) An annexin 2 phosphorylation switch mediates p11-dependent translocation of annexin 2 to the cell surface. J Biol Chem 279:43411-43418
    • (2004) J Biol Chem , vol.279 , pp. 43411-43418
    • Deora, A.B.1    Kreitzer, G.2    Jacovina, A.T.3    Hajjar, K.A.4
  • 43
    • 18444386848 scopus 로고    scopus 로고
    • Molecular mechanisms of fibrinolysis
    • Cesarman-Maus G, Hajjar KA (2005) Molecular mechanisms of fibrinolysis. Br J Haematol 129:307-321
    • (2005) Br J Haematol , vol.129 , pp. 307-321
    • Cesarman-Maus, G.1    Hajjar, K.A.2
  • 44
    • 33644792678 scopus 로고    scopus 로고
    • Annexin A2 may not play a role as a plasminogen receptor
    • author reply 554-556
    • Waisman DM (2005) Annexin A2 may not play a role as a plasminogen receptor. Br J Haematol 131:553-554 author reply 554-556
    • (2005) Br J Haematol , vol.131 , pp. 553-554
    • Waisman, D.M.1
  • 49
    • 0037112329 scopus 로고    scopus 로고
    • Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals
    • O'Kelly I, Butler MH, Zilberberg N, Goldstein SA (2002) Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals. Cell 111:577-588
    • (2002) Cell , vol.111 , pp. 577-588
    • O'Kelly, I.1    Butler, M.H.2    Zilberberg, N.3    Goldstein, S.A.4
  • 50
    • 0346655136 scopus 로고    scopus 로고
    • Targeting of ion channels to membrane microdomains: Localization of KV channels to lipid rafts
    • Martens JR, O'Connell K, Tamkun M (2004) Targeting of ion channels to membrane microdomains: localization of KV channels to lipid rafts. Trends Pharmacol Sci 25:16-21
    • (2004) Trends Pharmacol Sci , vol.25 , pp. 16-21
    • Martens, J.R.1    O'Connell, K.2    Tamkun, M.3
  • 52
    • 29744432410 scopus 로고    scopus 로고
    • Membrane organization of the human serotonin(1A) receptor monitored by detergent insolubility using GFP fluorescence
    • Kalipatnapu S, Chattopadhyay A (2005) Membrane organization of the human serotonin(1A) receptor monitored by detergent insolubility using GFP fluorescence. Mol Membr Biol 22:539-547
    • (2005) Mol Membr Biol , vol.22 , pp. 539-547
    • Kalipatnapu, S.1    Chattopadhyay, A.2
  • 54
    • 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
  • 55
    • 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
  • 56
    • 0023054163 scopus 로고
    • Functionally distinct serine phosphorylation sites of p36, the cellular substrate of retroviral protein kinase; Differential inhibition of reassociation with p11
    • Johnsson N, Nguyen Van P, Soling HD, Weber K (1986) Functionally distinct serine phosphorylation sites of p36, the cellular substrate of retroviral protein kinase; differential inhibition of reassociation with p11. EMBO J 5:3455-3460
    • (1986) EMBO J , vol.5 , pp. 3455-3460
    • Johnsson, N.1    Nguyen Van, P.2    Soling, H.D.3    Weber, K.4
  • 57
    • 0030580041 scopus 로고    scopus 로고
    • Mapping of a regulatory important site for protein kinase C phosphorylation in the N-terminal domain of annexin II
    • Jost M, Gerke V (1996) Mapping of a regulatory important site for protein kinase C phosphorylation in the N-terminal domain of annexin II. Biochim Biophys Acta 1313:283-289
    • (1996) Biochim Biophys Acta , vol.1313 , pp. 283-289
    • Jost, M.1    Gerke, V.2


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