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Volumn 355, Issue 1-2, 2011, Pages 47-55

Phosphorylation of human small heat shock protein HspB8 (Hsp22) by ERK1 protein kinase

Author keywords

Chaperone like activity; Human small heat shock protein HspB8; Phosphorylation; Structure

Indexed keywords

HEAT SHOCK PROTEIN 22; MITOGEN ACTIVATED PROTEIN KINASE 3; PROTEIN SUBUNIT; SERINE; THREONINE;

EID: 80051546725     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-011-0837-y     Document Type: Article
Times cited : (20)

References (32)
  • 1
    • 27144448839 scopus 로고    scopus 로고
    • Some like it hot: The structure and function of small heat-shock proteins
    • DOI 10.1038/nsmb993, PII N993
    • M Haslbeck T Franzmann D Weinfurtner J Buchner 2005 Some like it hot: the structure and function of small heat-shock proteins Nat Struct Mol Biol 12 10 842 846 16205709 10.1038/nsmb993 1:CAS:528:DC%2BD2MXhtVKnsrjF (Pubitemid 41486706)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.10 , pp. 842-846
    • Haslbeck, M.1    Franzmann, T.2    Weinfurtner, D.3    Buchner, J.4
  • 2
    • 77957841871 scopus 로고    scopus 로고
    • Independent evolution of the core domain and its flanking sequences in small heat shock proteins
    • 20501794 10.1096/fj.10-156992 1:CAS:528:DC%2BC3cXht12isLbM
    • T Kriehuber T Rattei T Weinmaier A Bepperling M Haslbeck J Buchner 2010 Independent evolution of the core domain and its flanking sequences in small heat shock proteins FASEB J 24 10 3633 3642 20501794 10.1096/fj.10-156992 1:CAS:528:DC%2BC3cXht12isLbM
    • (2010) FASEB J , vol.24 , Issue.10 , pp. 3633-3642
    • Kriehuber, T.1    Rattei, T.2    Weinmaier, T.3    Bepperling, A.4    Haslbeck, M.5    Buchner, J.6
  • 3
    • 29144527460 scopus 로고    scopus 로고
    • Small heat shock proteins: Molecular structure and chaperone function
    • DOI 10.1007/s00018-005-5190-4
    • Y Sun TH MacRae 2005 Small heat shock proteins: molecular structure and chaperone function Cell Mol Life Sci 62 21 2460 2476 16143830 10.1007/s00018-005-5190-4 1:CAS:528:DC%2BD2MXht1ynsL7E (Pubitemid 41801099)
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.21 , pp. 2460-2476
    • Sun, Y.1    MacRae, T.H.2
  • 4
    • 46849116411 scopus 로고    scopus 로고
    • Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families
    • DOI 10.1021/bi800639z
    • MJ Vos J Hageman S Carra HH Kampinga 2008 Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families Biochemistry 47 27 7001 7011 18557634 10.1021/bi800639z 1:CAS:528:DC%2BD1cXnt1Wjt7k%3D (Pubitemid 351956349)
    • (2008) Biochemistry , vol.47 , Issue.27 , pp. 7001-7011
    • Vos, M.J.1    Hageman, J.2    Carra, S.3    Kampinga, H.H.4
  • 5
    • 84934439863 scopus 로고    scopus 로고
    • The cellular "networking" of mammalian Hsp27 and its functions in the control of protein folding, redox state and apoptosis
    • 17205671 10.1007/978-0-387-39975-12
    • AP Arrigo 2007 The cellular "networking" of mammalian Hsp27 and its functions in the control of protein folding, redox state and apoptosis Adv Exp Med Biol 594 14 26 17205671 10.1007/978-0-387-39975-1-2
    • (2007) Adv Exp Med Biol , vol.594 , pp. 14-26
    • Arrigo, A.P.1
  • 6
    • 0037359564 scopus 로고    scopus 로고
    • The sperm outer dense fiber protein is the 10th member of the superfamily of mammalian small stress proteins
    • DOI 10.1379/1466-1268(2003)8<62:TSODFP>2.0.CO;2
    • JM Fontaine JS Rest MJ Welsh R Benndorf 2003 The sperm outer dense fiber protein is the 10th member of the superfamily of mammalian small stress proteins Cell Stress Chaperon 8 1 62 69 10.1379/1466-1268(2003)8<62:TSODFP>2.0. CO;2 1:CAS:528:DC%2BD3sXjsFWjsL8%3D (Pubitemid 36444091)
    • (2003) Cell Stress and Chaperones , vol.8 , Issue.1 , pp. 62-69
    • Fontaine, J.-M.1    Rest, J.S.2    Welsh, M.J.3    Benndorf, R.4
  • 7
    • 0037358061 scopus 로고    scopus 로고
    • The human genome encodes 10 α-crystallin-related small heat shock proteins: HspB1-10
    • DOI 10.1379/1466-1268(2003)8<53:THGECS>2.0.CO;2
    • G Kappe E Franck P Verschuure WC Boelens JA Leunissen WW de Jong 2003 The human genome encodes 10 alpha-crystallin-related small heat shock proteins: HspB1-10 Cell Stress Chaperon 8 1 53 61 10.1379/1466-1268(2003)8<53: THGECS>2.0.CO;2 1:CAS:528:DC%2BD3sXjsFWjsL4%3D (Pubitemid 36444090)
    • (2003) Cell Stress and Chaperones , vol.8 , Issue.1 , pp. 53-61
    • Kappe, G.1    Franck, E.2    Verschuure, P.3    Boelens, W.C.4    Leunissen, J.A.M.5    De Jong, W.W.6
  • 8
    • 0033516660 scopus 로고    scopus 로고
    • Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor by phosphorylation
    • DOI 10.1074/jbc.274.27.18947
    • T Rogalla M Ehrnsperger X Preville A Kotlyarov G Lutsch C Ducasse C Paul M Wieske AP Arrigo J Buchner M Gaestel 1999 Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation J Biol Chem 274 27 18947 18956 10383393 10.1074/jbc.274.27.18947 1:CAS:528:DyaK1MXksVWlsrY%3D (Pubitemid 29314087)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.27 , pp. 18947-18956
    • Rogalla, T.1    Ehrnsperger, M.2    Preville, X.3    Kotlyarov, A.4    Lutsch, G.5    Ducasse, C.6    Paul, C.7    Wieske, M.8    Arrigo, A.-P.9    Buchner, J.10    Gaestel, M.11
  • 9
    • 0036556697 scopus 로고    scopus 로고
    • Actin cytoskeleton and small heat shock proteins: How do they interact?
    • DOI 10.1379/1466-1268(2002)007<0167:ACASHS>2.0.CO;2
    • N Mounier AP Arrigo 2002 Actin cytoskeleton and small heat shock proteins: how do they interact? Cell Stress Chaperon 7 2 167 176 10.1379/1466-1268(2002)007<0167:ACASHS>2.0.CO;2 1:CAS:528: DC%2BD38XptV2gsL0%3D (Pubitemid 36133467)
    • (2002) Cell Stress and Chaperones , vol.7 , Issue.2 , pp. 167-176
    • Mounier, N.1    Arrigo, A.-P.2
  • 10
    • 42049123241 scopus 로고    scopus 로고
    • Small heat shock protein Hsp27 protects myosin S1 from heat-induced aggregation, but not from thermal denaturation and ATPase inactivation
    • 18387368 10.1016/j.febslet.2008.03.035 1:CAS:528:DC%2BD1cXkvVOiur4%3D
    • DI Markov AV Pivovarova IS Chernik NB Gusev DI Levitsky 2008 Small heat shock protein Hsp27 protects myosin S1 from heat-induced aggregation, but not from thermal denaturation and ATPase inactivation FEBS Lett 582 10 1407 1412 18387368 10.1016/j.febslet.2008.03.035 1:CAS:528:DC%2BD1cXkvVOiur4%3D
    • (2008) FEBS Lett , vol.582 , Issue.10 , pp. 1407-1412
    • Markov, D.I.1    Pivovarova, A.V.2    Chernik, I.S.3    Gusev, N.B.4    Levitsky, D.I.5
  • 11
    • 3142543752 scopus 로고    scopus 로고
    • Phosphorylation of αB-crystallin alters chaperone function through loss of dimeric substructure
    • DOI 10.1074/jbc.M403348200
    • JA Aquilina JL Benesch LL Ding O Yaron J Horwitz CV Robinson 2004 Phosphorylation of alphaB-crystallin alters chaperone function through loss of dimeric substructure J Biol Chem 279 27 28675 28680 15117944 10.1074/jbc.M403348200 1:CAS:528:DC%2BD2cXlt1CksLk%3D (Pubitemid 38900151)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.27 , pp. 28675-28680
    • Aquilina, J.A.1    Benesch, J.L.P.2    Ding, L.L.3    Yaron, O.4    Horwitz, J.5    Robinson, C.V.6
  • 14
    • 0035920143 scopus 로고    scopus 로고
    • HSP22, a new member of the small heat shock protein superfamily, interacts with mimic of phosphorylated HSP27 ((3D)HSP27)
    • 11342557 10.1074/jbc.M103001200 1:CAS:528:DC%2BD3MXlsV2jsLg%3D
    • R Benndorf X Sun RR Gilmont KJ Biederman MP Molloy CW Goodmurphy H Cheng PC Andrews MJ Welsh 2001 HSP22, a new member of the small heat shock protein superfamily, interacts with mimic of phosphorylated HSP27 ((3D)HSP27) J Biol Chem 276 29 26753 26761 11342557 10.1074/jbc.M103001200 1:CAS:528: DC%2BD3MXlsV2jsLg%3D
    • (2001) J Biol Chem , vol.276 , Issue.29 , pp. 26753-26761
    • Benndorf, R.1    Sun, X.2    Gilmont, R.R.3    Biederman, K.J.4    Molloy, M.P.5    Goodmurphy, C.W.6    Cheng, H.7    Andrews, P.C.8    Welsh, M.J.9
  • 16
    • 44449124267 scopus 로고    scopus 로고
    • Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis
    • 18220336 10.1021/pr0705441 1:CAS:528:DC%2BD1cXhtFamsLo%3D
    • GT Cantin W Yi B Lu SK Park T Xu JD Lee JR Yates 3rd 2008 Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis J Proteome Res 7 3 1346 1351 18220336 10.1021/pr0705441 1:CAS:528:DC%2BD1cXhtFamsLo%3D
    • (2008) J Proteome Res , vol.7 , Issue.3 , pp. 1346-1351
    • Cantin, G.T.1    Yi, W.2    Lu, B.3    Park, S.K.4    Xu, T.5    Lee, J.D.6    Yates III, J.R.7
  • 18
    • 40649120772 scopus 로고    scopus 로고
    • Phosphorylation by cyclic AMP-dependent protein kinase inhibits chaperone-like activity of human HSP22 in vitro
    • DOI 10.1007/s10541-008-2012-y
    • AA Shemetov AS Seit-Nebi OV Bukach NB Gusev 2008 Phosphorylation by cyclic AMP-dependent protein kinase inhibits chaperone-like activity of human HSP22 in vitro Biochemistry (Mosc) 73 2 200 208 10.1134/S0006297908020120 1:CAS:528:DC%2BD1cXjt1Sntbg%3D (Pubitemid 351374349)
    • (2008) Biochemistry (Moscow) , vol.73 , Issue.2 , pp. 200-208
    • Shemetov, A.A.1    Seit-Nebi, A.S.2    Bukach, O.V.3    Gusev, N.B.4
  • 19
    • 35448989800 scopus 로고    scopus 로고
    • Effect of mutations in the β5-β7 loop on the structure and properties of human small heat shock protein HSP22 (HspB8, H11)
    • DOI 10.1111/j.1742-4658.2007.06086.x
    • AS Kasakov OV Bukach AS Seit-Nebi SB Marston NB Gusev 2007 Effect of mutations in the beta5-beta7 loop on the structure and properties of human small heat shock protein HSP22 (HspB8, H11) FEBS J 274 21 5628 5642 17922839 10.1111/j.1742-4658.2007.06086.x 1:CAS:528:DC%2BD2sXhtlSksrnP (Pubitemid 47622077)
    • (2007) FEBS Journal , vol.274 , Issue.21 , pp. 5628-5642
    • Kasakov, A.S.1    Bukach, O.V.2    Seit-Nebi, A.S.3    Marston, S.B.4    Gusev, N.B.5
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 5432063 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • UK Laemmli 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 5259 680 685 5432063 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0014629135 scopus 로고
    • The relaxing protein system of striated muscle. Resolution of the troponin complex into inhibitory and calcium ion-sensitizing factors and their relationship to tropomyosin
    • 4243353 1:CAS:528:DyaE3cXmt1KmtQ%3D%3D
    • MC Schaub SV Perry 1969 The relaxing protein system of striated muscle. Resolution of the troponin complex into inhibitory and calcium ion-sensitizing factors and their relationship to tropomyosin Biochem J 115 5 993 1004 4243353 1:CAS:528:DyaE3cXmt1KmtQ%3D%3D
    • (1969) Biochem J , vol.115 , Issue.5 , pp. 993-1004
    • Schaub, M.C.1    Perry, S.V.2
  • 22
    • 0036707991 scopus 로고    scopus 로고
    • Modern analytical ultracentrifugation in protein science: A tutorial review
    • DOI 10.1110/ps.0207702
    • J Lebowitz MS Lewis P Schuck 2002 Modern analytical ultracentrifugation in protein science: a tutorial review Protein Sci 11 9 2067 2079 12192063 10.1110/ps.0207702 1:CAS:528:DC%2BD38XmslCjurg%3D (Pubitemid 34919611)
    • (2002) Protein Science , vol.11 , Issue.9 , pp. 2067-2079
    • Lebowitz, J.1    Lewis, M.S.2    Schuck, P.3
  • 23
    • 0025888298 scopus 로고
    • Identification of substrate recognition determinants for human ERK1 and ERK2 protein kinases
    • FA Gonzalez DL Raden RJ Davis 1991 Identification of substrate recognition determinants for human ERK1 and ERK2 protein kinases J Biol Chem 266 33 22159 22163 1939237 1:CAS:528:DyaK38XlsVeitA%3D%3D (Pubitemid 21908629)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.33 , pp. 22159-22163
    • Gonzalez, F.A.1    Raden, D.L.2    Davis, R.J.3
  • 24
    • 4644245263 scopus 로고    scopus 로고
    • Identification of major ERK-related phosphorylation sites in Gab1
    • DOI 10.1021/bi049753e
    • S Lehr J Kotzka H Avci A Sickmann HE Meyer A Herkner D Muller-Wieland 2004 Identification of major ERK-related phosphorylation sites in Gab1 Biochemistry 43 38 12133 12140 15379552 10.1021/bi049753e 1:CAS:528: DC%2BD2cXntVyis7o%3D (Pubitemid 39280557)
    • (2004) Biochemistry , vol.43 , Issue.38 , pp. 12133-12140
    • Lehr, S.1    Kotzka, J.2    Avci, H.3    Sickmann, A.4    Meyer, H.E.5    Herkner, A.6    Muller-Wieland, D.7
  • 26
    • 0033572811 scopus 로고    scopus 로고
    • The self-association of protein SV-IV and its possible functional implications
    • DOI 10.1046/j.1432-1327.1999.00944.x
    • P Stiuso S Metafora AM Facchiano G Colonna R Ragone 1999 The self-association of protein SV-IV and its possible functional implications Eur J Biochem 266 3 1029 1035 10583398 10.1046/j.1432-1327.1999.00944.x 1:CAS:528:DC%2BD3cXltFai (Pubitemid 30010121)
    • (1999) European Journal of Biochemistry , vol.266 , Issue.3 , pp. 1029-1035
    • Stiuso, P.1    Metafora, S.2    Facchiano, A.M.3    Colonna, G.4    Ragone, R.5
  • 27
    • 0037022171 scopus 로고    scopus 로고
    • Conformational change coupling the dimerization and activation of KSHV protease
    • DOI 10.1021/bi011753g
    • TR Pray KK Reiling BG Demirjian CS Craik 2002 Conformational change coupling the dimerization and activation of KSHV protease Biochemistry 41 5 1474 1482 11814340 10.1021/bi011753g 1:CAS:528:DC%2BD38Xis1yjtg%3D%3D (Pubitemid 34112736)
    • (2002) Biochemistry , vol.41 , Issue.5 , pp. 1474-1482
    • Pray, T.R.1    Reiling, K.K.2    Demirjian, B.G.3    Craik, C.S.4
  • 28
    • 68049128255 scopus 로고    scopus 로고
    • Analysis of secondary structure and self-assembly of amelogenin by variable temperature circular dichroism and isothermal titration calorimetry
    • 19274734 10.1002/prot.22369 1:CAS:528:DC%2BD1MXns1ertrY%3D
    • R Lakshminarayanan I Yoon BG Hegde D Fan C Du J Moradian-Oldak 2009 Analysis of secondary structure and self-assembly of amelogenin by variable temperature circular dichroism and isothermal titration calorimetry Proteins 76 3 560 569 19274734 10.1002/prot.22369 1:CAS:528:DC%2BD1MXns1ertrY%3D
    • (2009) Proteins , vol.76 , Issue.3 , pp. 560-569
    • Lakshminarayanan, R.1    Yoon, I.2    Hegde, B.G.3    Fan, D.4    Du, C.5    Moradian-Oldak, J.6
  • 29
    • 70350185414 scopus 로고    scopus 로고
    • Thermally induced structural changes of intrinsically disordered small heat shock protein Hsp22
    • 19783089 10.1016/j.bpc.2009.09.003 1:CAS:528:DC%2BD1MXhtlWitrvM
    • AS Kazakov DI Markov NB Gusev DI Levitsky 2009 Thermally induced structural changes of intrinsically disordered small heat shock protein Hsp22 Biophys Chem 145 2-3 79 85 19783089 10.1016/j.bpc.2009.09.003 1:CAS:528:DC%2BD1MXhtlWitrvM
    • (2009) Biophys Chem , vol.145 , Issue.23 , pp. 79-85
    • Kazakov, A.S.1    Markov, D.I.2    Gusev, N.B.3    Levitsky, D.I.4
  • 30
    • 0029160776 scopus 로고
    • Terminal marking of triosephosphate isomerase: Consequences of deamidation
    • 7574709 10.1006/abbi.1995.1476 1:CAS:528:DyaK2MXosVGhurg%3D
    • AQ Sun KU Yuksel RW Gracy 1995 Terminal marking of triosephosphate isomerase: consequences of deamidation Arch Biochem Biophys 322 2 361 368 7574709 10.1006/abbi.1995.1476 1:CAS:528:DyaK2MXosVGhurg%3D
    • (1995) Arch Biochem Biophys , vol.322 , Issue.2 , pp. 361-368
    • Sun, A.Q.1    Yuksel, K.U.2    Gracy, R.W.3
  • 31
    • 1342334759 scopus 로고    scopus 로고
    • Interaction of Human HSP22 (HSPB8) with Other Small Heat Shock Proteins
    • DOI 10.1074/jbc.M311324200
    • X Sun JM Fontaine JS Rest EA Shelden MJ Welsh R Benndorf 2004 Interaction of human HSP22 (HSPB8) with other small heat shock proteins J Biol Chem 279 4 2394 2402 14594798 10.1074/jbc.M311324200 1:CAS:528:DC%2BD2cXkslOlsg%3D%3D (Pubitemid 38114222)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.4 , pp. 2394-2402
    • Sun, X.1    Fontaine, J.-M.2    Rest, J.S.3    Shelden, E.A.4    Welsh, M.J.5    Benndorf, R.6
  • 32
    • 2542451125 scopus 로고    scopus 로고
    • 2-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27
    • DOI 10.1074/jbc.M402325200
    • JR Theriault H Lambert AT Chavez-Zobel G Charest P Lavigne J Landry 2004 Essential role of the NH2-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27 J Biol Chem 279 22 23463 23471 15033973 10.1074/jbc.M402325200 1:CAS:528:DC%2BD2cXkt1GitL8%3D (Pubitemid 38685657)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.22 , pp. 23463-23471
    • Theriault, J.R.1    Lambert, H.2    Chavez-Zobel, A.T.3    Charest, G.4    Lavigne, P.5    Landry, J.6


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