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Volumn 429, Issue 1, 2017, Pages 128-141

BAG3 Is a Modular, Scaffolding Protein that physically Links Heat Shock Protein 70 (Hsp70) to the Small Heat Shock Proteins

Author keywords

chaperones; Hsp27; intrinsically disordered proteins; protein folding; proteostasis

Indexed keywords

ALPHA CRYSTALLIN; BCL 2 ASSOCIATED ANTHANOGENE 3; CHAPERONE; HEAT SHOCK PROTEIN 20; HEAT SHOCK PROTEIN 22; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 70; LUCIFERASE; OLIGOMER; SCAFFOLD PROTEIN; SMALL HEAT SHOCK PROTEIN; UNCLASSIFIED DRUG; APOPTOSIS REGULATORY PROTEIN; BAG3 PROTEIN, HUMAN; PROTEIN BINDING; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 85006961032     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2016.11.013     Document Type: Article
Times cited : (107)

References (67)
  • 1
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • [1] Hartl, F.U., Bracher, A., Hayer-Hartl, M., Molecular chaperones in protein folding and proteostasis. Nature 475 (2011), 324–332.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 2
    • 59249106080 scopus 로고    scopus 로고
    • Integrating the stress response: lessons for neurodegenerative diseases from C. elegans
    • [2] Prahlad, V., Morimoto, R.I., Integrating the stress response: lessons for neurodegenerative diseases from C. elegans. Trends Cell Biol. 19 (2009), 52–61.
    • (2009) Trends Cell Biol. , vol.19 , pp. 52-61
    • Prahlad, V.1    Morimoto, R.I.2
  • 5
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery: J proteins as drivers of functional specificity
    • [5] Kampinga, H.H., Craig, E.A., The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat. Rev. Mol. Cell Biol. 11 (2010), 579–592.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 7
    • 0000012053 scopus 로고
    • Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous
    • [7] Bardwell, J.C., Craig, E.A., Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous. Proc. Natl. Acad. Sci. U. S. A. 81 (1984), 848–852.
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 848-852
    • Bardwell, J.C.1    Craig, E.A.2
  • 8
    • 0028036148 scopus 로고
    • Molecular evolution of the HSP70 multigene family
    • [8] Boorstein, W.R., Ziegelhoffer, T., Craig, E.A., Molecular evolution of the HSP70 multigene family. J. Mol. Evol. 38 (1994), 1–17.
    • (1994) J. Mol. Evol. , vol.38 , pp. 1-17
    • Boorstein, W.R.1    Ziegelhoffer, T.2    Craig, E.A.3
  • 9
    • 84948397326 scopus 로고    scopus 로고
    • Hsp70 and Hsp90 of E. coli directly interact for collaboration in protein remodeling
    • [9] Genest, O., Hoskins, J.R., Kravats, A.N., Doyle, S.M., Wickner, S., Hsp70 and Hsp90 of E. coli directly interact for collaboration in protein remodeling. J. Mol. Biol. 427 (2015), 3877–3889.
    • (2015) J. Mol. Biol. , vol.427 , pp. 3877-3889
    • Genest, O.1    Hoskins, J.R.2    Kravats, A.N.3    Doyle, S.M.4    Wickner, S.5
  • 10
    • 84896846203 scopus 로고    scopus 로고
    • Physical interaction between bacterial heat shock protein (Hsp) 90 and Hsp70 chaperones mediates their cooperative action to refold denatured proteins
    • [10] Nakamoto, H., Fujita, K., Ohtaki, A., Watanabe, S., Narumi, S., Maruyama, T., et al. Physical interaction between bacterial heat shock protein (Hsp) 90 and Hsp70 chaperones mediates their cooperative action to refold denatured proteins. J. Biol. Chem. 289 (2014), 6110–6119.
    • (2014) J. Biol. Chem. , vol.289 , pp. 6110-6119
    • Nakamoto, H.1    Fujita, K.2    Ohtaki, A.3    Watanabe, S.4    Narumi, S.5    Maruyama, T.6
  • 11
    • 84870792675 scopus 로고    scopus 로고
    • Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA + disaggregase at aggregate surfaces
    • [11] Seyffer, F., Kummer, E., Oguchi, Y., Winkler, J., Kumar, M., Zahn, R., et al. Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA + disaggregase at aggregate surfaces. Nat. Struct. Mol. Biol. 19 (2012), 1347–1355.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 1347-1355
    • Seyffer, F.1    Kummer, E.2    Oguchi, Y.3    Winkler, J.4    Kumar, M.5    Zahn, R.6
  • 12
    • 84858763945 scopus 로고    scopus 로고
    • The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop
    • [12] Schmid, A.B., Lagleder, S., Grawert, M.A., Rohl, A., Hagn, F., Wandinger, S.K., et al. The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop. EMBO J. 31 (2012), 1506–1517.
    • (2012) EMBO J. , vol.31 , pp. 1506-1517
    • Schmid, A.B.1    Lagleder, S.2    Grawert, M.A.3    Rohl, A.4    Hagn, F.5    Wandinger, S.K.6
  • 13
    • 84903149823 scopus 로고    scopus 로고
    • Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles
    • [13] Kirschke, E., Goswami, D., Southworth, D., Griffin, P.R., Agard, D.A., Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles. Cell 157 (2014), 1685–1697.
    • (2014) Cell , vol.157 , pp. 1685-1697
    • Kirschke, E.1    Goswami, D.2    Southworth, D.3    Griffin, P.R.4    Agard, D.A.5
  • 15
    • 0032488906 scopus 로고    scopus 로고
    • Hop modulates Hsp70/Hsp90 interactions in protein folding
    • [15] Johnson, B.D., Schumacher, R.J., Ross, E.D., Toft, D.O., Hop modulates Hsp70/Hsp90 interactions in protein folding. J. Biol. Chem. 273 (1998), 3679–3686.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3679-3686
    • Johnson, B.D.1    Schumacher, R.J.2    Ross, E.D.3    Toft, D.O.4
  • 17
    • 84923372470 scopus 로고    scopus 로고
    • Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop
    • [17] Alvira, S., Cuellar, J., Rohl, A., Yamamoto, S., Itoh, H., Alfonso, C., et al. Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop. Nat. Commun., 5, 2014, 5484.
    • (2014) Nat. Commun. , vol.5 , pp. 5484
    • Alvira, S.1    Cuellar, J.2    Rohl, A.3    Yamamoto, S.4    Itoh, H.5    Alfonso, C.6
  • 20
    • 1542320089 scopus 로고    scopus 로고
    • The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions
    • [20] Basha, E., Lee, G.J., Breci, L.A., Hausrath, A.C., Buan, N.R., Giese, K.C., et al. The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions. J. Biol. Chem. 279 (2004), 7566–7575.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7566-7575
    • Basha, E.1    Lee, G.J.2    Breci, L.A.3    Hausrath, A.C.4    Buan, N.R.5    Giese, K.C.6
  • 21
    • 84924126477 scopus 로고    scopus 로고
    • A first line of stress defense: small heat shock proteins and their function in protein homeostasis
    • [21] Haslbeck, M., Vierling, E., A first line of stress defense: small heat shock proteins and their function in protein homeostasis. J. Mol. Biol. 427 (2015), 1537–1548.
    • (2015) J. Mol. Biol. , vol.427 , pp. 1537-1548
    • Haslbeck, M.1    Vierling, E.2
  • 22
    • 84948073235 scopus 로고    scopus 로고
    • The chaperone alphaB-crystallin uses different interfaces to capture an amorphous and an amyloid client
    • [22] Mainz, A., Peschek, J., Stavropoulou, M., Back, K.C., Bardiaux, B., Asami, S., et al. The chaperone alphaB-crystallin uses different interfaces to capture an amorphous and an amyloid client. Nat. Struct. Mol. Biol. 22 (2015), 898–905.
    • (2015) Nat. Struct. Mol. Biol. , vol.22 , pp. 898-905
    • Mainz, A.1    Peschek, J.2    Stavropoulou, M.3    Back, K.C.4    Bardiaux, B.5    Asami, S.6
  • 23
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heat-shock protein
    • [23] Kim, K.K., Kim, R., Kim, S.H., Crystal structure of a small heat-shock protein. Nature 394 (1998), 595–599.
    • (1998) Nature , vol.394 , pp. 595-599
    • Kim, K.K.1    Kim, R.2    Kim, S.H.3
  • 25
    • 84899118154 scopus 로고    scopus 로고
    • The structured core domain of alphaB-crystallin can prevent amyloid fibrillation and associated toxicity
    • [25] Hochberg, G.K., Ecroyd, H., Liu, C., Cox, D., Cascio, D., Sawaya, M.R., et al. The structured core domain of alphaB-crystallin can prevent amyloid fibrillation and associated toxicity. Proc. Natl. Acad. Sci. U. S. A. 111 (2014), E1562–E1570.
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. E1562-E1570
    • Hochberg, G.K.1    Ecroyd, H.2    Liu, C.3    Cox, D.4    Cascio, D.5    Sawaya, M.R.6
  • 26
    • 84855480113 scopus 로고    scopus 로고
    • Multiple molecular architectures of the eye lens chaperone alphaB-crystallin elucidated by a triple hybrid approach
    • [26] Braun, N., Zacharias, M., Peschek, J., Kastenmuller, A., Zou, J., Hanzlik, M., et al. Multiple molecular architectures of the eye lens chaperone alphaB-crystallin elucidated by a triple hybrid approach. Proc. Natl. Acad. Sci. U. S. A. 108 (2011), 20491–20496.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 20491-20496
    • Braun, N.1    Zacharias, M.2    Peschek, J.3    Kastenmuller, A.4    Zou, J.5    Hanzlik, M.6
  • 27
    • 16544382615 scopus 로고    scopus 로고
    • The IXI/V motif in the C-terminal extension of alpha-crystallins: alternative interactions and oligomeric assemblies
    • [27] Pasta, S.Y., Raman, B., Ramakrishna, T., Rao Ch, M., The IXI/V motif in the C-terminal extension of alpha-crystallins: alternative interactions and oligomeric assemblies. Mol. Vis. 10 (2004), 655–662.
    • (2004) Mol. Vis. , vol.10 , pp. 655-662
    • Pasta, S.Y.1    Raman, B.2    Ramakrishna, T.3    Rao Ch, M.4
  • 28
    • 79955597623 scopus 로고    scopus 로고
    • N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity
    • [28] Jehle, S., Vollmar, B.S., Bardiaux, B., Dove, K.K., Rajagopal, P., Gonen, T., et al. N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. Proc. Natl. Acad. Sci. U. S. A. 108 (2011), 6409–6414.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 6409-6414
    • Jehle, S.1    Vollmar, B.S.2    Bardiaux, B.3    Dove, K.K.4    Rajagopal, P.5    Gonen, T.6
  • 29
    • 0036375506 scopus 로고    scopus 로고
    • A critical motif for oligomerization and chaperone activity of bacterial alpha-heat shock proteins
    • [29] Studer, S., Obrist, M., Lentze, N., Narberhaus, F., A critical motif for oligomerization and chaperone activity of bacterial alpha-heat shock proteins. Eur. J. Biochem. 269 (2002), 3578–3586.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3578-3586
    • Studer, S.1    Obrist, M.2    Lentze, N.3    Narberhaus, F.4
  • 30
    • 84878932295 scopus 로고    scopus 로고
    • Human small heat shock proteins: protein interactomes of homo- and hetero-oligomeric complexes: an update
    • [30] Arrigo, A.P., Human small heat shock proteins: protein interactomes of homo- and hetero-oligomeric complexes: an update. FEBS Lett. 587 (2013), 1959–1969.
    • (2013) FEBS Lett. , vol.587 , pp. 1959-1969
    • Arrigo, A.P.1
  • 31
    • 0033972325 scopus 로고    scopus 로고
    • Subunit exchange of small heat shock proteins. Analysis of oligomer formation of alphaA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations
    • [31] Bova, M.P., McHaourab, H.S., Han, Y., Fung, B.K., Subunit exchange of small heat shock proteins. Analysis of oligomer formation of alphaA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations. J. Biol. Chem. 275 (2000), 1035–1042.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1035-1042
    • Bova, M.P.1    McHaourab, H.S.2    Han, Y.3    Fung, B.K.4
  • 32
    • 0141703310 scopus 로고    scopus 로고
    • Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in alphaB-crystallin
    • [32] Aquilina, J.A., Benesch, J.L., Bateman, O.A., Slingsby, C., Robinson, C.V., Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in alphaB-crystallin. Proc. Natl. Acad. Sci. U. S. A. 100 (2003), 10611–10616.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 10611-10616
    • Aquilina, J.A.1    Benesch, J.L.2    Bateman, O.A.3    Slingsby, C.4    Robinson, C.V.5
  • 33
    • 84947208872 scopus 로고    scopus 로고
    • Pharmacological chaperone for alpha-crystallin partially restores transparency in cataract models
    • [33] Makley, L.N., McMenimen, K.A., DeVree, B.T., Goldman, J.W., McGlasson, B.N., Rajagopal, P., et al. Pharmacological chaperone for alpha-crystallin partially restores transparency in cataract models. Science 350 (2015), 674–677.
    • (2015) Science , vol.350 , pp. 674-677
    • Makley, L.N.1    McMenimen, K.A.2    DeVree, B.T.3    Goldman, J.W.4    McGlasson, B.N.5    Rajagopal, P.6
  • 34
    • 14044272992 scopus 로고    scopus 로고
    • Mechanism of chaperone function in small heat shock proteins: dissociation of the HSP27 oligomer is required for recognition and binding of destabilized T4 lysozyme
    • [34] Shashidharamurthy, R., Koteiche, H.A., Dong, J., McHaourab, H.S., Mechanism of chaperone function in small heat shock proteins: dissociation of the HSP27 oligomer is required for recognition and binding of destabilized T4 lysozyme. J. Biol. Chem. 280 (2005), 5281–5289.
    • (2005) J. Biol. Chem. , vol.280 , pp. 5281-5289
    • Shashidharamurthy, R.1    Koteiche, H.A.2    Dong, J.3    McHaourab, H.S.4
  • 35
    • 0037195859 scopus 로고    scopus 로고
    • Changes in oligomerization are essential for the chaperone activity of a small heat shock protein in vivo and in vitro
    • [35] Giese, K.C., Vierling, E., Changes in oligomerization are essential for the chaperone activity of a small heat shock protein in vivo and in vitro. J. Biol. Chem. 277 (2002), 46310–46318.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46310-46318
    • Giese, K.C.1    Vierling, E.2
  • 36
    • 0038043235 scopus 로고    scopus 로고
    • Analysis of the interaction of small heat shock proteins with unfolding proteins
    • [36] Stromer, T., Ehrnsperger, M., Gaestel, M., Buchner, J., Analysis of the interaction of small heat shock proteins with unfolding proteins. J. Biol. Chem. 278 (2003), 18015–18021.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18015-18021
    • Stromer, T.1    Ehrnsperger, M.2    Gaestel, M.3    Buchner, J.4
  • 37
    • 0037064096 scopus 로고    scopus 로고
    • Subunit exchange of multimeric protein complexes. Real-time monitoring of subunit exchange between small heat shock proteins by using electrospray mass spectrometry
    • [37] Sobott, F., Benesch, J.L., Vierling, E., Robinson, C.V., Subunit exchange of multimeric protein complexes. Real-time monitoring of subunit exchange between small heat shock proteins by using electrospray mass spectrometry. J. Biol. Chem. 277 (2002), 38921–38929.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38921-38929
    • Sobott, F.1    Benesch, J.L.2    Vierling, E.3    Robinson, C.V.4
  • 39
    • 84923126434 scopus 로고    scopus 로고
    • Phosphomimics destabilize Hsp27 oligomeric assemblies and enhance chaperone activity
    • [39] Jovcevski, B., Kelly, M.A., Rote, A.P., Berg, T., Gastall, H.Y., Benesch, J.L., et al. Phosphomimics destabilize Hsp27 oligomeric assemblies and enhance chaperone activity. Chem. Biol. 22 (2015), 186–195.
    • (2015) Chem. Biol. , vol.22 , pp. 186-195
    • Jovcevski, B.1    Kelly, M.A.2    Rote, A.P.3    Berg, T.4    Gastall, H.Y.5    Benesch, J.L.6
  • 41
    • 84918587127 scopus 로고    scopus 로고
    • Identification of peptides in human Hsp20 and Hsp27 that possess molecular chaperone and anti-apoptotic activities
    • [41] Nahomi, R.B., DiMauro, M.A., Wang, B., Nagaraj, R.H., Identification of peptides in human Hsp20 and Hsp27 that possess molecular chaperone and anti-apoptotic activities. Biochem. J. 465 (2015), 115–125.
    • (2015) Biochem. J. , vol.465 , pp. 115-125
    • Nahomi, R.B.1    DiMauro, M.A.2    Wang, B.3    Nagaraj, R.H.4
  • 42
    • 84867772627 scopus 로고    scopus 로고
    • HspB1 dynamic phospho-oligomeric structure dependent interactome as cancer therapeutic target
    • [42] Arrigo, A.P., Gibert, B., HspB1 dynamic phospho-oligomeric structure dependent interactome as cancer therapeutic target. Curr. Mol. Med. 12 (2012), 1151–1163.
    • (2012) Curr. Mol. Med. , vol.12 , pp. 1151-1163
    • Arrigo, A.P.1    Gibert, B.2
  • 43
    • 0031849099 scopus 로고    scopus 로고
    • Small heat-shock protein family: function in health and disease
    • [43] Welsh, M.J., Gaestel, M., Small heat-shock protein family: function in health and disease. Ann. N. Y. Acad. Sci. 851 (1998), 28–35.
    • (1998) Ann. N. Y. Acad. Sci. , vol.851 , pp. 28-35
    • Welsh, M.J.1    Gaestel, M.2
  • 44
    • 84930629588 scopus 로고    scopus 로고
    • A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis
    • [44] Rajagopal, P., Tse, E., Borst, A.J., Delbecq, S.P., Shi, L., Southworth, D.R., et al. A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis. eLife, 4, 2015.
    • (2015) eLife , vol.4
    • Rajagopal, P.1    Tse, E.2    Borst, A.J.3    Delbecq, S.P.4    Shi, L.5    Southworth, D.R.6
  • 45
    • 84937640129 scopus 로고    scopus 로고
    • The chaperone activity of the developmental small heat shock protein Sip1 is regulated by pH-dependent conformational changes
    • [45] Fleckenstein, T., Kastenmuller, A., Stein, M.L., Peters, C., Daake, M., Krause, M., et al. The chaperone activity of the developmental small heat shock protein Sip1 is regulated by pH-dependent conformational changes. Mol. Cell 58 (2015), 1067–1078.
    • (2015) Mol. Cell , vol.58 , pp. 1067-1078
    • Fleckenstein, T.1    Kastenmuller, A.2    Stein, M.L.3    Peters, C.4    Daake, M.5    Krause, M.6
  • 46
    • 84864387363 scopus 로고    scopus 로고
    • Chaperone networks in protein disaggregation and prion propagation
    • [46] Winkler, J., Tyedmers, J., Bukau, B., Mogk, A., Chaperone networks in protein disaggregation and prion propagation. J. Struct. Biol. 179 (2012), 152–160.
    • (2012) J. Struct. Biol. , vol.179 , pp. 152-160
    • Winkler, J.1    Tyedmers, J.2    Bukau, B.3    Mogk, A.4
  • 47
    • 84971433330 scopus 로고    scopus 로고
    • Heat shock proteins promote cancer: it's a protection racket
    • [47] Calderwood, S.K., Gong, J., Heat shock proteins promote cancer: it's a protection racket. Trends Biochem. Sci., 2016.
    • (2016) Trends Biochem. Sci.
    • Calderwood, S.K.1    Gong, J.2
  • 49
    • 80054740161 scopus 로고    scopus 로고
    • Nucleotide exchange factors for Hsp70 chaperones
    • [49] Rampelt, H., Mayer, M.P., Bukau, B., Nucleotide exchange factors for Hsp70 chaperones. Methods Mol. Biol. 787 (2011), 83–91.
    • (2011) Methods Mol. Biol. , vol.787 , pp. 83-91
    • Rampelt, H.1    Mayer, M.P.2    Bukau, B.3
  • 50
    • 84892653392 scopus 로고    scopus 로고
    • Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro
    • [50] Rauch, J.N., Gestwicki, J.E., Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro. J. Biol. Chem. 289 (2014), 1402–1414.
    • (2014) J. Biol. Chem. , vol.289 , pp. 1402-1414
    • Rauch, J.N.1    Gestwicki, J.E.2
  • 51
    • 77956940128 scopus 로고    scopus 로고
    • BAG3 directly associates with guanine nucleotide exchange factor of Rap1, PDZGEF2, and regulates cell adhesion
    • [51] Iwasaki, M., Tanaka, R., Hishiya, A., Homma, S., Reed, J.C., Takayama, S., BAG3 directly associates with guanine nucleotide exchange factor of Rap1, PDZGEF2, and regulates cell adhesion. Biochem. Biophys. Res. Commun. 400 (2010), 413–418.
    • (2010) Biochem. Biophys. Res. Commun. , vol.400 , pp. 413-418
    • Iwasaki, M.1    Tanaka, R.2    Hishiya, A.3    Homma, S.4    Reed, J.C.5    Takayama, S.6
  • 52
    • 84875210317 scopus 로고    scopus 로고
    • Cellular mechanotransduction relies on tension-induced and chaperone-assisted autophagy
    • [52] Ulbricht, A., Eppler, F.J., Tapia, V.E., van der Ven, P.F., Hampe, N., Hersch, N., et al. Cellular mechanotransduction relies on tension-induced and chaperone-assisted autophagy. Curr. Biol. 23 (2013), 430–435.
    • (2013) Curr. Biol. , vol.23 , pp. 430-435
    • Ulbricht, A.1    Eppler, F.J.2    Tapia, V.E.3    van der Ven, P.F.4    Hampe, N.5    Hersch, N.6
  • 53
    • 84907055560 scopus 로고    scopus 로고
    • Hsp70–Bag3 interactions regulate cancer-related signaling networks
    • [53] Colvin, T.A., Gabai, V.L., Gong, J., Calderwood, S.K., Li, H., Gummuluru, S., et al. Hsp70–Bag3 interactions regulate cancer-related signaling networks. Cancer Res. 74 (2014), 4731–4740.
    • (2014) Cancer Res. , vol.74 , pp. 4731-4740
    • Colvin, T.A.1    Gabai, V.L.2    Gong, J.3    Calderwood, S.K.4    Li, H.5    Gummuluru, S.6
  • 54
    • 0034618385 scopus 로고    scopus 로고
    • CAIR-1/BAG-3 forms an EGF-regulated ternary complex with phospholipase C-gamma and Hsp70/Hsc70
    • [54] Doong, H., Price, J., Kim, Y.S., Gasbarre, C., Probst, J., Liotta, L.A., et al. CAIR-1/BAG-3 forms an EGF-regulated ternary complex with phospholipase C-gamma and Hsp70/Hsc70. Oncogene 19 (2000), 4385–4395.
    • (2000) Oncogene , vol.19 , pp. 4385-4395
    • Doong, H.1    Price, J.2    Kim, Y.S.3    Gasbarre, C.4    Probst, J.5    Liotta, L.A.6
  • 55
    • 72449141635 scopus 로고    scopus 로고
    • Identification of the key structural motifs involved in HspB8/HspB6–Bag3 interaction
    • [55] Fuchs, M., Poirier, D.J., Seguin, S.J., Lambert, H., Carra, S., Charette, S.J., et al. Identification of the key structural motifs involved in HspB8/HspB6–Bag3 interaction. Biochem. J. 425 (2010), 245–255.
    • (2010) Biochem. J. , vol.425 , pp. 245-255
    • Fuchs, M.1    Poirier, D.J.2    Seguin, S.J.3    Lambert, H.4    Carra, S.5    Charette, S.J.6
  • 56
    • 38949184241 scopus 로고    scopus 로고
    • HspB8 and Bag3: a new chaperone complex targeting misfolded proteins to macroautophagy
    • [56] Carra, S., Seguin, S.J., Landry, J., HspB8 and Bag3: a new chaperone complex targeting misfolded proteins to macroautophagy. Autophagy 4 (2008), 237–239.
    • (2008) Autophagy , vol.4 , pp. 237-239
    • Carra, S.1    Seguin, S.J.2    Landry, J.3
  • 57
    • 79952635812 scopus 로고    scopus 로고
    • BAG3 directly interacts with mutated alphaB-crystallin to suppress its aggregation and toxicity
    • e16828
    • [57] Hishiya, A., Salman, M.N., Carra, S., Kampinga, H.H., Takayama, S., BAG3 directly interacts with mutated alphaB-crystallin to suppress its aggregation and toxicity. PLoS One, 6, 2011, e16828.
    • (2011) PLoS One , vol.6
    • Hishiya, A.1    Salman, M.N.2    Carra, S.3    Kampinga, H.H.4    Takayama, S.5
  • 59
    • 2542451125 scopus 로고    scopus 로고
    • Essential role of the NH2-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27
    • [59] Theriault, J.R., Lambert, H., Chavez-Zobel, A.T., Charest, G., Lavigne, P., Landry, J., Essential role of the NH2-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27. J. Biol. Chem. 279 (2004), 23463–23471.
    • (2004) J. Biol. Chem. , vol.279 , pp. 23463-23471
    • Theriault, J.R.1    Lambert, H.2    Chavez-Zobel, A.T.3    Charest, G.4    Lavigne, P.5    Landry, J.6
  • 60
    • 17644408766 scopus 로고    scopus 로고
    • Subunit exchange of polydisperse proteins: mass spectrometry reveals consequences of alphaA-crystallin truncation
    • [60] Aquilina, J.A., Benesch, J.L., Ding, L.L., Yaron, O., Horwitz, J., Robinson, C.V., Subunit exchange of polydisperse proteins: mass spectrometry reveals consequences of alphaA-crystallin truncation. J. Biol. Chem. 280 (2005), 14485–14491.
    • (2005) J. Biol. Chem. , vol.280 , pp. 14485-14491
    • Aquilina, J.A.1    Benesch, J.L.2    Ding, L.L.3    Yaron, O.4    Horwitz, J.5    Robinson, C.V.6
  • 61
    • 27144448839 scopus 로고    scopus 로고
    • Some like it hot: the structure and function of small heat-shock proteins
    • [61] Haslbeck, M., Franzmann, T., Weinfurtner, D., Buchner, J., Some like it hot: the structure and function of small heat-shock proteins. Nat. Struct. Mol. Biol. 12 (2005), 842–846.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 842-846
    • Haslbeck, M.1    Franzmann, T.2    Weinfurtner, D.3    Buchner, J.4
  • 62
    • 0042733148 scopus 로고    scopus 로고
    • Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK
    • [62] Mogk, A., Schlieker, C., Friedrich, K.L., Schonfeld, H.J., Vierling, E., Bukau, B., Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK. J. Biol. Chem. 278 (2003), 31033–31042.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31033-31042
    • Mogk, A.1    Schlieker, C.2    Friedrich, K.L.3    Schonfeld, H.J.4    Vierling, E.5    Bukau, B.6
  • 63
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
    • [63] Lee, G.J., Roseman, A.M., Saibil, H.R., Vierling, E., A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J. 16 (1997), 659–671.
    • (1997) EMBO J. , vol.16 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4
  • 64
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • [64] Ehrnsperger, M., Graber, S., Gaestel, M., Buchner, J., Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J. 16 (1997), 221–229.
    • (1997) EMBO J. , vol.16 , pp. 221-229
    • Ehrnsperger, M.1    Graber, S.2    Gaestel, M.3    Buchner, J.4
  • 65
    • 0033765314 scopus 로고    scopus 로고
    • A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein
    • [65] Lee, G.J., Vierling, E., A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein. Plant Physiol. 122 (2000), 189–198.
    • (2000) Plant Physiol. , vol.122 , pp. 189-198
    • Lee, G.J.1    Vierling, E.2
  • 66
    • 0032567434 scopus 로고    scopus 로고
    • Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery
    • [66] Chen, S., Smith, D.F., Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery. J. Biol. Chem. 273 (1998), 35194–35200.
    • (1998) J. Biol. Chem. , vol.273 , pp. 35194-35200
    • Chen, S.1    Smith, D.F.2
  • 67
    • 84867809427 scopus 로고    scopus 로고
    • Analysis of the tau-associated proteome reveals that exchange of Hsp70 for Hsp90 is involved in tau degradation
    • [67] Thompson, A.D., Scaglione, K.M., Prensner, J., Gillies, A.T., Chinnaiyan, A., Paulson, H.L., et al. Analysis of the tau-associated proteome reveals that exchange of Hsp70 for Hsp90 is involved in tau degradation. ACS Chem. Biol. 7 (2012), 1677–1686.
    • (2012) ACS Chem. Biol. , vol.7 , pp. 1677-1686
    • Thompson, A.D.1    Scaglione, K.M.2    Prensner, J.3    Gillies, A.T.4    Chinnaiyan, A.5    Paulson, H.L.6


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