메뉴 건너뛰기




Volumn 291, Issue 35, 2016, Pages 18096-18106

Structural and biological interaction of HSC-70 protein with phosphatidylserine in endosomal microautophagy

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; DISSOCIATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PLASMONS; SURFACE PLASMON RESONANCE;

EID: 84984783742     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M116.736744     Document Type: Article
Times cited : (48)

References (39)
  • 3
    • 0029013908 scopus 로고
    • The role of ATP in the functional cycle of the DnaK chaperone system
    • McCarty, J. S., Buchberger, A., Reinstein, J., and Bukau, B. (1995) The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol. 249, 126-137
    • (1995) J. Mol. Biol , vol.249 , pp. 126-137
    • McCarty, J.S.1    Buchberger, A.2    Reinstein, J.3    Bukau, B.4
  • 4
    • 0028151509 scopus 로고
    • The ATP hydrolysis-dependent reaction cycle of the Escherichia coli hsp70 system DnaK, DnaJ, and GrpE
    • Szabo, A., Langer, T., Schröder, H., Flanagan, J., Bukau, B., and Hartl, F. U. (1994) The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE. Proc. Natl. Acad. Sci. U.S.A. 91, 10345-10349
    • (1994) Proc. Natl. Acad. Sci. U.S.A , vol.91 , pp. 10345-10349
    • Szabo, A.1    Langer, T.2    Schröder, H.3    Flanagan, J.4    Bukau, B.5    Hartl, F.U.6
  • 5
    • 0027427986 scopus 로고
    • DnaK, DnaJ and GrpE form a cellular chaperone Machinery capable of repairing heat-induced protein damage
    • Schröder, H., Langer, T., Hartl, F. U., and Bukau, B. (1993) DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J. 12, 4137-4144
    • (1993) EMBO J , vol.12 , pp. 4137-4144
    • Schröder, H.1    Langer, T.2    Hartl, F.U.3    Bukau, B.4
  • 6
    • 0035900793 scopus 로고    scopus 로고
    • CHIP is a U-box-dependent E3 ubiquitin ligase: Identification of hsc70 as a target for ubiquitylation
    • Jiang, J., and Ballinger., C. A., Wu, Y., Dai, Q., Cyr, D. M., Höhfeld, J., and Patterson, C. (2001) CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation. J. Biol. Chem. 276, 42938-42944
    • (2001) J. Biol. Chem , vol.276 , pp. 42938-42944
    • Jiang, J.1    Ballinger, C.A.2    Wu, Y.3    Dai, Q.4    Cyr, D.M.5    Höhfeld, J.6    Patterson, C.7
  • 7
    • 0039172708 scopus 로고    scopus 로고
    • Theubiquitin-relatedBAG-1 provides a link between the molecular chaperones hsc70/Hsp70 and the proteasome
    • Lüders, J., Demand, J., and Höhfeld, J. (2000) Theubiquitin-relatedBAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome. J. Biol. Chem. 275, 4613-4617
    • (2000) J. Biol. Chem , vol.275 , pp. 4613-4617
    • Lüders, J.1    Demand, J.2    Höhfeld, J.3
  • 9
    • 77956178939 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: Molecular mechanisms and physiological relevance. Semin
    • Orenstein, S. J., and Cuervo, A. M. (2010) Chaperone-mediated autophagy: molecular mechanisms and physiological relevance. Semin. Cell Dev. Biol. 21, 719-726
    • (2010) Cell Dev. Biol , vol.21 , pp. 719-726
    • Orenstein, S.J.1    Cuervo, A.M.2
  • 10
    • 79551609332 scopus 로고    scopus 로고
    • BAG3 mediates chaperone-based aggresome-targeting and selective autophagy of misfolded proteins
    • Gamerdinger, M., and Kaya., A. M., Wolfrum, U., Clement, A. M., and Behl, C. (2011) BAG3 mediates chaperone-based aggresome-targeting and selective autophagy of misfolded proteins. EMBO Rep. 12, 149-156
    • (2011) EMBO Rep , vol.12 , pp. 149-156
    • Gamerdinger, M.1    Kaya, A.M.2    Wolfrum, U.3    Clement, A.M.4    Behl, C.5
  • 11
    • 35648993510 scopus 로고    scopus 로고
    • To be, or not to be-molecular chaperones in protein degradation
    • Arndt, V., Rogon, C, and Höhfeld, J. (2007) To be, or not to be-molecular chaperones in protein degradation. Cell. Mol. Life Sci. 64, 2525-2541
    • (2007) Cell. Mol. Life Sci , vol.64 , pp. 2525-2541
    • Arndt, V.1    Rogon, C.2    Höhfeld, J.3
  • 12
    • 33744962120 scopus 로고    scopus 로고
    • Hsc70 contacts helix III of the J domain from polyomavirus T antigens: Addressing a dilemma in the chaperone hypothesis of how they release E2F frompRb
    • Garimella, R., Liu, X., Qiao, W., Liang, X., and Zuiderweg., E. R., Riley, M. I., and Van Doren, S. R. (2006) Hsc70 contacts helix III of the J domain from polyomavirus T antigens: addressing a dilemma in the chaperone hypothesis of how they release E2F frompRb. Biochemistry 45, 6917-6929
    • (2006) Biochemistry , vol.45 , pp. 6917-6929
    • Garimella, R.1    Liu, X.2    Qiao, W.3    Liang, X.4    Zuiderweg, E.R.5    Riley, M.I.6    Van Doren, S.R.7
  • 13
    • 0033603631 scopus 로고    scopus 로고
    • High-resolution solution structure of the 18-kDa substrate binding domain of the mammalian chaperone protein hsc70
    • Morshauser, R. C, Hu, W., Wang, H, Pang, Y., Flynn, G. C, and Zuiderweg, E. R. (1999) High-resolution solution structure of the 18-kDa substrate binding domain of the mammalian chaperone protein Hsc70. J. Mol. Biol. 289, 1387-1403
    • (1999) J. Mol. Biol , vol.289 , pp. 1387-1403
    • Morshauser, R.C.1    Hu, W.2    Wang, H.3    Pang, Y.4    Flynn, G.C.5    Zuiderweg, E.R.6
  • 14
    • 0029038683 scopus 로고
    • The peptide binding domain of the chaperone protein hsc70 has an unusual secondary structure topology
    • Morshauser, R.C., Wang, H., Flynn, G.C., and Zuiderweg, E. R. (1995) The peptide binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology. Biochemistry 34, 6261-6266
    • (1995) Biochemistry , vol.34 , pp. 6261-6266
    • Morshauser, R.C.1    Wang, H.2    Flynn, G.C.3    Zuiderweg, E.R.4
  • 16
    • 0034613163 scopus 로고    scopus 로고
    • ATP and ADP modulate a cation channel formed by hsc70 in acidic phospholipid membranes
    • Arispe, N, and De Maio, A. (2000) ATP and ADP modulate a cation channel formed by Hsc70 in acidic phospholipid membranes. J. Biol. Chem. 275, 30839-30843
    • (2000) J. Biol. Chem , vol.275 , pp. 30839-30843
    • Arispe, N.1    De Maio, A.2
  • 17
    • 38149094836 scopus 로고    scopus 로고
    • Membrane phosphatidylserine regulates surface charge and protein localization
    • Yeung, T., and Gilbert., G. E., Shi, J., Silvius, J., Kapus, A., and Grinstein, S. (2008) Membrane phosphatidylserine regulates surface charge and protein localization. Science 319, 210-213
    • (2008) Science , vol.319 , pp. 210-213
    • Yeung, T.1    Gilbert, G.E.2    Shi, J.3    Silvius, J.4    Kapus, A.5    Grinstein, S.6
  • 18
    • 0142179052 scopus 로고    scopus 로고
    • Self-assembly of single integral membrane proteins into soluble nanoscale phospholipid bilayers
    • Bayburt, T. H, and Sligar, S. G. (2003) Self-assembly of single integral membrane proteins into soluble nanoscale phospholipid bilayers. Protein Sci. 12, 2476-2481
    • (2003) Protein Sci , vol.12 , pp. 2476-2481
    • Bayburt, T.H.1    Sligar, S.G.2
  • 20
    • 84896717085 scopus 로고    scopus 로고
    • An ensemble of rapidly interconverting orientations in electrostatic protein-peptide complexes characterized by NMR spectroscopy
    • Guan, J. Y., and Foerster., J. M., Drijfhout, J. W., Timmer, M., Blok, A., and Ullmann., G. M., and Ubbink, M. (2014) An ensemble of rapidly interconverting orientations in electrostatic protein-peptide complexes characterized by NMR spectroscopy. Chembiochem 15, 556-566
    • (2014) Chembiochem , vol.15 , pp. 556-566
    • Guan, J.Y.1    Foerster, J.M.2    Drijfhout, J.W.3    Timmer, M.4    Blok, A.5    Ullmann, G.M.6    Ubbink, M.7
  • 21
    • 33646356250 scopus 로고    scopus 로고
    • Detecting transient intermediates in macromolecular binding by paramagnetic NMR
    • Iwahara, J., and Clore, G. M. (2006) Detecting transient intermediates in macromolecular binding by paramagnetic NMR. Nature 440, 1227-1230
    • (2006) Nature , vol.440 , pp. 1227-1230
    • Iwahara, J.1    Clore, G.M.2
  • 22
    • 0036204856 scopus 로고    scopus 로고
    • Biological staining: Mechanisms and theory
    • Horobin, R. W. (2002) Biological staining: mechanisms and theory. Biotech. Histochem. 77, 3-13
    • (2002) Biotech. Histochem , vol.77 , pp. 3-13
    • Horobin, R.W.1
  • 23
    • 0030071247 scopus 로고    scopus 로고
    • A Monte Carlo simulation study of protein-induced heat capacity changes and lipid-induced protein clustering
    • Heimburg, T., and Biltonen, R. L. (1996) A Monte Carlo simulation study of protein-induced heat capacity changes and lipid-induced protein clustering. Biophys. J. 70, 84-96
    • (1996) Biophys. J , vol.70 , pp. 84-96
    • Heimburg, T.1    Biltonen, R.L.2
  • 24
    • 0029669955 scopus 로고    scopus 로고
    • Free-energy determinants of a-helix insertion into lipid bilayers
    • Ben-Tal, N., Ben-Shaul, A., Nicholls, A., and Honig, B. (1996) Free-energy determinants of a-helix insertion into lipid bilayers. Biophys. J. 70, 1803-1812
    • (1996) Biophys. J , vol.70 , pp. 1803-1812
    • Ben-Tal, N.1    Ben-Shaul, A.2    Nicholls, A.3    Honig, B.4
  • 28
    • 84871689599 scopus 로고    scopus 로고
    • Structure and dynamics of the ATP-bound open conformation of hsp70 chaperones
    • Kityk, R., Kopp, J., Sinning, I., and Mayer, M. P. (2012) Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones. Mol. Cell 48, 863-874
    • (2012) Mol. Cell , vol.48 , pp. 863-874
    • Kityk, R.1    Kopp, J.2    Sinning, I.3    Mayer, M.P.4
  • 29
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
    • Flaherty, K. M., DeLuca-Flaherty, C., and McKay, D. B. (1990) Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 346, 623-628
    • (1990) Nature , vol.346 , pp. 623-628
    • Flaherty, K.M.1    DeLuca-Flaherty, C.2    McKay, D.B.3
  • 31
    • 0041734594 scopus 로고    scopus 로고
    • Structural features required for the interaction of the hsp70 molecular chaperone DnaK with its cochaperone DnaJ
    • Suh, W. C., and Lu., C. Z., and Gross, C. A. (1999) Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ. J. Biol. Chem. 274, 30534-30539
    • (1999) J. Biol. Chem , vol.274 , pp. 30534-30539
    • Suh, W.C.1    Lu, C.Z.2    Gross, C.A.3
  • 32
    • 0035936826 scopus 로고    scopus 로고
    • Structure of a bag/Hsc70 complex: Convergent functional evolution of hsp70 nucleotide exchange factors
    • Sondermann, H., Scheufler, C., Schneider, C., Hohfeld, J., and Hartl., F. U., and Moarefi, I. (2001) Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors. Science 291, 1553-1557
    • (2001) Science , vol.291 , pp. 1553-1557
    • Sondermann, H.1    Scheufler, C.2    Schneider, C.3    Hohfeld, J.4    Hartl, F.U.5    Moarefi, I.6
  • 33
    • 43049155955 scopus 로고    scopus 로고
    • The BAG proteins: A ubiquitous family of chaperone regulators
    • Kabbage, M., and Dickman, M. B. (2008) The BAG proteins: a ubiquitous family of chaperone regulators. Cell. Mol. Life Sci. 65, 1390-1402
    • (2008) Cell. Mol. Life Sci , vol.65 , pp. 1390-1402
    • Kabbage, M.1    Dickman, M.B.2
  • 34
    • 79960927001 scopus 로고    scopus 로고
    • Allosteric drugs: The interaction of antitumor compound MKT-077 with human hsp70 chaperones
    • Rousaki, A., Miyata, Y., Jinwal, U. K., and Dickey., C. A., Gestwicki, J. E., and Zuiderweg, E. R. (2011) Allosteric drugs: the interaction of antitumor compound MKT-077 with human Hsp70 chaperones. J. Mol. Biol. 411, 614-632
    • (2011) J. Mol. Biol , vol.411 , pp. 614-632
    • Rousaki, A.1    Miyata, Y.2    Jinwal, U.K.3    Dickey, C.A.4    Gestwicki, J.E.5    Zuiderweg, E.R.6
  • 36
    • 84914104764 scopus 로고    scopus 로고
    • Structural basis for the inhibition of HSP70 and DnaK chaperones by small-molecule targeting of a C-terminal allosteric pocket
    • Leu, J. I., Zhang, P., Murphy, M. E., Marmorstein, R., and George, D. L. (2014) Structural basis for the inhibition of HSP70 and DnaK chaperones by small-molecule targeting of a C-terminal allosteric pocket. ACS Chem. Biol. 9, 2508-2516
    • (2014) ACS Chem. Biol , vol.9 , pp. 2508-2516
    • Leu, J.I.1    Zhang, P.2    Murphy, M.E.3    Marmorstein, R.4    George, D.L.5
  • 37
    • 79951837256 scopus 로고    scopus 로고
    • Chemical screens against a reconstituted multiprotein complex: Myricetin blocks DnaJ regulation of DnaK through an allosteric mechanism
    • Chang, L., Miyata, Y., Ung, P. M., and Bertelsen., E. B., McQuade, T. J., Carlson, H. A., and Zuiderweg., E. R., and Gestwicki, J. E. (2011) Chemical screens against a reconstituted multiprotein complex: myricetin blocks DnaJ regulation of DnaK through an allosteric mechanism. Chem. Biol. 18, 210-221
    • (2011) Chem. Biol , vol.18 , pp. 210-221
    • Chang, L.1    Miyata, Y.2    Ung, P.M.3    Bertelsen, E.B.4    McQuade, T.J.5    Carlson, H.A.6    Zuiderweg, E.R.7    Gestwicki, J.E.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.