메뉴 건너뛰기




Volumn 45, Issue 2, 2013, Pages 344-346

Commentary on paper: Small heat shock proteins and the cytoskeleton: An essential interplay for cell integrity? (Wettstein et al.)

Author keywords

Actin filaments; Cytoskeleton; Phosphorylation; Small heat shock proteins

Indexed keywords

ALPHA CRYSTALLIN; F ACTIN; G ACTIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 20; HEAT SHOCK PROTEIN 27; TUBULIN;

EID: 84872316472     PISSN: 13572725     EISSN: 18785875     Source Type: Journal    
DOI: 10.1016/j.biocel.2012.11.011     Document Type: Article
Times cited : (9)

References (32)
  • 2
    • 84934439863 scopus 로고    scopus 로고
    • The cellular "networking" of mammalian Hsp27 and its functions in the control of protein folding, redox state and apoptosis
    • A.P. Arrigo The cellular "networking" of mammalian Hsp27 and its functions in the control of protein folding, redox state and apoptosis Advances in Experimental Medicine and Biology 594 2007 14 26
    • (2007) Advances in Experimental Medicine and Biology , vol.594 , pp. 14-26
    • Arrigo, A.P.1
  • 3
    • 0030966372 scopus 로고    scopus 로고
    • Cyclic nucleotide-dependent vasorelaxation is associated with the phosphorylation of a small heat shock-related protein
    • A.C. Beall, K. Kato, J.R. Goldenring, H. Rasmussen, and C.M. Brophy Cyclic nucleotide-dependent vasorelaxation is associated with the phosphorylation of a small heat shock-related protein Journal of Biological Chemistry 272 1997 11283 11287
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 11283-11287
    • Beall, A.C.1    Kato, K.2    Goldenring, J.R.3    Rasmussen, H.4    Brophy, C.M.5
  • 4
    • 0028071812 scopus 로고
    • Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity
    • R. Benndorf, K. Hayess, S. Ryazantsev, M. Wieske, J. Behlke, and G. Lutsch Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity Journal of Biological Chemistry 269 1994 20780 20784
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 20780-20784
    • Benndorf, R.1    Hayess, K.2    Ryazantsev, S.3    Wieske, M.4    Behlke, J.5    Lutsch, G.6
  • 5
    • 0036092538 scopus 로고    scopus 로고
    • HSP27 modulates agonist-induced association of translocated RhoA and PKC-alpha in muscle cells of the colon
    • K.N. Bitar, A. Ibitayo, and S.B. Patil HSP27 modulates agonist-induced association of translocated RhoA and PKC-alpha in muscle cells of the colon Journal of Applied Physiology 92 2002 41 49
    • (2002) Journal of Applied Physiology , vol.92 , pp. 41-49
    • Bitar, K.N.1    Ibitayo, A.2    Patil, S.B.3
  • 6
    • 0033016897 scopus 로고    scopus 로고
    • The small heat shock-related protein-20 is an actin-associated protein
    • C.M. Brophy, S. Lamb, and A. Graham The small heat shock-related protein-20 is an actin-associated protein Journal of Vascular Surgery 29 1999 326 333
    • (1999) Journal of Vascular Surgery , vol.29 , pp. 326-333
    • Brophy, C.M.1    Lamb, S.2    Graham, A.3
  • 7
    • 28444497458 scopus 로고    scopus 로고
    • Small heat shock protein with apparent molecular mass 20 kDa (Hsp20, HspB6) is not a genuine actin-binding protein
    • O.V. Bukach, S.B. Marston, and N.B. Gusev Small heat shock protein with apparent molecular mass 20 kDa (Hsp20, HspB6) is not a genuine actin-binding protein Journal of Muscle Research and Cell Motility 26 2005 175 181
    • (2005) Journal of Muscle Research and Cell Motility , vol.26 , pp. 175-181
    • Bukach, O.V.1    Marston, S.B.2    Gusev, N.B.3
  • 8
    • 0035831438 scopus 로고    scopus 로고
    • Heat shock protein 27 is a substrate of cGMP-dependent protein kinase in intact human platelets: Phosphorylation-induced actin polymerization caused by HSP27 mutants
    • E. Butt, D. Immler, H.E. Meyer, A. Kotlyarov, K. Laass, and M. Gaestel Heat shock protein 27 is a substrate of cGMP-dependent protein kinase in intact human platelets: phosphorylation-induced actin polymerization caused by HSP27 mutants Journal of Biological Chemistry 276 2001 7108 7113
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 7108-7113
    • Butt, E.1    Immler, D.2    Meyer, H.E.3    Kotlyarov, A.4    Laass, K.5    Gaestel, M.6
  • 10
    • 0035893961 scopus 로고    scopus 로고
    • The actin cytoskeleton response to oxidants: From small heat shock protein phosphorylation to changes in the redox state of actin itself
    • I. Dalle-Donne, R. Rossi, A. Milzani, P. Di Simplicio, and R. Colombo The actin cytoskeleton response to oxidants: from small heat shock protein phosphorylation to changes in the redox state of actin itself Free Radical Biology and Medicine 31 2001 1624 1632
    • (2001) Free Radical Biology and Medicine , vol.31 , pp. 1624-1632
    • Dalle-Donne, I.1    Rossi, R.2    Milzani, A.3    Di Simplicio, P.4    Colombo, R.5
  • 11
    • 34247643279 scopus 로고    scopus 로고
    • Anthrax lethal toxin paralyzes actin-based motility by blocking Hsp27 phosphorylation
    • R.L. During, B.G. Gibson, W. Li, E.A. Bishai, G.S. Sidhu, and J. Landry Anthrax lethal toxin paralyzes actin-based motility by blocking Hsp27 phosphorylation EMBO Journal 26 2007 2240 2250
    • (2007) EMBO Journal , vol.26 , pp. 2240-2250
    • During, R.L.1    Gibson, B.G.2    Li, W.3    Bishai, E.A.4    Sidhu, G.S.5    Landry, J.6
  • 14
    • 77950366991 scopus 로고    scopus 로고
    • Thiolutin inhibits endothelial cell adhesion by perturbing Hsp27 interactions with components of the actin and intermediate filament cytoskeleton
    • Y. Jia, S.L. Wu, J.S. Isenberg, S. Dai, J.M. Sipes, and L. Field Thiolutin inhibits endothelial cell adhesion by perturbing Hsp27 interactions with components of the actin and intermediate filament cytoskeleton Cell Stress and Chaperones 15 2010 165 181
    • (2010) Cell Stress and Chaperones , vol.15 , pp. 165-181
    • Jia, Y.1    Wu, S.L.2    Isenberg, J.S.3    Dai, S.4    Sipes, J.M.5    Field, L.6
  • 15
    • 1442300779 scopus 로고    scopus 로고
    • Cytoskeletal disruption and small heat shock protein translocation immediately after lengthening contractions
    • T.J. Koh, and J. Escobedo Cytoskeletal disruption and small heat shock protein translocation immediately after lengthening contractions American Journal of Physiology-Cell Physiology 286 2004 C713 C722
    • (2004) American Journal of Physiology-Cell Physiology , vol.286
    • Koh, T.J.1    Escobedo, J.2
  • 16
    • 84866425540 scopus 로고    scopus 로고
    • Influences of temperature, oxidative stress, and phosphorylation on binding of heat shock proteins in skeletal muscle fibers
    • N.T. Larkins, R.M. Murphy, and G.D. Lamb Influences of temperature, oxidative stress, and phosphorylation on binding of heat shock proteins in skeletal muscle fibers American Journal of Physiology-Cell Physiology 303 2012 C654 C665
    • (2012) American Journal of Physiology-Cell Physiology , vol.303
    • Larkins, N.T.1    Murphy, R.M.2    Lamb, G.D.3
  • 19
    • 0025813543 scopus 로고
    • Geiger B A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein
    • T. Miron, K. Vancompernolle, J. Vandekerckhove, and M. Wilchek Geiger B A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein Journal of Cell Biology 114 1991 255 261
    • (1991) Journal of Cell Biology , vol.114 , pp. 255-261
    • Miron, T.1    Vancompernolle, K.2    Vandekerckhove, J.3    Wilchek, M.4
  • 20
    • 0024212723 scopus 로고
    • Characterization of an inhibitor of actin polymerization in vinculin-rich fraction of turkey gizzard smooth muscle
    • T. Miron, M. Wilchek, and B. Geiger Characterization of an inhibitor of actin polymerization in vinculin-rich fraction of turkey gizzard smooth muscle European Journal of Biochemistry 178 1988 543 553
    • (1988) European Journal of Biochemistry , vol.178 , pp. 543-553
    • Miron, T.1    Wilchek, M.2    Geiger, B.3
  • 21
    • 0037338308 scopus 로고    scopus 로고
    • Interaction of the small heat shock protein with molecular mass 25 kDa (hsp25) with actin
    • O.O. Panasenko, M.V. Kim, S.B. Marston, and N.B. Gusev Interaction of the small heat shock protein with molecular mass 25 kDa (hsp25) with actin European Journal of Biochemistry 270 2003 892 901
    • (2003) European Journal of Biochemistry , vol.270 , pp. 892-901
    • Panasenko, O.O.1    Kim, M.V.2    Marston, S.B.3    Gusev, N.B.4
  • 23
    • 35748965834 scopus 로고    scopus 로고
    • Small heat shock protein Hsp27 prevents heat-induced aggregation of F-actin by forming soluble complexes with denatured actin
    • A.V. Pivovarova, N.A. Chebotareva, I.S. Chernik, N.B. Gusev, and D.I. Levitsky Small heat shock protein Hsp27 prevents heat-induced aggregation of F-actin by forming soluble complexes with denatured actin FEBS Journal 274 2007 5937 5948
    • (2007) FEBS Journal , vol.274 , pp. 5937-5948
    • Pivovarova, A.V.1    Chebotareva, N.A.2    Chernik, I.S.3    Gusev, N.B.4    Levitsky, D.I.5
  • 24
    • 0034192553 scopus 로고    scopus 로고
    • CGMP-mediated phosphorylation of heat shock protein 20 may cause smooth muscle relaxation without myosin light chain dephosphorylation in swine carotid artery
    • Pt 3
    • C.M. Rembold, D.B. Foster, J.D. Strauss, C.J. Wingard, and J.E. Eyk cGMP-mediated phosphorylation of heat shock protein 20 may cause smooth muscle relaxation without myosin light chain dephosphorylation in swine carotid artery Journal of Physiology 524 2000 865 878 Pt 3
    • (2000) Journal of Physiology , vol.524 , pp. 865-878
    • Rembold, C.M.1    Foster, D.B.2    Strauss, J.D.3    Wingard, C.J.4    Eyk, J.E.5
  • 26
    • 0033516660 scopus 로고    scopus 로고
    • Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation
    • T. Rogalla, M. Ehrnsperger, X. Preville, A. Kotlyarov, G. Lutsch, and C. Ducasse Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation Journal of Biological Chemistry 274 1999 18947 18956
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 18947-18956
    • Rogalla, T.1    Ehrnsperger, M.2    Preville, X.3    Kotlyarov, A.4    Lutsch, G.5    Ducasse, C.6
  • 27
    • 77951256339 scopus 로고    scopus 로고
    • Versatility of the small heat shock protein HSPB6 (Hsp20)
    • A.S. Seit-Nebi, and N.B. Gusev Versatility of the small heat shock protein HSPB6 (Hsp20) Cell Stress and Chaperones 15 2010 233 236
    • (2010) Cell Stress and Chaperones , vol.15 , pp. 233-236
    • Seit-Nebi, A.S.1    Gusev, N.B.2
  • 29
    • 84860462182 scopus 로고    scopus 로고
    • Cofilin weakly interacts with 14-3-3 and therefore can only indirectly participate in regulation of cell motility by small heat shock protein HspB6 (Hsp20)
    • M.V. Sudnitsyna, A.S. Seit-Nebi, and N.B. Gusev Cofilin weakly interacts with 14-3-3 and therefore can only indirectly participate in regulation of cell motility by small heat shock protein HspB6 (Hsp20) Archives of Biochemistry and Biophysics 521 2012 62 70
    • (2012) Archives of Biochemistry and Biophysics , vol.521 , pp. 62-70
    • Sudnitsyna, M.V.1    Seit-Nebi, A.S.2    Gusev, N.B.3
  • 30
    • 0037709152 scopus 로고    scopus 로고
    • The small heat shock protein (HSP) 20 is dynamically associated with the actin cross-linking protein actinin
    • D.J. Tessier, P. Komalavilas, A. Panitch, L. Joshi, and C.M. Brophy The small heat shock protein (HSP) 20 is dynamically associated with the actin cross-linking protein actinin Journal of Surgical Research 111 2003 152 157
    • (2003) Journal of Surgical Research , vol.111 , pp. 152-157
    • Tessier, D.J.1    Komalavilas, P.2    Panitch, A.3    Joshi, L.4    Brophy, C.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.