메뉴 건너뛰기




Volumn 396, Issue 2, 2010, Pages 317-322

Drosophila UNC-45 prevents heat-induced aggregation of skeletal muscle myosin and facilitates refolding of citrate synthase

Author keywords

Chaperone; Drosophila; Myosin; Protein aggregation; Refolding; UNC 45

Indexed keywords

ALPHA LACTALBUMIN; CHAPERONE; CITRATE SYNTHASE; MEROMYOSIN; MYOSIN; MYOSIN SUBFRAGMENT 1; PROTEIN UNC 45; UNCLASSIFIED DRUG; UREA;

EID: 77952744235     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.04.090     Document Type: Article
Times cited : (31)

References (33)
  • 1
    • 0037169028 scopus 로고    scopus 로고
    • Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin
    • Barral J.M., Hutagalung A.H., Brinker A., Hartl F.U., and Epstein H.F. Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin. Science 295 (2002) 669-671
    • (2002) Science , vol.295 , pp. 669-671
    • Barral, J.M.1    Hutagalung, A.H.2    Brinker, A.3    Hartl, F.U.4    Epstein, H.F.5
  • 2
    • 44649176937 scopus 로고    scopus 로고
    • Protein quality control gets muscle into shape
    • Kim J., Lowe T., and Hoppe T. Protein quality control gets muscle into shape. Trends Cell Biol. 18 (2008) 264-272
    • (2008) Trends Cell Biol. , vol.18 , pp. 264-272
    • Kim, J.1    Lowe, T.2    Hoppe, T.3
  • 3
    • 0033886530 scopus 로고    scopus 로고
    • Fission yeast Rng3p: an UCS-domain protein that mediates myosin II assembly during cytokinesis
    • Wong K.C., Naqvi N.I., Iino Y., Yamamoto M., and Balasubramanian M.K. Fission yeast Rng3p: an UCS-domain protein that mediates myosin II assembly during cytokinesis. J. Cell Sci. 113 (2000) 2421-2432
    • (2000) J. Cell Sci. , vol.113 , pp. 2421-2432
    • Wong, K.C.1    Naqvi, N.I.2    Iino, Y.3    Yamamoto, M.4    Balasubramanian, M.K.5
  • 4
    • 45249089995 scopus 로고    scopus 로고
    • Yeast UCS proteins promote actomyosin interactions and limit myosin turnover in cells
    • Lord M., Sladewski T.E., and Pollard T.D. Yeast UCS proteins promote actomyosin interactions and limit myosin turnover in cells. Proc. Natl. Acad. Sci. USA 105 (2008) 8014-8019
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 8014-8019
    • Lord, M.1    Sladewski, T.E.2    Pollard, T.D.3
  • 5
    • 0016358187 scopus 로고
    • Temperature-sensitive mutation affecting myofilament assembly in Caenorhabditis elegans
    • Epstein H.F., and Thomson J.N. Temperature-sensitive mutation affecting myofilament assembly in Caenorhabditis elegans. Nature 250 (1974) 579-580
    • (1974) Nature , vol.250 , pp. 579-580
    • Epstein, H.F.1    Thomson, J.N.2
  • 6
    • 0344527945 scopus 로고    scopus 로고
    • Unc-45 gene of Caenorhabditis elegans encodes a muscle-specific tetratricopeptide repeat-containing protein
    • Venolia L., Ao W., Kim S., Kim C., and Pilgrim D. Unc-45 gene of Caenorhabditis elegans encodes a muscle-specific tetratricopeptide repeat-containing protein. Cell Motil. Cytoskeleton 42 (1999) 163-177
    • (1999) Cell Motil. Cytoskeleton , vol.42 , pp. 163-177
    • Venolia, L.1    Ao, W.2    Kim, S.3    Kim, C.4    Pilgrim, D.5
  • 7
    • 0036022268 scopus 로고    scopus 로고
    • A zebrafish unc-45-related gene expressed during muscle development
    • Etheridge L., Diiorio P., and Sagerstrom C.G. A zebrafish unc-45-related gene expressed during muscle development. Dev. Dyn. 224 (2002) 457-460
    • (2002) Dev. Dyn. , vol.224 , pp. 457-460
    • Etheridge, L.1    Diiorio, P.2    Sagerstrom, C.G.3
  • 8
    • 1842833926 scopus 로고    scopus 로고
    • Two mammalian UNC-45 isoforms are related to distinct cytoskeletal and muscle-specific functions
    • Price M.G., Landsverk M.L., Barral J.M., and Epstein H.F. Two mammalian UNC-45 isoforms are related to distinct cytoskeletal and muscle-specific functions. J. Cell Sci. 115 (2002) 4013-4023
    • (2002) J. Cell Sci. , vol.115 , pp. 4013-4023
    • Price, M.G.1    Landsverk, M.L.2    Barral, J.M.3    Epstein, H.F.4
  • 9
    • 33847392824 scopus 로고    scopus 로고
    • The myosin co-chaperone UNC-45 is required for skeletal and cardiac muscle function in zebrafish
    • Wohlgemuth S.L., Crawford B.D., and Pilgrim D.B. The myosin co-chaperone UNC-45 is required for skeletal and cardiac muscle function in zebrafish. Dev. Biol. 303 (2007) 483-492
    • (2007) Dev. Biol. , vol.303 , pp. 483-492
    • Wohlgemuth, S.L.1    Crawford, B.D.2    Pilgrim, D.B.3
  • 11
    • 34547103542 scopus 로고    scopus 로고
    • The UCS factor Steif/Unc-45b interacts with the heat shock protein Hsp90a during myofibrillogenesis
    • Etard C., Behra M., Fischer N., Hutcheson D., Geisler R., and Strahle U. The UCS factor Steif/Unc-45b interacts with the heat shock protein Hsp90a during myofibrillogenesis. Dev. Biol. 308 (2007) 133-143
    • (2007) Dev. Biol. , vol.308 , pp. 133-143
    • Etard, C.1    Behra, M.2    Fischer, N.3    Hutcheson, D.4    Geisler, R.5    Strahle, U.6
  • 13
    • 34247466028 scopus 로고    scopus 로고
    • The UNC-45 chaperone mediates sarcomere assembly through myosin degradation in Caenorhabditis elegans
    • Landsverk M.L., Li S., Hutagalung A.H., Najafov A., Hoppe T., Barral J.M., and Epstein H.F. The UNC-45 chaperone mediates sarcomere assembly through myosin degradation in Caenorhabditis elegans. J. Cell Biol. 177 (2007) 205-210
    • (2007) J. Cell Biol. , vol.177 , pp. 205-210
    • Landsverk, M.L.1    Li, S.2    Hutagalung, A.H.3    Najafov, A.4    Hoppe, T.5    Barral, J.M.6    Epstein, H.F.7
  • 14
    • 0037672216 scopus 로고    scopus 로고
    • UCS proteins: managing the myosin motor
    • Yu Q., and Bernstein S.I. UCS proteins: managing the myosin motor. Curr. Biol. 13 (2003) R525-R527
    • (2003) Curr. Biol. , vol.13
    • Yu, Q.1    Bernstein, S.I.2
  • 15
    • 1542286175 scopus 로고    scopus 로고
    • A new structural state of myosin
    • Kull F.J., and Endow S.A. A new structural state of myosin. Trends Biochem. Sci. 29 (2004) 103-106
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 103-106
    • Kull, F.J.1    Endow, S.A.2
  • 16
    • 0026484244 scopus 로고
    • Genetic approaches to understanding muscle development
    • Epstein H.F., and Bernstein S.I. Genetic approaches to understanding muscle development. Dev. Biol. 154 (1992) 231-244
    • (1992) Dev. Biol. , vol.154 , pp. 231-244
    • Epstein, H.F.1    Bernstein, S.I.2
  • 17
    • 33646042860 scopus 로고    scopus 로고
    • AlphaB-crystallin maintains skeletal muscle myosin enzymatic activity and prevents its aggregation under heat-shock stress
    • Melkani G.C., Cammarato A., and Bernstein S.I. AlphaB-crystallin maintains skeletal muscle myosin enzymatic activity and prevents its aggregation under heat-shock stress. J. Mol. Biol. 358 (2006) 635-645
    • (2006) J. Mol. Biol. , vol.358 , pp. 635-645
    • Melkani, G.C.1    Cammarato, A.2    Bernstein, S.I.3
  • 19
    • 0037014666 scopus 로고    scopus 로고
    • Suppression of DTT-induced aggregation of abrin by alphaA- and alphaB-crystallins: a model aggregation assay for alpha-crystallin chaperone activity in vitro
    • Reddy G.B., Narayanan S., Reddy P.Y., and Surolia I. Suppression of DTT-induced aggregation of abrin by alphaA- and alphaB-crystallins: a model aggregation assay for alpha-crystallin chaperone activity in vitro. FEBS Lett. 522 (2002) 59-64
    • (2002) FEBS Lett. , vol.522 , pp. 59-64
    • Reddy, G.B.1    Narayanan, S.2    Reddy, P.Y.3    Surolia, I.4
  • 21
    • 0032477726 scopus 로고    scopus 로고
    • ATP-enhanced molecular chaperone functions of the small heat shock protein human alphaB crystallin
    • Muchowski P.J., and Clark J.I. ATP-enhanced molecular chaperone functions of the small heat shock protein human alphaB crystallin. Proc. Natl. Acad. Sci. USA 95 (1998) 1004-1009
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1004-1009
    • Muchowski, P.J.1    Clark, J.I.2
  • 22
    • 0035805601 scopus 로고    scopus 로고
    • Alternative exon-encoded regions of Drosophila myosin heavy chain modulate ATPase rates and actin sliding velocity
    • Swank D.M., Bartoo M.L., Knowles A.F., Iliffe C., Bernstein S.I., Molloy J.E., and Sparrow J.C. Alternative exon-encoded regions of Drosophila myosin heavy chain modulate ATPase rates and actin sliding velocity. J. Biol. Chem. 276 (2001) 15117-15124
    • (2001) J. Biol. Chem. , vol.276 , pp. 15117-15124
    • Swank, D.M.1    Bartoo, M.L.2    Knowles, A.F.3    Iliffe, C.4    Bernstein, S.I.5    Molloy, J.E.6    Sparrow, J.C.7
  • 23
    • 0346118918 scopus 로고    scopus 로고
    • Kinetic analysis of Drosophila muscle myosin isoforms suggests a novel mode of mechanochemical coupling
    • Miller B.M., Nyitrai M., Bernstein S.I., and Geeves M.A. Kinetic analysis of Drosophila muscle myosin isoforms suggests a novel mode of mechanochemical coupling. J. Biol. Chem. 278 (2003) 50293-50300
    • (2003) J. Biol. Chem. , vol.278 , pp. 50293-50300
    • Miller, B.M.1    Nyitrai, M.2    Bernstein, S.I.3    Geeves, M.A.4
  • 24
    • 0020021291 scopus 로고
    • Preparation of myosin and its subfragments from rabbit skeletal muscle
    • Margossian S.S., and Lowey S. Preparation of myosin and its subfragments from rabbit skeletal muscle. Methods Enzymol. 85 (1982) 55-71
    • (1982) Methods Enzymol. , vol.85 , pp. 55-71
    • Margossian, S.S.1    Lowey, S.2
  • 25
    • 0018425157 scopus 로고
    • Chicken gizzard heavy meromyosin that retains the two light-chain components, including a phosphorylatable one
    • Onishi H., and Watanabe S. Chicken gizzard heavy meromyosin that retains the two light-chain components, including a phosphorylatable one. J. Biochem. 85 (1979) 457-472
    • (1979) J. Biochem. , vol.85 , pp. 457-472
    • Onishi, H.1    Watanabe, S.2
  • 26
    • 0020678721 scopus 로고
    • Light-chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin molecules
    • Craig R., Smith R., and Kendrick-Jones J. Light-chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin molecules. Nature 302 (1983) 436-439
    • (1983) Nature , vol.302 , pp. 436-439
    • Craig, R.1    Smith, R.2    Kendrick-Jones, J.3
  • 27
    • 47749122973 scopus 로고    scopus 로고
    • Unc45b forms a cytosolic complex with Hsp90 and targets the unfolded myosin motor domain
    • Srikakulam R., Liu L., and Winkelmann D.A. Unc45b forms a cytosolic complex with Hsp90 and targets the unfolded myosin motor domain. PLoS One 3 (2008) e2137
    • (2008) PLoS One , vol.3
    • Srikakulam, R.1    Liu, L.2    Winkelmann, D.A.3
  • 28
    • 0025251847 scopus 로고
    • Melting of myosin and tropomyosin: electron microscopic observations
    • Mabuchi K. Melting of myosin and tropomyosin: electron microscopic observations. J. Struct. Biol. 103 (1990) 249-256
    • (1990) J. Struct. Biol. , vol.103 , pp. 249-256
    • Mabuchi, K.1
  • 29
    • 0032583155 scopus 로고    scopus 로고
    • Unc-45 mutations in Caenorhabditis elegans implicate a CRO1/She4p-like domain in myosin assembly
    • Barral J.M., Bauer C.C., Ortiz I., and Epstein H.F. Unc-45 mutations in Caenorhabditis elegans implicate a CRO1/She4p-like domain in myosin assembly. J. Cell Biol. 143 (1998) 1215-1225
    • (1998) J. Cell Biol. , vol.143 , pp. 1215-1225
    • Barral, J.M.1    Bauer, C.C.2    Ortiz, I.3    Epstein, H.F.4
  • 30
    • 7244226219 scopus 로고    scopus 로고
    • UCS protein Rng3p activates actin filament gliding by fission yeast myosin-II
    • Lord M., and Pollard T.D. UCS protein Rng3p activates actin filament gliding by fission yeast myosin-II. J. Cell Biol. 167 (2004) 315-325
    • (2004) J. Cell Biol. , vol.167 , pp. 315-325
    • Lord, M.1    Pollard, T.D.2
  • 31
    • 45149115936 scopus 로고    scopus 로고
    • Unc45 activates Hsp90-dependent folding of the myosin motor domain
    • Liu L., Srikakulam R., and Winkelmann D.A. Unc45 activates Hsp90-dependent folding of the myosin motor domain. J. Biol. Chem. 283 (2008) 13185-13193
    • (2008) J. Biol. Chem. , vol.283 , pp. 13185-13193
    • Liu, L.1    Srikakulam, R.2    Winkelmann, D.A.3
  • 32
    • 77952745070 scopus 로고    scopus 로고
    • Proteomic analysis of ischemic heart failure patients reveals increases in a myosin assembly protein (UNC-45)
    • Stanley B.A., Liu P., Kirshenbaum L.A., and Van Eyk J.E. Proteomic analysis of ischemic heart failure patients reveals increases in a myosin assembly protein (UNC-45). Circ. Res. 97 (2005) 10
    • (2005) Circ. Res. , vol.97 , pp. 10
    • Stanley, B.A.1    Liu, P.2    Kirshenbaum, L.A.3    Van Eyk, J.E.4
  • 33
    • 41549132154 scopus 로고    scopus 로고
    • Shuttling of the chaperones Unc45b and Hsp90a between the A band and the Z line of the myofibril
    • Etard C., Roostalu U., and Strahle U. Shuttling of the chaperones Unc45b and Hsp90a between the A band and the Z line of the myofibril. J. Cell Biol. 180 (2008) 1163-1175
    • (2008) J. Cell Biol. , vol.180 , pp. 1163-1175
    • Etard, C.1    Roostalu, U.2    Strahle, U.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.