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Volumn 4, Issue 5, 2008, Pages 717-720

Clearance of a Hirano body-like F-actin aggresome generated by jasplakinolide

Author keywords

Actin; Aggresome; Autophagy; Cytoskeleton; Heat shock proteins; Hirano body; Jasplakinolide; Lysosomes; Microtubules; Proteasomes

Indexed keywords

CHAPERONE; F ACTIN; JASPAMIDE; PROTEASOME;

EID: 48249115147     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.4161/auto.6345     Document Type: Article
Times cited : (9)

References (29)
  • 1
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol 2000; 10:524-30.
    • (2000) Trends Cell Biol , vol.10 , pp. 524-530
    • Kopito, R.1
  • 2
    • 0036303981 scopus 로고    scopus 로고
    • Hassles with taking out the garbage: Aggravating aggresomes
    • Garcia-Mata R, Gao YS, Sztul E. Hassles with taking out the garbage: aggravating aggresomes. Traffic 2002; 3:388-6.
    • (2002) Traffic , vol.3 , pp. 388-396
    • Garcia-Mata, R.1    Gao, Y.S.2    Sztul, E.3
  • 3
    • 0028286860 scopus 로고
    • Hirano bodies and related neuronal inclusions
    • Hirano A. Hirano bodies and related neuronal inclusions. Neuropathol Appl Neurobiol 1994; 20:3-11.
    • (1994) Neuropathol Appl Neurobiol , vol.20 , pp. 3-11
    • Hirano, A.1
  • 4
  • 6
    • 0023387681 scopus 로고
    • Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells
    • Nishida E, Iida K, Yonezawa N, Koyasu S, Yahara I, Sakai H. Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells. Proc Natl Acad Sci USA 1987; 84: 5262-66.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5262-5266
    • Nishida, E.1    Iida, K.2    Yonezawa, N.3    Koyasu, S.4    Yahara, I.5    Sakai, H.6
  • 7
    • 0034282106 scopus 로고    scopus 로고
    • Neurodegenerative stimuli induce persisrent ADF/cofilin-actin rods that disrupt distal neurire function
    • Minamide LS, Striegl AM, Boyle JA, Meberg PJ, Bamburg JR. Neurodegenerative stimuli induce persisrent ADF/cofilin-actin rods that disrupt distal neurire function. Nat Cell Biol 2000; 2:628-36.
    • (2000) Nat Cell Biol , vol.2 , pp. 628-636
    • Minamide, L.S.1    Striegl, A.M.2    Boyle, J.A.3    Meberg, P.J.4    Bamburg, J.R.5
  • 8
    • 27644495116 scopus 로고    scopus 로고
    • Cofilin expression induces cofilin-actin rod formation and disrupts synaptic structure and function in Aplysia synapses
    • Jang DH, Han JH, Lee SH, Lee YS, Park H, Lee H, Kim H, Kaang BK. Cofilin expression induces cofilin-actin rod formation and disrupts synaptic structure and function in Aplysia synapses. Proc Natl Acad Sci USA 2005; 102:16072-77.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16072-16077
    • Jang, D.H.1    Han, J.H.2    Lee, S.H.3    Lee, Y.S.4    Park, H.5    Lee, H.6    Kim, H.7    Kaang, B.K.8
  • 9
    • 33751082967 scopus 로고    scopus 로고
    • Formation of actin-ADF/cofilin rods transiently retards decline of mitochondrial potential and ATP in stressed neurons
    • Bernstein BW, Chen H, Boyle JA, Bamburg JR. Formation of actin-ADF/cofilin rods transiently retards decline of mitochondrial potential and ATP in stressed neurons. Am J Physiol Cell Physiol 2006; 291:828-9.
    • (2006) Am J Physiol Cell Physiol , vol.291 , pp. 828-829
    • Bernstein, B.W.1    Chen, H.2    Boyle, J.A.3    Bamburg, J.R.4
  • 10
    • 0036573221 scopus 로고    scopus 로고
    • Formation of Hirano bodies in Dictyostelium and mammalian cells induced by expression of a modified form of an actin-crosslinking protein
    • Maselli AG, Davis R, Furukawa R, Fechheimer M. Formation of Hirano bodies in Dictyostelium and mammalian cells induced by expression of a modified form of an actin-crosslinking protein. J Cell Sci 2002; 115:1939-49.
    • (2002) J Cell Sci , vol.115 , pp. 1939-1949
    • Maselli, A.G.1    Davis, R.2    Furukawa, R.3    Fechheimer, M.4
  • 11
    • 0042232060 scopus 로고    scopus 로고
    • Formation of Hirano bodies induced by expression of an actin cross-linking protein with a gain-of-function mutation
    • Maselli AG, Furukawa R, Thomson SA, Davis RC, Fechheimer M. Formation of Hirano bodies induced by expression of an actin cross-linking protein with a gain-of-function mutation. Eukaryot Cell 2003; 2:778-87.
    • (2003) Eukaryot Cell , vol.2 , pp. 778-787
    • Maselli, A.G.1    Furukawa, R.2    Thomson, S.A.3    Davis, R.C.4    Fechheimer, M.5
  • 12
    • 38349002996 scopus 로고    scopus 로고
    • A cell culture model for investigation of Hirano bodies
    • Davis R, Furukawa R, Fechheimer M. A cell culture model for investigation of Hirano bodies. Acta Neuropathol 2008; 115:205-17.
    • (2008) Acta Neuropathol , vol.115 , pp. 205-217
    • Davis, R.1    Furukawa, R.2    Fechheimer, M.3
  • 13
    • 0031914182 scopus 로고    scopus 로고
    • Formation of F-actin aggregates in cells treated with acrin stabilizing drugs
    • Lee E, Shelden EA, Knecht DA. Formation of F-actin aggregates in cells treated with acrin stabilizing drugs. Cell Motil Cytoskeleton 1998; 39:122-33.
    • (1998) Cell Motil Cytoskeleton , vol.39 , pp. 122-133
    • Lee, E.1    Shelden, E.A.2    Knecht, D.A.3
  • 15
    • 34250900953 scopus 로고    scopus 로고
    • LC3, an autophagosome marker, can be incorporated into protein aggregates independent of autophagy: Caution in the interpretation of LC3 localization
    • Kuma A, Matsui M, Mizushima N. LC3, an autophagosome marker, can be incorporated into protein aggregates independent of autophagy: Caution in the interpretation of LC3 localization. Autophagy 2007; 3:323-8.
    • (2007) Autophagy , vol.3 , pp. 323-328
    • Kuma, A.1    Matsui, M.2    Mizushima, N.3
  • 17
    • 34248594926 scopus 로고    scopus 로고
    • Collaboration of proteolytic systems
    • Mizushima N. Collaboration of proteolytic systems. Autophagy 2007; 3:179-80.
    • (2007) Autophagy , vol.3 , pp. 179-180
    • Mizushima, N.1
  • 18
    • 38549119467 scopus 로고    scopus 로고
    • Chaperones in control of protein disaggregation
    • Liberek K, Lewandowska A, Zietkiewicz S. Chaperones in control of protein disaggregation. EMBO J 2008; 27:328-35.
    • (2008) EMBO J , vol.27 , pp. 328-335
    • Liberek, K.1    Lewandowska, A.2    Zietkiewicz, S.3
  • 19
    • 2442624755 scopus 로고    scopus 로고
    • Microtubule disruption inhibits autophagosome-lysosome fusion: Implications for studying the roles of aggresomes in polyglutamine diseases
    • Webb JL, Ravikumar B, Rubinsztein DC. Microtubule disruption inhibits autophagosome-lysosome fusion: implications for studying the roles of aggresomes in polyglutamine diseases. Int J Biochem Cell Biol 2004; 36:2541-50.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2541-2550
    • Webb, J.L.1    Ravikumar, B.2    Rubinsztein, D.C.3
  • 20
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin
    • Iwata A, Riley BE, Johnston JA, Kopito RR. HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin. J Biol Chem 2005; 280:40282-92.
    • (2005) J Biol Chem , vol.280 , pp. 40282-40292
    • Iwata, A.1    Riley, B.E.2    Johnston, J.A.3    Kopito, R.R.4
  • 21
    • 0028244823 scopus 로고    scopus 로고
    • Bubb MR, Senderowicz AM, Sausville EA, Duncan KL, Korn ED. Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin. J Biol Chem 1994; 269:14869-71.
    • Bubb MR, Senderowicz AM, Sausville EA, Duncan KL, Korn ED. Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin. J Biol Chem 1994; 269:14869-71.
  • 22
    • 0035229253 scopus 로고    scopus 로고
    • An actin-specific reagent that promotes actin polymerization
    • Holzinger A. Jasplakinolide. An actin-specific reagent that promotes actin polymerization. Methods Mol Biol 2001; 161:109-20.
    • (2001) Methods Mol Biol , vol.161 , pp. 109-120
    • Jasplakinolide, H.A.1
  • 23
  • 24
    • 0142009674 scopus 로고    scopus 로고
    • Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions
    • Fuertes G, Martin de Llano JJ, Villarroya A, Rivett AJ, Knecht E. Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions. Biochem J 2003; 375:75-86.
    • (2003) Biochem J , vol.375 , pp. 75-86
    • Fuertes, G.1    Martin de Llano, J.J.2    Villarroya, A.3    Rivett, A.J.4    Knecht, E.5
  • 25
    • 0442323561 scopus 로고    scopus 로고
    • Autophagy: In sickness and in health
    • Cuervo AM. Autophagy: in sickness and in health. Trends Cell Biol 2004; 14:70-7.
    • (2004) Trends Cell Biol , vol.14 , pp. 70-77
    • Cuervo, A.M.1
  • 26
    • 27644484061 scopus 로고    scopus 로고
    • Autophagy: Molecular machinery for self-eating
    • Yorimitsu T, Klionsky DJ. Autophagy: molecular machinery for self-eating. Cell Death Differ 2005; 12:1542-52.
    • (2005) Cell Death Differ , vol.12 , pp. 1542-1552
    • Yorimitsu, T.1    Klionsky, D.J.2
  • 27
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein DC. The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 2006; 443:780-6.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 28
    • 34250822281 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy
    • Dice J. Chaperone-mediated autophagy. Autophagy 2007; 3:295-9.
    • (2007) Autophagy , vol.3 , pp. 295-299
    • Dice, J.1
  • 29
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima N, Levine B, Cuervo AM, Klionsky DJ. Autophagy fights disease through cellular self-digestion. Nature 2008; 451:1069-75.
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.