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Volumn 80, Issue , 2007, Pages 683-706

Cell-Free Assays for Mitochondria-Cytoskeleton Interactions

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN;

EID: 34147192982     PISSN: 0091679X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0091-679X(06)80031-2     Document Type: Review
Times cited : (2)

References (33)
  • 2
    • 0032526412 scopus 로고    scopus 로고
    • Interaction between mitochondria and the actin cytoskeleton in budding yeast requires two integral mitochondrial outer membrane proteins, Mmm1p and Mdm10p
    • Boldogh I., Vojtov N., Karmon S., and Pon L.A. Interaction between mitochondria and the actin cytoskeleton in budding yeast requires two integral mitochondrial outer membrane proteins, Mmm1p and Mdm10p. J. Cell Biol. 141 (1998) 1371-1381
    • (1998) J. Cell Biol. , vol.141 , pp. 1371-1381
    • Boldogh, I.1    Vojtov, N.2    Karmon, S.3    Pon, L.A.4
  • 3
    • 0035227199 scopus 로고    scopus 로고
    • Assaying actin-binding activity of mitochondria in yeast
    • Boldogh I.R., and Pon L.A. Assaying actin-binding activity of mitochondria in yeast. Methods Cell Biol. 65 (2001) 159-173
    • (2001) Methods Cell Biol. , vol.65 , pp. 159-173
    • Boldogh, I.R.1    Pon, L.A.2
  • 4
    • 4344703533 scopus 로고    scopus 로고
    • A type V myosin (Myo2p) and a Rab-like G-protein (Ypt11p) are required for retention of newly inherited mitochondria in yeast cells during cell division
    • Boldogh I.R., Ramcharan S.L., Yang H.C., and Pon L.A. A type V myosin (Myo2p) and a Rab-like G-protein (Ypt11p) are required for retention of newly inherited mitochondria in yeast cells during cell division. Mol. Biol. Cell. 15 (2004) 3994-4002
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 3994-4002
    • Boldogh, I.R.1    Ramcharan, S.L.2    Yang, H.C.3    Pon, L.A.4
  • 6
    • 0032614931 scopus 로고    scopus 로고
    • Studying the composition and function of centrosomes in vertebrates
    • Bornens M., and Moudjou M. Studying the composition and function of centrosomes in vertebrates. Methods Cell Biol. 61 (1999) 13-34
    • (1999) Methods Cell Biol. , vol.61 , pp. 13-34
    • Bornens, M.1    Moudjou, M.2
  • 8
    • 0035234395 scopus 로고    scopus 로고
    • An improved microscope for bead and surface-based motility assasy
    • Vernos I. (Ed), Humana Press, Totowa, NJ
    • Carter N., and Cross R. An improved microscope for bead and surface-based motility assasy. In: Vernos I. (Ed). "Kinesin Protocols" Vol. 164 (2001), Humana Press, Totowa, NJ 73-89
    • (2001) "Kinesin Protocols" , vol.164 , pp. 73-89
    • Carter, N.1    Cross, R.2
  • 9
    • 3343021928 scopus 로고    scopus 로고
    • Nerve growth factor signaling regulates motility and docking of axonal mitochondria
    • Chada S.R., and Hollenbeck P.J. Nerve growth factor signaling regulates motility and docking of axonal mitochondria. Curr. Biol. 14 (2004) 1272-1276
    • (2004) Curr. Biol. , vol.14 , pp. 1272-1276
    • Chada, S.R.1    Hollenbeck, P.J.2
  • 10
    • 0022458304 scopus 로고
    • Identification and characterization of a nuclear pore complex protein
    • Davis L.I., and Blobel G. Identification and characterization of a nuclear pore complex protein. Cell 45 (1986) 699-709
    • (1986) Cell , vol.45 , pp. 699-709
    • Davis, L.I.1    Blobel, G.2
  • 11
    • 0034641135 scopus 로고    scopus 로고
    • Tumor necrosis factor induces hyperphosphorylation of kinesin light chain and inhibits kinesin-mediated transport of mitochondria
    • De Vos K., Severin F., Van Herreweghe F., Vancompernolle K., Goossens V., Hyman A., and Grooten J. Tumor necrosis factor induces hyperphosphorylation of kinesin light chain and inhibits kinesin-mediated transport of mitochondria. J. Cell Biol. 149 (2000) 1207-1214
    • (2000) J. Cell Biol. , vol.149 , pp. 1207-1214
    • De Vos, K.1    Severin, F.2    Van Herreweghe, F.3    Vancompernolle, K.4    Goossens, V.5    Hyman, A.6    Grooten, J.7
  • 12
    • 0032476645 scopus 로고    scopus 로고
    • Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: Implications for Alzheimer's disease
    • Ebneth A., Godemann R., Stamer K., Illenberger S., Trinczek B., and Mandelkow E. Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: Implications for Alzheimer's disease. J. Cell Biol. 143 (1998) 777-794
    • (1998) J. Cell Biol. , vol.143 , pp. 777-794
    • Ebneth, A.1    Godemann, R.2    Stamer, K.3    Illenberger, S.4    Trinczek, B.5    Mandelkow, E.6
  • 13
    • 27644497685 scopus 로고    scopus 로고
    • A role for jsn1p in recruiting the arp2/3 complex to mitochondria in budding yeast
    • Fehrenbacher K.L., Boldogh I.R., and Pon L.A. A role for jsn1p in recruiting the arp2/3 complex to mitochondria in budding yeast. Mol. Biol. Cell 16 (2005) 5094-5102
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5094-5102
    • Fehrenbacher, K.L.1    Boldogh, I.R.2    Pon, L.A.3
  • 14
    • 9244263050 scopus 로고    scopus 로고
    • Live cell imaging of mitochondrial movement along actin cables in budding yeast
    • Fehrenbacher K.L., Yang H.C., Gay A.C., Huckaba T.M., and Pon L.A. Live cell imaging of mitochondrial movement along actin cables in budding yeast. Curr. Biol. 14 (2004) 1996-2004
    • (2004) Curr. Biol. , vol.14 , pp. 1996-2004
    • Fehrenbacher, K.L.1    Yang, H.C.2    Gay, A.C.3    Huckaba, T.M.4    Pon, L.A.5
  • 15
    • 30544452263 scopus 로고    scopus 로고
    • The axonal transport of mitochondria
    • Hollenbeck P.J., and Saxton W.M. The axonal transport of mitochondria. J. Cell Sci. 118 (2005) 5411-5419
    • (2005) J. Cell Sci. , vol.118 , pp. 5411-5419
    • Hollenbeck, P.J.1    Saxton, W.M.2
  • 16
    • 0025933084 scopus 로고
    • Preparation of marked microtubules for the assay of the polarity of microtubule-based motors by fluorescence
    • Hyman A.A. Preparation of marked microtubules for the assay of the polarity of microtubule-based motors by fluorescence. J. Cell Sci. Suppl. 14 (1991) 125-127
    • (1991) J. Cell Sci. Suppl. , vol.14 , pp. 125-127
    • Hyman, A.A.1
  • 17
    • 0035227730 scopus 로고    scopus 로고
    • Purification of kinesin from brain
    • Vernos I. (Ed), Humana Press, Totowa, NJ
    • Kuznetsov S.A., and Gelfand V.I. Purification of kinesin from brain. In: Vernos I. (Ed). "Kinesin Protocols" Vol. 164 (2001), Humana Press, Totowa, NJ 1-7
    • (2001) "Kinesin Protocols" , vol.164 , pp. 1-7
    • Kuznetsov, S.A.1    Gelfand, V.I.2
  • 18
    • 0028048692 scopus 로고
    • Yeast mitochondria contain ATP-sensitive, reversible actin-binding activity
    • Lazzarino D.A., Boldogh I., Smith M.G., Rosand J., and Pon L.A. Yeast mitochondria contain ATP-sensitive, reversible actin-binding activity. Mol. Biol. Cell 5 (1994) 807-818
    • (1994) Mol. Biol. Cell , vol.5 , pp. 807-818
    • Lazzarino, D.A.1    Boldogh, I.2    Smith, M.G.3    Rosand, J.4    Pon, L.A.5
  • 19
    • 0023803882 scopus 로고
    • Two monoclonal antibodies to actin: One muscle selective and one generally reactive
    • Lessard J.L. Two monoclonal antibodies to actin: One muscle selective and one generally reactive. Cell Motil. Cytoskeleton 10 (1988) 349-362
    • (1988) Cell Motil. Cytoskeleton , vol.10 , pp. 349-362
    • Lessard, J.L.1
  • 20
    • 0034694152 scopus 로고    scopus 로고
    • Role of microtubules and actin filaments in the movement of mitochondria in the axons and dendrites of cultured hippocampal neurons
    • Ligon L.A., and Steward O. Role of microtubules and actin filaments in the movement of mitochondria in the axons and dendrites of cultured hippocampal neurons. J. Comp. Neurol. 427 (2000) 351-361
    • (2000) J. Comp. Neurol. , vol.427 , pp. 351-361
    • Ligon, L.A.1    Steward, O.2
  • 21
    • 0027533201 scopus 로고
    • Steric inhibition of cytoplasmic dynein and kinesin motility by MAP2
    • Lopez L.A., and Sheetz M.P. Steric inhibition of cytoplasmic dynein and kinesin motility by MAP2. Cell Motil. Cytoskeleton 24 (1993) 1-16
    • (1993) Cell Motil. Cytoskeleton , vol.24 , pp. 1-16
    • Lopez, L.A.1    Sheetz, M.P.2
  • 23
    • 0021711717 scopus 로고
    • Microtubule assembly nucleated by isolated centrosomes
    • Mitchison T., and Kirschner M. Microtubule assembly nucleated by isolated centrosomes. Nature 312 (1984) 232-237
    • (1984) Nature , vol.312 , pp. 232-237
    • Mitchison, T.1    Kirschner, M.2
  • 25
    • 0035220960 scopus 로고    scopus 로고
    • In vitro reconstitution of endosome motiltiy along microtubules
    • Vernos I. (Ed), Humana Press, Totowa, NJ
    • Nielsen E., Severin F., Hyman A., and Zerial M. In vitro reconstitution of endosome motiltiy along microtubules. In: Vernos I. (Ed). "Kinesin Protocols" Vol. 164 (2001), Humana Press, Totowa, NJ 133-146
    • (2001) "Kinesin Protocols" , vol.164 , pp. 133-146
    • Nielsen, E.1    Severin, F.2    Hyman, A.3    Zerial, M.4
  • 26
    • 0027270310 scopus 로고
    • Analysis of the sequence requirements for glycosylphosphatidylinositol anchoring of Saccharomyces cerevisiae Gas1 protein
    • Nuoffer C., Horvath A., and Riezman H. Analysis of the sequence requirements for glycosylphosphatidylinositol anchoring of Saccharomyces cerevisiae Gas1 protein. J. Biol. Chem. 268 (1993) 10558-10563
    • (1993) J. Biol. Chem. , vol.268 , pp. 10558-10563
    • Nuoffer, C.1    Horvath, A.2    Riezman, H.3
  • 27
    • 0031000089 scopus 로고    scopus 로고
    • Mitochondrial association of a plus end-directed microtubule motor expressed during mitosis in Drosophila
    • Pereira A.J., Dalby B., Stewart R.J., Doxsey S.J., and Goldstein L.S. Mitochondrial association of a plus end-directed microtubule motor expressed during mitosis in Drosophila. J. Cell Biol. 136 (1997) 1081-1090
    • (1997) J. Cell Biol. , vol.136 , pp. 1081-1090
    • Pereira, A.J.1    Dalby, B.2    Stewart, R.J.3    Doxsey, S.J.4    Goldstein, L.S.5
  • 28
    • 1042278630 scopus 로고    scopus 로고
    • Organelle inheritance in plant cell division: The actin cytoskeleton is required for unbiased inheritance of chloroplasts, mitochondria and endoplasmic reticulum in dividing protoplasts
    • Sheahan M.B., Rose R.J., and McCurdy D.W. Organelle inheritance in plant cell division: The actin cytoskeleton is required for unbiased inheritance of chloroplasts, mitochondria and endoplasmic reticulum in dividing protoplasts. Plant J. 37 (2004) 379-390
    • (2004) Plant J. , vol.37 , pp. 379-390
    • Sheahan, M.B.1    Rose, R.J.2    McCurdy, D.W.3
  • 29
    • 0027058051 scopus 로고
    • Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum
    • Stirling C.J., Rothblatt J., Hosobuchi M., Deshaies R., and Schekman R. Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum. Mol. Biol. Cell 3 (1992) 129-142
    • (1992) Mol. Biol. Cell , vol.3 , pp. 129-142
    • Stirling, C.J.1    Rothblatt, J.2    Hosobuchi, M.3    Deshaies, R.4    Schekman, R.5
  • 30
    • 0033987381 scopus 로고    scopus 로고
    • Mitochondrial movement and morphology depend on an intact actin cytoskeleton in Aspergillus nidulans
    • Suelmann R., and Fischer R. Mitochondrial movement and morphology depend on an intact actin cytoskeleton in Aspergillus nidulans. Cell Motil. Cytoskeleton 45 (2000) 42-50
    • (2000) Cell Motil. Cytoskeleton , vol.45 , pp. 42-50
    • Suelmann, R.1    Fischer, R.2
  • 31
    • 0032568790 scopus 로고    scopus 로고
    • Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria
    • Tanaka Y., Kanai Y., Okada Y., Nonaka S., Takeda S., Harada A., and Hirokawa N. Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria. Cell 93 (1998) 1147-1158
    • (1998) Cell , vol.93 , pp. 1147-1158
    • Tanaka, Y.1    Kanai, Y.2    Okada, Y.3    Nonaka, S.4    Takeda, S.5    Harada, A.6    Hirokawa, N.7
  • 32
    • 0036009370 scopus 로고    scopus 로고
    • Plant mitochondria move on F-actin, but their positioning in the cortical cytoplasm depends on both F-actin and microtubules
    • Van Gestel K., Kohler R.H., and Verbelen J.P. Plant mitochondria move on F-actin, but their positioning in the cortical cytoplasm depends on both F-actin and microtubules. J. Exp. Bot. 53 (2002) 659-667
    • (2002) J. Exp. Bot. , vol.53 , pp. 659-667
    • Van Gestel, K.1    Kohler, R.H.2    Verbelen, J.P.3
  • 33
    • 0033533697 scopus 로고    scopus 로고
    • A retention mechanism for distribution of mitochondria during cell division in budding yeast
    • Yang H.C., Palazzo A., Swayne T.C., and Pon L.A. A retention mechanism for distribution of mitochondria during cell division in budding yeast. Curr. Biol. 9 (1999) 1111-1114
    • (1999) Curr. Biol. , vol.9 , pp. 1111-1114
    • Yang, H.C.1    Palazzo, A.2    Swayne, T.C.3    Pon, L.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.