메뉴 건너뛰기




Volumn 18, Issue 11, 1999, Pages 2991-3006

Recruitment of an alternatively spliced form of synaptojanin 2 to mitochondria by the interaction with the PDZ domain of a mitochondrial outer membrane protein

Author keywords

Dynamin; Inositol 5' phosphatase; Mitochondria clustering; Phosphoinositide; Signal anchor sequence

Indexed keywords

INOSITOL PENTAKISPHOSPHATE; MESSENGER RNA; MUTANT PROTEIN; OUTER MEMBRANE PROTEIN;

EID: 0033152496     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.11.2991     Document Type: Article
Times cited : (151)

References (149)
  • 1
    • 0039064824 scopus 로고
    • Mitochondria are associated with microtubules and not with intermediate filaments in cultured fibroblasts
    • Ball, E.H. and Singer, S.J. (1982) Mitochondria are associated with microtubules and not with intermediate filaments in cultured fibroblasts. Proc. Natl Acad. Sci. USA, 79, 123-126.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 123-126
    • Ball, E.H.1    Singer, S.J.2
  • 2
    • 0030695315 scopus 로고    scopus 로고
    • Amphiphysin I is associated with coated endocytic intermediates and undergoes stimulation-dependent dephosphorylation in nerve terminals
    • Bauerfeind, R., Takei, K. and De Camilli, P. (1997) Amphiphysin I is associated with coated endocytic intermediates and undergoes stimulation-dependent dephosphorylation in nerve terminals. J. Biol. Chem., 272, 30984-30992.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30984-30992
    • Bauerfeind, R.1    Takei, K.2    De Camilli, P.3
  • 3
    • 0031059722 scopus 로고    scopus 로고
    • Mdm12p, a component required for mitochondrial inheritance that is conserved between budding and fission yeast
    • Berger, K.H., Sogo, L.F. and Yaffe, M.P. (1997) Mdm12p, a component required for mitochondrial inheritance that is conserved between budding and fission yeast. J. Cell Biol., 136, 545-553.
    • (1997) J. Cell Biol. , vol.136 , pp. 545-553
    • Berger, K.H.1    Sogo, L.F.2    Yaffe, M.P.3
  • 4
    • 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. (1998) Interaction between mitochondria and the actin cytoskeleton in budding yeast requires two integral mitochondrial outer membrane proteins, Mmm1p and Mdm10p. J. Cell Biol., 141, 1371-1381.
    • (1998) J. Cell Biol. , vol.141 , pp. 1371-1381
    • Boldogh, I.1    Vojtov, N.2    Karmon, S.3    Pon, L.A.4
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0028129071 scopus 로고
    • MMM1 encodes a mitochondrial outer membrane protein essential for establishing and maintaining the structure of yeast mitochondria
    • Burgess, S.M., Delannoy, M. and Jensen, R.E. (1994) MMM1 encodes a mitochondrial outer membrane protein essential for establishing and maintaining the structure of yeast mitochondria. J. Cell Biol., 126, 1375-1391.
    • (1994) J. Cell Biol. , vol.126 , pp. 1375-1391
    • Burgess, S.M.1    Delannoy, M.2    Jensen, R.E.3
  • 7
    • 0026048669 scopus 로고
    • Colocalization of synaptophysin with transferrin receptors: Implications for synaptic vesicle biogenesis
    • Cameron, P.L., Sudhof, T.C., Jahn, R. and De Camilli, P. (1991) Colocalization of synaptophysin with transferrin receptors: implications for synaptic vesicle biogenesis. J. Cell Biol., 115, 151-164.
    • (1991) J. Cell Biol. , vol.115 , pp. 151-164
    • Cameron, P.L.1    Sudhof, T.C.2    Jahn, R.3    De Camilli, P.4
  • 8
    • 0031720535 scopus 로고    scopus 로고
    • Differential distribution of dynamin isoforms in mammalian cells
    • Cao, H., Garcia, F. and McNiven, M.A. (1998) Differential distribution of dynamin isoforms in mammalian cells. Mol. Biol. Cell, 9, 2595-2609.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2595-2609
    • Cao, H.1    Garcia, F.2    McNiven, M.A.3
  • 9
    • 0026492629 scopus 로고
    • The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein
    • Cho, K.O., Hunt, C.A. and Kennedy, M.B. (1992) The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein. Neuron, 9, 929-942.
    • (1992) Neuron , vol.9 , pp. 929-942
    • Cho, K.O.1    Hunt, C.A.2    Kennedy, M.B.3
  • 10
    • 0024828304 scopus 로고
    • Mutations in the SAC1 gene suppress defects in yeast Golgi and yeast actin function
    • Cleves, A.E., Novick, P.J. and Bankaitis, V.A. (1989) Mutations in the SAC1 gene suppress defects in yeast Golgi and yeast actin function. J. Cell Biol., 109, 2939-2950.
    • (1989) J. Cell Biol. , vol.109 , pp. 2939-2950
    • Cleves, A.E.1    Novick, P.J.2    Bankaitis, V.A.3
  • 11
    • 0019958455 scopus 로고
    • Organelle-cytoskeleton relationships in fibroblasts: Mitochondria, Golgi apparatus and endoplasmic reticulum in phases of movement and growth
    • Couchman, J.R. and Rees, D.A. (1982) Organelle-cytoskeleton relationships in fibroblasts: mitochondria, Golgi apparatus and endoplasmic reticulum in phases of movement and growth. Eur. J. Cell Biol., 27, 47-54.
    • (1982) Eur. J. Cell Biol. , vol.27 , pp. 47-54
    • Couchman, J.R.1    Rees, D.A.2
  • 13
    • 0031470335 scopus 로고    scopus 로고
    • Import of lipids into mitochondria
    • Daum, G. and Vance, J.E. (1997) Import of lipids into mitochondria. Prog. Lipid Res., 36, 103-130.
    • (1997) Prog. Lipid Res. , vol.36 , pp. 103-130
    • Daum, G.1    Vance, J.E.2
  • 14
    • 0030060326 scopus 로고    scopus 로고
    • A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals
    • David, C., McPherson, P.S., Mundigl, O. and de Camilli, P. (1996) A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals. Proc. Natl Acad. Sci. USA. 93, 331-335.
    • (1996) Proc. Natl Acad. Sci. USA. , vol.93 , pp. 331-335
    • David, C.1    McPherson, P.S.2    Mundigl, O.3    De Camilli, P.4
  • 16
    • 0030604722 scopus 로고    scopus 로고
    • Crystal structures of a complexed and peptide-free membrane protein-binding domain: Molecular basis of peptide recognition by PDZ
    • Doyle, D.A., Lee, A., Lewis, J., Kim, E., Sheng, M. and MacKinnon, R. (1996) Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell, 85, 1067-1076.
    • (1996) Cell , vol.85 , pp. 1067-1076
    • Doyle, D.A.1    Lee, A.2    Lewis, J.3    Kim, E.4    Sheng, M.5    MacKinnon, R.6
  • 17
    • 0027765526 scopus 로고
    • Actin structure and function: Roles in mitochondrial organization and morphogenesis in budding yeast and identification of the phalloidin-binding site
    • Drubin, D.G., Jones, H.D. and Wertman, K.F. (1993) Actin structure and function: roles in mitochondrial organization and morphogenesis in budding yeast and identification of the phalloidin-binding site. Mol. Biol. Cell, 4, 1277-1294.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1277-1294
    • Drubin, D.G.1    Jones, H.D.2    Wertman, K.F.3
  • 18
    • 0029074236 scopus 로고
    • Fast axonal transport of kinesin in the rat visual system: Functionality of kinesin heavy chain isoforms
    • Elluru, R.G., Bloom, G.S. and Brady, S.T. (1995) Fast axonal transport of kinesin in the rat visual system: functionality of kinesin heavy chain isoforms. Mol. Biol. Cell, 6, 21-40.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 21-40
    • Elluru, R.G.1    Bloom, G.S.2    Brady, S.T.3
  • 19
    • 0030734979 scopus 로고    scopus 로고
    • PDZ domains and the formation of protein networks at the plasma membrane
    • Fanning, A.S. and Anderson, J.M. (1998) PDZ domains and the formation of protein networks at the plasma membrane. Curr. Top. Microbiol. Immunol., 228, 209-233.
    • (1998) Curr. Top. Microbiol. Immunol. , vol.228 , pp. 209-233
    • Fanning, A.S.1    Anderson, J.M.2
  • 20
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki, Y., Hubbard, A.L., Fowler, S. and Lazarow, P.B. (1982) Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J. Cell Biol., 93, 97-102.
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 21
    • 0026345013 scopus 로고
    • Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein
    • Gill, S.R., Schroer, T.A., Szilak, I., Steuer, E.R., Sheetz, M.P. and Cleveland, D.W. (1991) Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein. J. Cell Biol., 115, 1639-1650.
    • (1991) J. Cell Biol. , vol.115 , pp. 1639-1650
    • Gill, S.R.1    Schroer, T.A.2    Szilak, I.3    Steuer, E.R.4    Sheetz, M.P.5    Cleveland, D.W.6
  • 22
    • 0027362241 scopus 로고
    • The GTPase dynamin binds to and is activated by a subset of SH3 domains
    • Gout, I. et al. (1993) The GTPase dynamin binds to and is activated by a subset of SH3 domains. Cell, 75, 25-36.
    • (1993) Cell , vol.75 , pp. 25-36
    • Gout, I.1
  • 23
    • 0031434562 scopus 로고    scopus 로고
    • Synaptojanin 1: Localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15
    • Haffner, C., Takei, K., Chen, H., Ringstad, N., Hudson, A., Butler, M.H., Salcini, A.E., Di Fiore, P.P. and De Camilli, P. (1997) Synaptojanin 1: localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15. FEBS Lett., 419, 175-180.
    • (1997) FEBS Lett. , vol.419 , pp. 175-180
    • Haffner, C.1    Takei, K.2    Chen, H.3    Ringstad, N.4    Hudson, A.5    Butler, M.H.6    Salcini, A.E.7    Di Fiore, P.P.8    De Camilli, P.9
  • 24
    • 0031440879 scopus 로고    scopus 로고
    • Developmentally regulated mitochondrial fusion mediated by a conserved, novel, predicted GTPase
    • Hales, K.G. and Fuller, M.T. (1997) Developmentally regulated mitochondrial fusion mediated by a conserved, novel, predicted GTPase. Cell, 90, 121-129.
    • (1997) Cell , vol.90 , pp. 121-129
    • Hales, K.G.1    Fuller, M.T.2
  • 25
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow, E. and Lane, D. (1988) Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 26
    • 0008688565 scopus 로고
    • Association of mitochondria with microtubules in cultured cells
    • Heggeness, M.H., Simon, M. and Singer, S.J. (1978) Association of mitochondria with microtubules in cultured cells. Proc. Natl Acad. Sci. USA, 75, 3863-3866.
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 3863-3866
    • Heggeness, M.H.1    Simon, M.2    Singer, S.J.3
  • 27
    • 0030951615 scopus 로고    scopus 로고
    • The yeast gene, MDM20, is necessary for mitochondrial inheritance and organization of the actin cytoskeleton
    • Hermann, G.J., King, E.J. and Shaw, J.M. (1997) The yeast gene, MDM20, is necessary for mitochondrial inheritance and organization of the actin cytoskeleton. J. Cell Biol., 137, 141-153.
    • (1997) J. Cell Biol. , vol.137 , pp. 141-153
    • Hermann, G.J.1    King, E.J.2    Shaw, J.M.3
  • 28
    • 0024234855 scopus 로고
    • CLUSTAL: A package for performing multiple sequence alignment on a microcomputer
    • Higgins, D.G. and Sharp, P.M. (1988) CLUSTAL: a package for performing multiple sequence alignment on a microcomputer. Gene, 73, 237-244.
    • (1988) Gene , vol.73 , pp. 237-244
    • Higgins, D.G.1    Sharp, P.M.2
  • 29
    • 0032559260 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins and the mechanism of organelle transport
    • Hirokawa, N. (1998) Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science, 279, 519-526.
    • (1998) Science , vol.279 , pp. 519-526
    • Hirokawa, N.1
  • 30
    • 0023794908 scopus 로고
    • Diverse effects of beta-tubulin mutations on microtubule formation and function
    • Huffaker, T.C., Thomas, J.H. and Botstein, D. (1988) Diverse effects of beta-tubulin mutations on microtubule formation and function. J. Cell Biol., 106, 1997-2010.
    • (1988) J. Cell Biol. , vol.106 , pp. 1997-2010
    • Huffaker, T.C.1    Thomas, J.H.2    Botstein, D.3
  • 31
    • 0031799717 scopus 로고    scopus 로고
    • Identification and functional characterization of a novel human protein highly related to the yeast dynamin-like GTPase Vps1p
    • Imoto, M., Tachibana, I. and Urrutia, R. (1998) Identification and functional characterization of a novel human protein highly related to the yeast dynamin-like GTPase Vps1p. J. Cell Sci., 111, 1341-1349.
    • (1998) J. Cell Sci. , vol.111 , pp. 1341-1349
    • Imoto, M.1    Tachibana, I.2    Urrutia, R.3
  • 32
    • 0027300689 scopus 로고
    • The 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: cDNA cloning and immunoelectron microscopy
    • Itoh, M., Nagafuchi, A., Yonemura, S., Kitani-Yasuda, T., Tsukita, S. and Tsukita, S. (1993) The 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: cDNA cloning and immunoelectron microscopy. J. Cell Biol., 121, 491-502.
    • (1993) J. Cell Biol. , vol.121 , pp. 491-502
    • Itoh, M.1    Nagafuchi, A.2    Yonemura, S.3    Kitani-Yasuda, T.4    Tsukita, S.5    Tsukita, S.6
  • 34
    • 0031985126 scopus 로고    scopus 로고
    • Dymple, a novel dynamin-like high molecular weight GTPase lacking a proline-rich carboxyl-terminal domain in mammalian cells
    • Kamimoto, T., Nagai, Y., Onogi, H., Muro, Y., Wakabayashi, T. and Hagiwara, M. (1998) Dymple, a novel dynamin-like high molecular weight GTPase lacking a proline-rich carboxyl-terminal domain in mammalian cells. J. Biol. Chem., 273, 1044-1051.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1044-1051
    • Kamimoto, T.1    Nagai, Y.2    Onogi, H.3    Muro, Y.4    Wakabayashi, T.5    Hagiwara, M.6
  • 35
    • 0031883078 scopus 로고    scopus 로고
    • A specific light chain of kinesin associates with mitochondria in cultured cells
    • Khodjakov, A., Lizunova, E.M., Minin, A.A., Koonce, M.P. and Gyoeva, F.K. (1998) A specific light chain of kinesin associates with mitochondria in cultured cells. Mol. Biol. Cell, 9, 333-343.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 333-343
    • Khodjakov, A.1    Lizunova, E.M.2    Minin, A.A.3    Koonce, M.P.4    Gyoeva, F.K.5
  • 36
    • 2642714117 scopus 로고    scopus 로고
    • Developmentally regulated alternative splicing in a novel synaptojanin
    • Khvotchev, M. and Südhof, T.C. (1998) Developmentally regulated alternative splicing in a novel synaptojanin. J. Biol. Chem., 273, 2306-2311.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2306-2311
    • Khvotchev, M.1    Südhof, T.C.2
  • 39
    • 0028897142 scopus 로고
    • Nucleotide binding by the synapse associated protein SAP90
    • Kistner, U., Garner, C.C. and Linial, M. (1995) Nucleotide binding by the synapse associated protein SAP90. FEBS Lett., 359, 159-163.
    • (1995) FEBS Lett. , vol.359 , pp. 159-163
    • Kistner, U.1    Garner, C.C.2    Linial, M.3
  • 40
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • Kornau, H.C., Schenker, L.T., Kennedy, M.B. and Seeburg, P.H. (1995) Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science, 269, 1737-1740.
    • (1995) Science , vol.269 , pp. 1737-1740
    • Kornau, H.C.1    Schenker, L.T.2    Kennedy, M.B.3    Seeburg, P.H.4
  • 41
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. and Doolittle, R.F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol., 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 42
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 43
    • 0029788216 scopus 로고    scopus 로고
    • Interaction of the N-methyl-D-aspartate receptor complex with a novel synapse-associated protein, SAP102
    • Lau, L.F., Mammen, A., Ehlers, M.D., Kindler, S., Chung, W.J., Garner, C.C. and Huganir, R.L. (1996) Interaction of the N-methyl-D-aspartate receptor complex with a novel synapse-associated protein, SAP102. J. Biol. Chem., 271, 21622-21628.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21622-21628
    • Lau, L.F.1    Mammen, A.2    Ehlers, M.D.3    Kindler, S.4    Chung, W.J.5    Garner, C.C.6    Huganir, R.L.7
  • 44
    • 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. (1994) Yeast mitochondria contain ATP-sensitive, reversible actin-binding activity. Mol. Biol. Cell, 5, 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
  • 46
    • 0028096801 scopus 로고
    • Cloning and characterization of hdlg: The human homologue of the Drosophila discs large tumor suppressor binds to protein 4
    • Lue, R.A., Marfatia, S.M., Branton, D. and Chishti, A.H. (1994) Cloning and characterization of hdlg: the human homologue of the Drosophila discs large tumor suppressor binds to protein 4. Proc. Natl Acad. Sci. USA, 91, 9818-9822.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 9818-9822
    • Lue, R.A.1    Marfatia, S.M.2    Branton, D.3    Chishti, A.H.4
  • 47
    • 0030809534 scopus 로고    scopus 로고
    • Novel genes involved in endosomal traffic in yeast revealed by suppression of a targeting-defective plasma membrane ATPase mutant
    • Luo, W. and Chang, A. (1997) Novel genes involved in endosomal traffic in yeast revealed by suppression of a targeting-defective plasma membrane ATPase mutant. J. Cell Biol., 138, 731-746.
    • (1997) J. Cell Biol. , vol.138 , pp. 731-746
    • Luo, W.1    Chang, A.2
  • 48
    • 0032407241 scopus 로고    scopus 로고
    • Phosphoinositide lipids as signaling molecules: Common themes for signal transduction, cytoskeletal regulation and membrane trafficking
    • Martin, T.F.J. (1998) Phosphoinositide lipids as signaling molecules: common themes for signal transduction, cytoskeletal regulation and membrane trafficking. Annu. Rev. Cell Dev. Biol., 14, 231-264.
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 231-264
    • Martin, T.F.J.1
  • 49
    • 0025076787 scopus 로고
    • Temperature-sensitive yeast mutants defective in mitochondrial inheritance
    • McConnell, S.J., Stewart, L.C., Talin, A. and Yaffe, M.P. (1990) Temperature-sensitive yeast mutants defective in mitochondrial inheritance. J. Cell Biol., 111, 967-976.
    • (1990) J. Cell Biol. , vol.111 , pp. 967-976
    • McConnell, S.J.1    Stewart, L.C.2    Talin, A.3    Yaffe, M.P.4
  • 51
    • 0028073746 scopus 로고
    • P145, a major Grb2-binding protein in brain, is co-localized with dynamin in nerve terminals where it undergoes activity-dependent dephosphorylation
    • McPherson, P.S., Takei, K., Schmid, S.L. and De Camilli, P. (1994b) p145, a major Grb2-binding protein in brain, is co-localized with dynamin in nerve terminals where it undergoes activity-dependent dephosphorylation. J. Biol. Chem., 269, 30132-30139.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30132-30139
    • McPherson, P.S.1    Takei, K.2    Schmid, S.L.3    De Camilli, P.4
  • 52
    • 2642622186 scopus 로고    scopus 로고
    • A presynaptic inositol-5-phosphatase
    • McPherson, P.S. et al. (1996) A presynaptic inositol-5-phosphatase. Nature, 379, 353-357.
    • (1996) Nature , vol.379 , pp. 353-357
    • McPherson, P.S.1
  • 53
    • 0030856743 scopus 로고    scopus 로고
    • Synaptojanin forms two separate complexes in the nerve terminal
    • Micheva, K.D., Kay, B.K. and McPherson, P.S. (1997) Synaptojanin forms two separate complexes in the nerve terminal. J. Biol. Chem., 272, 27239-27245.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27239-27245
    • Micheva, K.D.1    Kay, B.K.2    McPherson, P.S.3
  • 54
    • 0028821852 scopus 로고
    • Protein import into mammalian mitochondria
    • Mihara, K. and Omura, T. (1995) Protein import into mammalian mitochondria. Methods Enzymol., 260, 302-310.
    • (1995) Methods Enzymol. , vol.260 , pp. 302-310
    • Mihara, K.1    Omura, T.2
  • 55
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller, J.H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 56
    • 0028906288 scopus 로고
    • Molecular characterization and spatial distribution of SAP97, a novel presynaptic protein homologous to SAP90 and the Drosophila discs-large tumor suppressor protein
    • Müller, B.M., Kistner, U., Veh, R.W., Cases-Langhoff, C., Becker, B., Gundelfinger, E.D. and Garner, C.C. (1995) Molecular characterization and spatial distribution of SAP97, a novel presynaptic protein homologous to SAP90 and the Drosophila discs-large tumor suppressor protein. J. Neurosci., 15, 2354-2366.
    • (1995) J. Neurosci. , vol.15 , pp. 2354-2366
    • Müller, B.M.1    Kistner, U.2    Veh, R.W.3    Cases-Langhoff, C.4    Becker, B.5    Gundelfinger, E.D.6    Garner, C.C.7
  • 57
    • 0039793622 scopus 로고    scopus 로고
    • SAP102, a novel postsynaptic protein that interacts with NMDA receptor complexes in vivo
    • Müller, B.M. et al. (1996) SAP102, a novel postsynaptic protein that interacts with NMDA receptor complexes in vivo. Neuron, 17, 255-265.
    • (1996) Neuron , vol.17 , pp. 255-265
    • Müller, B.M.1
  • 58
    • 0028641560 scopus 로고
    • KIF1B, a novel microtubule plus end-directed monomeric motor protein for transport of mitochondria
    • Nangaku, M., Sato-Yoshitake, R., Okada, Y., Noda, Y., Takemura, R., Yamazaki, H. and Hirokawa, N. (1994) KIF1B, a novel microtubule plus end-directed monomeric motor protein for transport of mitochondria. Cell, 79, 1209-1220.
    • (1994) Cell , vol.79 , pp. 1209-1220
    • Nangaku, M.1    Sato-Yoshitake, R.2    Okada, Y.3    Noda, Y.4    Takemura, R.5    Yamazaki, H.6    Hirokawa, N.7
  • 59
    • 0030707815 scopus 로고    scopus 로고
    • Synaptojanin 2, a novel synaptojanin isoform with a distinct targeting domain and expression pattern
    • Nemoto, Y., Arribas, M., Haffner, C. and DeCamilli, P. (1997) Synaptojanin 2, a novel synaptojanin isoform with a distinct targeting domain and expression pattern. J. Biol. Chem., 272, 30817-30821.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30817-30821
    • Nemoto, Y.1    Arribas, M.2    Haffner, C.3    DeCamilli, P.4
  • 60
    • 0022574421 scopus 로고
    • Import and processing of hybrid proteins by mammalian mitochondria in vitro
    • Nguyen, M., Argan, C., Lusty, C.J. and Shore, G.C. (1986) Import and processing of hybrid proteins by mammalian mitochondria in vitro. J. Biol. Chem., 261, 800-805.
    • (1986) J. Biol. Chem. , vol.261 , pp. 800-805
    • Nguyen, M.1    Argan, C.2    Lusty, C.J.3    Shore, G.C.4
  • 61
    • 0029946167 scopus 로고    scopus 로고
    • Interaction between the C terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases
    • Niethammer, M., Kim, E. and Sheng, M. (1996) Interaction between the C terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases. J. Neurosci., 16, 2157-2163.
    • (1996) J. Neurosci. , vol.16 , pp. 2157-2163
    • Niethammer, M.1    Kim, E.2    Sheng, M.3
  • 62
    • 0024549504 scopus 로고
    • Suppressors of yeast actin mutations
    • Novick, P., Osmond, B.C. and Botstein, D. (1989) Suppressors of yeast actin mutations. Genetics, 121, 659-674.
    • (1989) Genetics , vol.121 , pp. 659-674
    • Novick, P.1    Osmond, B.C.2    Botstein, D.3
  • 64
    • 0030812638 scopus 로고    scopus 로고
    • The HtrA family of serine proteases
    • Pallen, M.J. and Wren, B.W. (1997) The HtrA family of serine proteases. Mol. Microbiol., 26, 209-221.
    • (1997) Mol. Microbiol. , vol.26 , pp. 209-221
    • Pallen, M.J.1    Wren, B.W.2
  • 65
    • 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. (1997) Mitochondrial association of a plus end-directed microtubule motor expressed during mitosis in Drosophila. J. Cell Biol., 136, 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
  • 67
    • 0032919866 scopus 로고    scopus 로고
    • Syndapin I, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein
    • Qualmann, B., Roos, J., DiGregorio, P.J. and Kelly, R.B. (1999) Syndapin I, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein. Mol. Biol. Cell, 10, 501-513.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 501-513
    • Qualmann, B.1    Roos, J.2    DiGregorio, P.J.3    Kelly, R.B.4
  • 68
    • 0029773891 scopus 로고    scopus 로고
    • Tissue-specific alternative splicing generates two synaptojanin isoforms with differential membrane binding properties
    • Ramjaun, A.R. and McPherson, P.S. (1996) Tissue-specific alternative splicing generates two synaptojanin isoforms with differential membrane binding properties. J. Biol. Chem., 271, 24856-24861.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24856-24861
    • Ramjaun, A.R.1    McPherson, P.S.2
  • 69
    • 0030908644 scopus 로고    scopus 로고
    • Identification and characterization of a nerve terminal-enriched amphiphysin isoform
    • Ramjaun, A.R., Micheva, K.D., Bouchelet, I. and McPherson, P.S. (1997) Identification and characterization of a nerve terminal-enriched amphiphysin isoform. J. Biol. Chem., 272, 16700-16706.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16700-16706
    • Ramjaun, A.R.1    Micheva, K.D.2    Bouchelet, I.3    McPherson, P.S.4
  • 70
    • 0030739938 scopus 로고    scopus 로고
    • The SH3p4/SH3p8/ SH3p13 protein family: Binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain
    • Ringstad, N., Nemoto, Y. and De Camilli, P. (1997) The SH3p4/SH3p8/ SH3p13 protein family: binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain. Proc. Natl Acad. Sci. USA, 94, 8569-8574.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 8569-8574
    • Ringstad, N.1    Nemoto, Y.2    De Camilli, P.3
  • 72
    • 0027723051 scopus 로고
    • Microtubule-dependent control of cell shape and pseudopodial activity is inhibited by the antibody to kinesin motor domain
    • Rodionov, V.I., Gyoeva, F.K., Tanaka, E., Bershadsky, A.D., Vasiliev, J.M. and Gelfand, V.I. (1993) Microtubule-dependent control of cell shape and pseudopodial activity is inhibited by the antibody to kinesin motor domain. J. Cell Biol., 123, 1811-1820.
    • (1993) J. Cell Biol. , vol.123 , pp. 1811-1820
    • Rodionov, V.I.1    Gyoeva, F.K.2    Tanaka, E.3    Bershadsky, A.D.4    Vasiliev, J.M.5    Gelfand, V.I.6
  • 73
    • 0023920458 scopus 로고
    • Mitochondrial presequences
    • Roise, D. and Schatz, G. (1988) Mitochondrial presequences. J. Biol. Chem., 263, 4509-4511.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4509-4511
    • Roise, D.1    Schatz, G.2
  • 74
    • 0030747392 scopus 로고    scopus 로고
    • The role of lipid signaling in constitutive membrane traffic
    • Roth, M.G. and Sternweis, P.C. (1997) The role of lipid signaling in constitutive membrane traffic. Curr. Opin. Cell Biol., 9, 519-526.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 519-526
    • Roth, M.G.1    Sternweis, P.C.2
  • 76
    • 0032499612 scopus 로고    scopus 로고
    • Molecular cloning of multiple isoforms of synaptojanin 2 and assignment of the gene to mouse chromosome 17A2-3
    • Seet, L.F., Cho, S., Hessel, A. and Dumont, D.J. (1998) Molecular cloning of multiple isoforms of synaptojanin 2 and assignment of the gene to mouse chromosome 17A2-3. Biochem. Biophys. Res. Commun., 247, 116-122.
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 116-122
    • Seet, L.F.1    Cho, S.2    Hessel, A.3    Dumont, D.J.4
  • 77
    • 0023058975 scopus 로고
    • A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation
    • Shaw, G. and Kamen, R. (1986) A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation. Cell, 46, 659-667.
    • (1986) Cell , vol.46 , pp. 659-667
    • Shaw, G.1    Kamen, R.2
  • 78
    • 0033593816 scopus 로고    scopus 로고
    • The yeast dynamin-like protein, Mgm1p, functions on the mitochondrial outer membrane to mediate mitochondrial inheritance
    • Shepard, K.A. and Yaffe, M.P. (1999) The yeast dynamin-like protein, Mgm1p, functions on the mitochondrial outer membrane to mediate mitochondrial inheritance. J. Cell Biol., 144, 711-720.
    • (1999) J. Cell Biol. , vol.144 , pp. 711-720
    • Shepard, K.A.1    Yaffe, M.P.2
  • 79
    • 0030817913 scopus 로고    scopus 로고
    • Identification and subcellular localization of a novel mammalian dynamin-related protein homologous to yeast Vps1p and Dnm1p
    • Shin, H.W., Shinotsuka, C., Torii, S., Murakami, K. and Nakayama, K. (1997) Identification and subcellular localization of a novel mammalian dynamin-related protein homologous to yeast Vps1p and Dnm1p. J. Biochem. (Tokyo), 122, 525-530.
    • (1997) J. Biochem. (Tokyo) , vol.122 , pp. 525-530
    • Shin, H.W.1    Shinotsuka, C.2    Torii, S.3    Murakami, K.4    Nakayama, K.5
  • 81
    • 0029078227 scopus 로고
    • Actin-dependent mitochondrial motility in mitotic yeast and cell-free systems: Identification of a motor activity on the mitochondrial surface
    • Simon, V.R., Swayne, T.C. and Pon, L.A. (1995) Actin-dependent mitochondrial motility in mitotic yeast and cell-free systems: identification of a motor activity on the mitochondrial surface. J. Cell Biol., 130, 345-354.
    • (1995) J. Cell Biol. , vol.130 , pp. 345-354
    • Simon, V.R.1    Swayne, T.C.2    Pon, L.A.3
  • 82
    • 0345646448 scopus 로고    scopus 로고
    • Synaptojanin family members are implicated in endocytic membrane traffic in yeast
    • Singer-Krüger, B., Nemoto, Y., Daniell, L., Ferro-Novick, S. and De Camilli, P. (1998) Synaptojanin family members are implicated in endocytic membrane traffic in yeast. J. Cell Sci., 111, 3347-3356.
    • (1998) J. Cell Sci. , vol.111 , pp. 3347-3356
    • Singer-Krüger, B.1    Nemoto, Y.2    Daniell, L.3    Ferro-Novick, S.4    De Camilli, P.5
  • 83
    • 0032493929 scopus 로고    scopus 로고
    • Role of phosphorylation in regulation of the assembly of endocytic coat complexes
    • Slepnev, V.I., Ochoa, G.C., Butler, M.H., Grabs, D. and Camilli, P.D. (1998) Role of phosphorylation in regulation of the assembly of endocytic coat complexes. Science, 281, 821-824.
    • (1998) Science , vol.281 , pp. 821-824
    • Slepnev, V.I.1    Ochoa, G.C.2    Butler, M.H.3    Grabs, D.4    Camilli, P.D.5
  • 84
    • 0032547754 scopus 로고    scopus 로고
    • A human dynamin-related protein controls the distribution of mitochondria
    • Smirnova, E., Shurland, D.L., Ryazantsev, S.N. and van der Bliek, A.M. (1998) A human dynamin-related protein controls the distribution of mitochondria. J. Cell Biol., 143, 351-358.
    • (1998) J. Cell Biol. , vol.143 , pp. 351-358
    • Smirnova, E.1    Shurland, D.L.2    Ryazantsev, S.N.3    Van Der Bliek, A.M.4
  • 85
    • 0028799104 scopus 로고
    • Organelle-cytoskeletal interactions: Actin mutations inhibit meiosis-dependent mitochondrial rearrangement in the budding yeast Saccharomyces cerevisiae
    • Smith, M.G., Simon, V.R., O'Sullivan, H. and Pon, L.A. (1995) Organelle-cytoskeletal interactions: actin mutations inhibit meiosis-dependent mitochondrial rearrangement in the budding yeast Saccharomyces cerevisiae. Mol. Biol. Cell, 6, 1381-1396.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1381-1396
    • Smith, M.G.1    Simon, V.R.2    O'Sullivan, H.3    Pon, L.A.4
  • 87
    • 0028024592 scopus 로고
    • Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane
    • Sogo, L.F. and Yaffe, M.P. (1994) Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane. J. Cell Biol., 126, 1361-1373.
    • (1994) J. Cell Biol. , vol.126 , pp. 1361-1373
    • Sogo, L.F.1    Yaffe, M.P.2
  • 88
    • 15644379801 scopus 로고    scopus 로고
    • Recognition of unique carboxyl-terminal motifs by distinct PDZ domains
    • Songyang, Z. et al. (1997) Recognition of unique carboxyl-terminal motifs by distinct PDZ domains. Science, 275, 73-77.
    • (1997) Science , vol.275 , pp. 73-77
    • Songyang, Z.1
  • 89
    • 0030686464 scopus 로고    scopus 로고
    • Disruption of three phosphatidylinositol-polyphosphate 5-phosphatase genes from Saccharomyces cerevisiae results in pleiotropic abnormalities of vacuole morphology, cell shape and osmohomeostasis
    • Srinivasan, S., Seaman, M., Nemoto, Y., Daniell, L., Suchy, S.F., Emr, S., De Camilli, P. and Nussbaum, R. (1997) Disruption of three phosphatidylinositol-polyphosphate 5-phosphatase genes from Saccharomyces cerevisiae results in pleiotropic abnormalities of vacuole morphology, cell shape and osmohomeostasis. Eur. J. Cell Biol., 74, 350-360.
    • (1997) Eur. J. Cell Biol. , vol.74 , pp. 350-360
    • Srinivasan, S.1    Seaman, M.2    Nemoto, Y.3    Daniell, L.4    Suchy, S.F.5    Emr, S.6    De Camilli, P.7    Nussbaum, R.8
  • 90
    • 0031893414 scopus 로고    scopus 로고
    • Identification and characterization of an essential family of inositol polyphosphate 5-phosphatases (INP51, INP52 and INP53 gene products) in the yeast Saccharomyces cerevisiae
    • Stolz, L.E., Huynh, C.V., Thorner, J. and York, J.D. (1998) Identification and characterization of an essential family of inositol polyphosphate 5-phosphatases (INP51, INP52 and INP53 gene products) in the yeast Saccharomyces cerevisiae. Genetics, 148, 1715-1729.
    • (1998) Genetics , vol.148 , pp. 1715-1729
    • Stolz, L.E.1    Huynh, C.V.2    Thorner, J.3    York, J.D.4
  • 91
    • 0020760101 scopus 로고
    • Effect of microtubules and intermediate filaments on mitochondrial distribution
    • Summerhayes, I.C., Wong, D. and Chen, L.B. (1983) Effect of microtubules and intermediate filaments on mitochondrial distribution. J. Cell Sci., 61, 87-105.
    • (1983) J. Cell Sci. , vol.61 , pp. 87-105
    • Summerhayes, I.C.1    Wong, D.2    Chen, L.B.3
  • 92
    • 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. (1998) Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria. Cell, 93, 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
  • 93
    • 0022137059 scopus 로고
    • Transient accumulation of c-fos RNA following serum stimulation requires a conserved 5′ element and c-fos 3′ sequences
    • Treisman, R. (1985) Transient accumulation of c-fos RNA following serum stimulation requires a conserved 5′ element and c-fos 3′ sequences. Cell, 42, 889-902.
    • (1985) Cell , vol.42 , pp. 889-902
    • Treisman, R.1
  • 94
    • 0029932027 scopus 로고    scopus 로고
    • Targeting of motor proteins
    • Vallee, R.B. and Sheetz, M.P. (1996) Targeting of motor proteins. Science, 271, 1539-1544.
    • (1996) Science , vol.271 , pp. 1539-1544
    • Vallee, R.B.1    Sheetz, M.P.2
  • 95
    • 0027250250 scopus 로고
    • Mammalian Ras interacts directly with the serine/threonine kinase Raf
    • Vojtek, A.B., Hollenberg, S.M. and Cooper, J.A. (1993) Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell, 74, 205-214.
    • (1993) Cell , vol.74 , pp. 205-214
    • Vojtek, A.B.1    Hollenberg, S.M.2    Cooper, J.A.3
  • 96
    • 0025941465 scopus 로고
    • The discs-large tumor suppressor gene of Drosophila encodes a guanylate kinase homolog localized at septate junctions
    • Woods, D.F. and Bryant, P.J. (1991) The discs-large tumor suppressor gene of Drosophila encodes a guanylate kinase homolog localized at septate junctions. Cell, 66, 451-464.
    • (1991) Cell , vol.66 , pp. 451-464
    • Woods, D.F.1    Bryant, P.J.2
  • 98
    • 0028073746 scopus 로고
    • P145, a major Grb2-binding protein in brain, is co-localized with dynamin in nerve terminals where it undergoes activity-dependent dephosphorylation
    • McPherson, P.S., Takei, K., Schmid, S.L. and De Camilli, P. (1994b) p145, a major Grb2-binding protein in brain, is co-localized with dynamin in nerve terminals where it undergoes activity-dependent dephosphorylation. J. Biol. Chem., 269, 30132-30139.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30132-30139
    • McPherson, P.S.1    Takei, K.2    Schmid, S.L.3    De Camilli, P.4
  • 99
    • 2642622186 scopus 로고    scopus 로고
    • A presynaptic inositol-5-phosphatase
    • McPherson, P.S. et al. (1996) A presynaptic inositol-5-phosphatase. Nature, 379, 353-357.
    • (1996) Nature , vol.379 , pp. 353-357
    • McPherson, P.S.1
  • 100
    • 0030856743 scopus 로고    scopus 로고
    • Synaptojanin forms two separate complexes in the nerve terminal
    • Micheva, K.D., Kay, B.K. and McPherson, P.S. (1997) Synaptojanin forms two separate complexes in the nerve terminal. J. Biol. Chem., 272, 27239-27245.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27239-27245
    • Micheva, K.D.1    Kay, B.K.2    McPherson, P.S.3
  • 101
    • 0028821852 scopus 로고
    • Protein import into mammalian mitochondria
    • Mihara, K. and Omura, T. (1995) Protein import into mammalian mitochondria. Methods Enzymol., 260, 302-310.
    • (1995) Methods Enzymol. , vol.260 , pp. 302-310
    • Mihara, K.1    Omura, T.2
  • 102
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller, J.H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 103
    • 0028906288 scopus 로고
    • Molecular characterization and spatial distribution of SAP97, a novel presynaptic protein homologous to SAP90 and the Drosophila discs-large tumor suppressor protein
    • Müller, B.M., Kistner, U., Veh, R.W., Cases-Langhoff, C., Becker, B., Gundelfinger, E.D. and Garner, C.C. (1995) Molecular characterization and spatial distribution of SAP97, a novel presynaptic protein homologous to SAP90 and the Drosophila discs-large tumor suppressor protein. J. Neurosci., 15, 2354-2366.
    • (1995) J. Neurosci. , vol.15 , pp. 2354-2366
    • Müller, B.M.1    Kistner, U.2    Veh, R.W.3    Cases-Langhoff, C.4    Becker, B.5    Gundelfinger, E.D.6    Garner, C.C.7
  • 104
    • 0039793622 scopus 로고    scopus 로고
    • SAP102, a novel postsynaptic protein that interacts with NMDA receptor complexes in vivo
    • Müller, B.M. et al. (1996) SAP102, a novel postsynaptic protein that interacts with NMDA receptor complexes in vivo. Neuron, 17, 255-265.
    • (1996) Neuron , vol.17 , pp. 255-265
    • Müller, B.M.1
  • 105
    • 0028641560 scopus 로고
    • KIF1B, a novel microtubule plus end-directed monomeric motor protein for transport of mitochondria
    • Nangaku, M., Sato-Yoshitake, R., Okada, Y., Noda, Y., Takemura, R., Yamazaki, H. and Hirokawa, N. (1994) KIF1B, a novel microtubule plus end-directed monomeric motor protein for transport of mitochondria. Cell, 79, 1209-1220.
    • (1994) Cell , vol.79 , pp. 1209-1220
    • Nangaku, M.1    Sato-Yoshitake, R.2    Okada, Y.3    Noda, Y.4    Takemura, R.5    Yamazaki, H.6    Hirokawa, N.7
  • 106
    • 0030707815 scopus 로고    scopus 로고
    • Synaptojanin 2, a novel synaptojanin isoform with a distinct targeting domain and expression pattern
    • Nemoto, Y., Arribas, M., Haffner, C. and DeCamilli, P. (1997) Synaptojanin 2, a novel synaptojanin isoform with a distinct targeting domain and expression pattern. J. Biol. Chem., 272, 30817-30821.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30817-30821
    • Nemoto, Y.1    Arribas, M.2    Haffner, C.3    DeCamilli, P.4
  • 107
    • 0022574421 scopus 로고
    • Import and processing of hybrid proteins by mammalian mitochondria in vitro
    • Nguyen, M., Argan, C., Lusty, C.J. and Shore, G.C. (1986) Import and processing of hybrid proteins by mammalian mitochondria in vitro. J. Biol. Chem., 261, 800-805.
    • (1986) . J. Biol. Chem. , vol.261 , pp. 800-805
    • Nguyen, M.1    Argan, C.2    Lusty, C.J.3    Shore, G.C.4
  • 108
    • 0029946167 scopus 로고    scopus 로고
    • Interaction between the C terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases
    • Niethammer, M., Kim, E. and Sheng, M. (1996) Interaction between the C terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases. J. Neurosci., 16, 2157-2163.
    • (1996) J. Neurosci. , vol.16 , pp. 2157-2163
    • Niethammer, M.1    Kim, E.2    Sheng, M.3
  • 109
    • 0024549504 scopus 로고
    • Suppressors of yeast actin mutations
    • Novick, P., Osmond, B.C. and Botstein, D. (1989) Suppressors of yeast actin mutations. Genetics, 121, 659-674.
    • (1989) Genetics , vol.121 , pp. 659-674
    • Novick, P.1    Osmond, B.C.2    Botstein, D.3
  • 111
    • 0030812638 scopus 로고    scopus 로고
    • The HtrA family of serine proteases
    • Pallen, M.J. and Wren, B.W. (1997) The HtrA family of serine proteases. Mol. Microbiol., 26, 209-221.
    • (1997) Mol. Microbiol. , vol.26 , pp. 209-221
    • Pallen, M.J.1    Wren, B.W.2
  • 112
    • 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. (1997) Mitochondrial association of a plus end-directed microtubule motor expressed during mitosis in Drosophila. J. Cell Biol., 136, 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
  • 114
    • 0032919866 scopus 로고    scopus 로고
    • Syndapin 1, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein
    • Qualmann, B., Roos, J., DiGregorio, P.J. and Kelly, R.B. (1999) Syndapin 1, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein. Mol. Biol. Cell, 10, 501-513.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 501-513
    • Qualmann, B.1    Roos, J.2    DiGregorio, P.J.3    Kelly, R.B.4
  • 115
    • 0029773891 scopus 로고    scopus 로고
    • Tissue-specific alternative splicing generates two synaptojanin isoforms with differential membrane binding properties
    • Ramjaun, A.R. and McPherson, P.S. (1996) Tissue-specific alternative splicing generates two synaptojanin isoforms with differential membrane binding properties. J. Biol. Chem., 271, 24856-24861.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24856-24861
    • Ramjaun, A.R.1    McPherson, P.S.2
  • 116
    • 0030908644 scopus 로고    scopus 로고
    • Identification and characterization of a nerve terminal-enriched amphiphysin isoform
    • Ramjaun, A.R., Micheva, K.D., Bouchelet, I. and McPherson, P.S. (1997) Identification and characterization of a nerve terminal-enriched amphiphysin isoform. J. Biol. Chem., 272, 16700-16706.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16700-16706
    • Ramjaun, A.R.1    Micheva, K.D.2    Bouchelet, I.3    McPherson, P.S.4
  • 117
    • 0030739938 scopus 로고    scopus 로고
    • The SH3p4/SH3p8/ SH3p13 protein family: Binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain
    • Ringstad, N., Nemoto, Y. and De Camilli, P. (1997) The SH3p4/SH3p8/ SH3p13 protein family: binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain. Proc. Natl Acad. Sci. USA, 94, 8569-8574.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 8569-8574
    • Ringstad, N.1    Nemoto, Y.2    De Camilli, P.3
  • 119
    • 0027723051 scopus 로고
    • Microtubule-dependent control of cell shape and pseudopodial activity is inhibited by the antibody to kinesin motor domain
    • Rodionov, V.I., Gyoeva, F.K., Tanaka, E., Bershadsky, A.D., Vasiliev, J.M. and Gelfand, V.I. (1993) Microtubule-dependent control of cell shape and pseudopodial activity is inhibited by the antibody to kinesin motor domain. J. Cell Biol., 123, 1811-1820.
    • (1993) J. Cell Biol. , vol.123 , pp. 1811-1820
    • Rodionov, V.I.1    Gyoeva, F.K.2    Tanaka, E.3    Bershadsky, A.D.4    Vasiliev, J.M.5    Gelfand, V.I.6
  • 120
    • 0023920458 scopus 로고
    • Mitochondrial presequences
    • Roise, D. and Schatz, G. (1988) Mitochondrial presequences. J. Biol. Chem., 263, 4509-4511.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4509-4511
    • Roise, D.1    Schatz, G.2
  • 121
    • 0030747392 scopus 로고    scopus 로고
    • The role of lipid signaling in constitutive membrane traffic
    • Roth, M.G. and Sternweis, P.C. (1997) The role of lipid signaling in constitutive membrane traffic. Curr. Opin. Cell Biol., 9, 519-526.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 519-526
    • Roth, M.G.1    Sternweis, P.C.2
  • 123
    • 0032499612 scopus 로고    scopus 로고
    • Molecular cloning of multiple isoforms of synaptojanin 2 and assignment of the gene to mouse chromosome 17A2-3
    • Seet, L.F., Cho, S., Hessel, A. and Dumont, D.J. (1998) Molecular cloning of multiple isoforms of synaptojanin 2 and assignment of the gene to mouse chromosome 17A2-3. Biochem. Biophys. Res. Commun., 247, 116-122.
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 116-122
    • Seet, L.F.1    Cho, S.2    Hessel, A.3    Dumont, D.J.4
  • 124
    • 0023058975 scopus 로고
    • A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation
    • Shaw, G. and Kamen, R. (1986) A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation. Cell, 46, 659-667.
    • (1986) Cell , vol.46 , pp. 659-667
    • Shaw, G.1    Kamen, R.2
  • 125
    • 0033593816 scopus 로고    scopus 로고
    • The yeast dynamin-like protein, Mgm1p, functions on the mitochondrial outer membrane to mediate mitochondrial inheritance
    • Shepard, K.A and Yaffe, M.P. (1999) The yeast dynamin-like protein, Mgm1p, functions on the mitochondrial outer membrane to mediate mitochondrial inheritance. J. Cell Biol., 144, 711-720.
    • (1999) J. Cell Biol. , vol.144 , pp. 711-720
    • Shepard, K.A.1    Yaffe, M.P.2
  • 126
    • 0030817913 scopus 로고    scopus 로고
    • Identification and subcellular localization of a novel mammalian dynamin-related protein homologous to yeast Vps1p and Dnm1p
    • Shin, H.W., Shinotsuka, C., Torii, S., Murakami, K. and Nakayama, K. (1997) Identification and subcellular localization of a novel mammalian dynamin-related protein homologous to yeast Vps1p and Dnm1p. J. Biochem. (Tokyo), 122, 525-530.
    • (1997) J. Biochem. (Tokyo) , vol.122 , pp. 525-530
    • Shin, H.W.1    Shinotsuka, C.2    Torii, S.3    Murakami, K.4    Nakayama, K.5
  • 128
    • 0029078227 scopus 로고
    • Actin-dependent mitochondrial motility in mitotic yeast and cell-free systems: Identification of a motor activity on the mitochondrial surface
    • Simon, V.R., Swayne, T.C. and Pon, L.A. (1995) Actin-dependent mitochondrial motility in mitotic yeast and cell-free systems: identification of a motor activity on the mitochondrial surface. J. Cell Biol., 130, 345-354.
    • (1995) J. Cell Biol. , vol.130 , pp. 345-354
    • Simon, V.R.1    Swayne, T.C.2    Pon, L.A.3
  • 129
    • 0345646448 scopus 로고    scopus 로고
    • Synaptojanin family members are implicated in endocytic membrane traffic in yeast
    • Singer-Krüger, B., Nemoto, Y., Daniell, L., Ferro-Novick, S. and De Camilli, P. (1998) Synaptojanin family members are implicated in endocytic membrane traffic in yeast. J. Cell Sci., 111, 3347-3356.
    • (1998) J. Cell Sci. , vol.111 , pp. 3347-3356
    • Singer-Krüger, B.1    Nemoto, Y.2    Daniell, L.3    Ferro-Novick, S.4    De Camilli, P.5
  • 130
    • 0032493929 scopus 로고    scopus 로고
    • Role of phosphorylation in regulation of the assembly of endocytic coat complexes
    • Slepnev, V.I., Ochoa, G.C., Butler, M.H., Grabs, D. and Camilli, P.D. (1998) Role of phosphorylation in regulation of the assembly of endocytic coat complexes. Science, 281, 821-824.
    • (1998) Science , vol.281 , pp. 821-824
    • Slepnev, V.I.1    Ochoa, G.C.2    Butler, M.H.3    Grabs, D.4    Camilli, P.D.5
  • 131
    • 0032547754 scopus 로고    scopus 로고
    • A human dynamin-related protein controls the distribution of mitochondria
    • Smirnova, E., Shurland, D.L., Ryazantsev, S.N. and van der Bliek, A.M. (1998) A human dynamin-related protein controls the distribution of mitochondria. J. Cell Biol., 143, 351-358.
    • (1998) J. Cell Biol. , vol.143 , pp. 351-358
    • Smirnova, E.1    Shurland, D.L.2    Ryazantsev, S.N.3    Van Der Bliek, A.M.4
  • 132
    • 0028799104 scopus 로고
    • Organelle-cytoskeletal interactions: Actin mutations inhibit meiosis-dependent mitochondrial rearrangement in the budding yeast Saccharomyces cerevisiae
    • Smith, M.G., Simon, V.R., O'Sullivan, H. and Pon, L.A. (1995) Organelle-cytoskeletal interactions: actin mutations inhibit meiosis-dependent mitochondrial rearrangement in the budding yeast Saccharomyces cerevisiae. Mol. Biol. Cell, 6, 1381-1396.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1381-1396
    • Smith, M.G.1    Simon, V.R.2    O'Sullivan, H.3    Pon, L.A.4
  • 134
    • 0028024592 scopus 로고
    • Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane
    • Sogo, L.F. and Yaffe, M.P. (1994) Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane. J. Cell Biol., 126, 1361-1373.
    • (1994) J. Cell Biol. , vol.126 , pp. 1361-1373
    • Sogo, L.F.1    Yaffe, M.P.2
  • 135
    • 15644379801 scopus 로고    scopus 로고
    • Recognition of unique carboxyl-terminal motifs by distinct PDZ domains
    • Songyang, Z. et al. (1997) Recognition of unique carboxyl-terminal motifs by distinct PDZ domains. Science, 275, 73-77.
    • (1997) Science , vol.275 , pp. 73-77
    • Songyang, Z.1
  • 136
    • 0030686464 scopus 로고    scopus 로고
    • Disruption of three phosphatidylinositol-polyphosphate 5-phosphatase genes from Saccharomyces cerevisiae results in pleiotropic abnormalities of vacuole morphology, cell shape and osmohomeostasis
    • Srinivasan, S., Seaman, M., Nemoto, Y., Daniell, L., Suchy, S.F., Emr, S., De Camilli, P. and Nussbaum, R. (1997) Disruption of three phosphatidylinositol-polyphosphate 5-phosphatase genes from Saccharomyces cerevisiae results in pleiotropic abnormalities of vacuole morphology, cell shape and osmohomeostasis. Eur. J. Cell Biol., 74, 350-360.
    • (1997) Eur. J. Cell Biol. , vol.74 , pp. 350-360
    • Srinivasan, S.1    Seaman, M.2    Nemoto, Y.3    Daniell, L.4    Suchy, S.F.5    Emr, S.6    De Camilli, P.7    Nussbaum, R.8
  • 137
    • 0031893414 scopus 로고    scopus 로고
    • Identification and characterization of an essential family of inositol polyphosphate 5-phosphatases (INP51, INP52 and INP53 gene products) in the yeast Saccharomyces cerevisiae
    • Stolz, L.E., Huynh, C.V., Thorner, J. and York, J.D. (1998) Identification and characterization of an essential family of inositol polyphosphate 5-phosphatases (INP51, INP52 and INP53 gene products) in the yeast Saccharomyces cerevisiae. Genetics, 148, 1715-1729.
    • (1998) Genetics , vol.148 , pp. 1715-1729
    • Stolz, L.E.1    Huynh, C.V.2    Thorner, J.3    York, J.D.4
  • 138
    • 0020760101 scopus 로고
    • Effect of microtubules and intermediate filaments on mitochondrial distribution
    • Summerhayes, I.C., Wong, D. and Chen, L.B. (1983) Effect of microtubules and intermediate filaments on mitochondrial distribution. J. Cell Sci., 61, 87-105.
    • (1983) J. Cell Sci. , vol.61 , pp. 87-105
    • Summerhayes, I.C.1    Wong, D.2    Chen, L.B.3
  • 139
    • 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. (1998) Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria. Cell, 93, 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
  • 140
    • 0022137059 scopus 로고
    • Transient accumulation of c-fos RNA following serum stimulation requires a conserved 5′ element and c-fos 3′ sequences
    • Treisman, R. (1985) Transient accumulation of c-fos RNA following serum stimulation requires a conserved 5′ element and c-fos 3′ sequences. Cell. 42, 889-902.
    • (1985) Cell. , vol.42 , pp. 889-902
    • Treisman, R.1
  • 141
    • 0029932027 scopus 로고    scopus 로고
    • Targeting of motor proteins
    • Vallee, R.B. and Sheetz, M.P. (1996) Targeting of motor proteins. Science, 271, 1539-1544.
    • (1996) Science , vol.271 , pp. 1539-1544
    • Vallee, R.B.1    Sheetz, M.P.2
  • 142
    • 0027250250 scopus 로고
    • Mammalian Ras interacts directly with the serine/threonine kinase Raf
    • Vojtek, A.B., Hollenberg, S.M. and Cooper, J.A. (1993) Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell, 74, 205-214.
    • (1993) Cell , vol.74 , pp. 205-214
    • Vojtek, A.B.1    Hollenberg, S.M.2    Cooper, J.A.3
  • 143
    • 0025941465 scopus 로고
    • The discs-large tumor suppressor gene of Drosophila encodes a guanylate kinase homolog localized at septate junctions
    • Woods, D.F. and Bryant, P.J. (1991) The discs-large tumor suppressor gene of Drosophila encodes a guanylate kinase homolog localized at septate junctions. Cell, 66, 451-464.
    • (1991) Cell , vol.66 , pp. 451-464
    • Woods, D.F.1    Bryant, P.J.2
  • 144
  • 145
    • 0033525615 scopus 로고    scopus 로고
    • The machinery of mitochondrial inheritance and behavior
    • Yaffe, M.P. (1999) The machinery of mitochondrial inheritance and behavior. Science, 283, 1493-1497.
    • (1999) Science , vol.283 , pp. 1493-1497
    • Yaffe, M.P.1
  • 148
    • 0032559599 scopus 로고    scopus 로고
    • A novel dynamin-like protein associates with cytoplasmic vesicles and tubules of the endoplasmic reticulum in mammalian cells
    • Yoon, Y., Pitts, K.R., Dahan, S. and McNiven, M.A. (1998) A novel dynamin-like protein associates with cytoplasmic vesicles and tubules of the endoplasmic reticulum in mammalian cells. J. Cell Biol., 140, 779-793.
    • (1998) J. Cell Biol. , vol.140 , pp. 779-793
    • Yoon, Y.1    Pitts, K.R.2    Dahan, S.3    McNiven, M.A.4
  • 149
    • 0023833889 scopus 로고
    • Orientation of the cytoplasmically made subunits of beef heart cytochrome c oxidase determined by protease digestion and antibody binding experiments
    • Zhang, Y.Z., Lindorfer, M.A. and Capaldi, R.A. (1988) Orientation of the cytoplasmically made subunits of beef heart cytochrome c oxidase determined by protease digestion and antibody binding experiments. Biochemistry, 27, 1389-1394.
    • (1988) Biochemistry , vol.27 , pp. 1389-1394
    • Zhang, Y.Z.1    Lindorfer, M.A.2    Capaldi, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.