메뉴 건너뛰기




Volumn 9, Issue 9, 1998, Pages 2595-2609

Differential distribution of dynamin isoforms in mammalian cells

Author keywords

[No Author keywords available]

Indexed keywords

CLATHRIN; COMPLEMENTARY DNA; DYNAMIN; GENE PRODUCT; GREEN FLUORESCENT PROTEIN; GUANOSINE TRIPHOSPHATASE; MESSENGER RNA;

EID: 0031720535     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.9.9.2595     Document Type: Article
Times cited : (348)

References (52)
  • 1
    • 0027081711 scopus 로고
    • Developmental stage- And tissue-specific expression of shibire, a Drosophila gene involved in endocytosis
    • Chen, M.S., Burgess, C.C., Vallee, R.B., and Wadsworth, S.C. (1992). Developmental stage-and tissue-specific expression of shibire, a Drosophila gene involved in endocytosis. J. Cell Sci. 103, 619-628.
    • (1992) J. Cell Sci. , vol.103 , pp. 619-628
    • Chen, M.S.1    Burgess, C.C.2    Vallee, R.B.3    Wadsworth, S.C.4
  • 3
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P., and Sacchi, N. (1987). Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem, 162, 156-159.
    • (1987) Anal. Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 4
    • 0031469525 scopus 로고    scopus 로고
    • Inhibition of axonal growth from sensory neurons by excess nerve growth factor
    • Conti, A.M., Fischer, S.J., and Windebank, A.J. (1997). Inhibition of axonal growth from sensory neurons by excess nerve growth factor. Ann. Neurol. 42, 838-846.
    • (1997) Ann. Neurol. , vol.42 , pp. 838-846
    • Conti, A.M.1    Fischer, S.J.2    Windebank, A.J.3
  • 5
    • 0029799506 scopus 로고    scopus 로고
    • Three dynamin-encoding genes are differently expressed in developing rat brain
    • Cook, T., Mesa, K., and Urrutia, R. (1996). Three dynamin-encoding genes are differently expressed in developing rat brain. J. Neurochem. 67, 927-931.
    • (1996) J. Neurochem. , vol.67 , pp. 927-931
    • Cook, T.1    Mesa, K.2    Urrutia, R.3
  • 6
    • 0028137796 scopus 로고
    • Identification of dynamin 2, an isoform ubiquitously expressed in rat tissues
    • Cook, T.A., Urrutia, R., and McNiven, M.A. (1994). Identification of dynamin 2, an isoform ubiquitously expressed in rat tissues. Proc. Natl. Acad. Sci. USA 91, 644-648.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 644-648
    • Cook, T.A.1    Urrutia, R.2    McNiven, M.A.3
  • 7
    • 2842574825 scopus 로고
    • TGN38 forms a macromolecular complex with small GTP-binding proteins: Functional studies using a cell-free assay
    • Abstract
    • Crosby, J.R., Jones, S.M., and Howell, K.E. (1992). TGN38 forms a macromolecular complex with small GTP-binding proteins: functional studies using a cell-free assay. Mol. Biol. Cell 3, A308 (Abstract).
    • (1992) Mol. Biol. Cell , vol.3
    • Crosby, J.R.1    Jones, S.M.2    Howell, K.E.3
  • 8
    • 0029134736 scopus 로고
    • Clathrin-independent pinocytosis is induced in cells overexpressing a temperature-sensitive mutant of dynamin
    • Damke, H., Baba, T., van der Bliek, A.M., and Schmid, S.L. (1995). Clathrin-independent pinocytosis is induced in cells overexpressing a temperature-sensitive mutant of dynamin. J. Cell Biol. 131, 69-80.
    • (1995) J. Cell Biol. , vol.131 , pp. 69-80
    • Damke, H.1    Baba, T.2    Van Der Bliek, A.M.3    Schmid, S.L.4
  • 9
    • 0028036513 scopus 로고
    • Induction of mutant dynamin specifically blocks endocytic coated vesicle formation
    • Damke, H., Baba, T., Warnock, D.E., and Schmid, S.L. (1994). Induction of mutant dynamin specifically blocks endocytic coated vesicle formation. J. Cell Biol. 127, 915-934.
    • (1994) J. Cell Biol. , vol.127 , pp. 915-934
    • Damke, H.1    Baba, T.2    Warnock, D.E.3    Schmid, S.L.4
  • 12
    • 0015934086 scopus 로고
    • Temperature-sensitive mutations in Drosophila melanogaster XV: A selection of immobile adults
    • Grigliatti, T.A., Hall, L., Rosenbluth, R., and Suzuki, D.T. (1973). Temperature-sensitive mutations in Drosophila melanogaster XV: a selection of immobile adults. Mol. Gen. Genet. 120, 107-114.
    • (1973) Mol. Gen. Genet. , vol.120 , pp. 107-114
    • Grigliatti, T.A.1    Hall, L.2    Rosenbluth, R.3    Suzuki, D.T.4
  • 14
    • 0029942238 scopus 로고    scopus 로고
    • Association of a dynamin-like protein with the Golgi apparatus in mammalian cells
    • Henley, J.R., and McNiven, M.A. (1996). Association of a dynamin-like protein with the Golgi apparatus in mammalian cells. J. Cell Biol. 133, 761-775.
    • (1996) J. Cell Biol. , vol.133 , pp. 761-775
    • Henley, J.R.1    McNiven, M.A.2
  • 16
    • 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
  • 17
    • 0032559342 scopus 로고    scopus 로고
    • Role of dynamin in the formation of transport vesicles from the trans-Golgi network
    • Jones, S.M., Howell, K.E., Henley, J.R., Cao, H., and McNiven, M.A. (1998). Role of dynamin in the formation of transport vesicles from the trans-Golgi network. Science 279, 573-577.
    • (1998) Science , vol.279 , pp. 573-577
    • Jones, S.M.1    Howell, K.E.2    Henley, J.R.3    Cao, H.4    McNiven, M.A.5
  • 18
    • 4243054380 scopus 로고
    • Membranous intermediates in endocytosis are labile, as shown in a temperature-sensitive mutant
    • Kessell, I., Holst, B.D., and Roth, T.F. (1989). Membranous intermediates in endocytosis are labile, as shown in a temperature-sensitive mutant. Proc. Natl. Acad. Sci. USA 86, 4968-4972.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4968-4972
    • Kessell, I.1    Holst, B.D.2    Roth, T.F.3
  • 19
    • 0020603664 scopus 로고
    • Possible temperature-dependent blockage of synaptic vesicle recycling induced by a single gene mutation in Drosophila
    • Kosaka, T., and Ikeda, K. (1983a). Possible temperature-dependent blockage of synaptic vesicle recycling induced by a single gene mutation in Drosophila. J. Neurobiol. 14, 207-225.
    • (1983) J. Neurobiol. , vol.14 , pp. 207-225
    • Kosaka, T.1    Ikeda, K.2
  • 22
    • 0032498544 scopus 로고    scopus 로고
    • Expression of mutant dynamin inhibits toxicity and transport of endocytosed ricin to the Golgi apparatus
    • Llorente, A., Rapak, A., Schmid, S.L., van Deurs, B., and Sandvig, K. (1998). Expression of mutant dynamin inhibits toxicity and transport of endocytosed ricin to the Golgi apparatus. J. Cell Biol, 140, 553-563.
    • (1998) J. Cell Biol , vol.140 , pp. 553-563
    • Llorente, A.1    Rapak, A.2    Schmid, S.L.3    Van Deurs, B.4    Sandvig, K.5
  • 23
    • 0027059192 scopus 로고
    • Insertion of dynamin with microtubules: Its structure and GTPase activity investigated by using highly purified dynamin
    • Maeda, K., Nakata, T., Noda, Y., Sato-Yoshitake, R., and Hirokawa, N. (1992). Insertion of dynamin with microtubules: its structure and GTPase activity investigated by using highly purified dynamin. Mol. Biol. Cell 3, 1181-1194.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1181-1194
    • Maeda, K.1    Nakata, T.2    Noda, Y.3    Sato-Yoshitake, R.4    Hirokawa, N.5
  • 26
    • 0032559349 scopus 로고    scopus 로고
    • Unconventional myosins in cell movement, membrane traffic, and signal transduction
    • Mermall, V., Post, P.L., and Mooseker, M.S. (1998). Unconventional myosins in cell movement, membrane traffic, and signal transduction. Science 279, 527-533.
    • (1998) Science , vol.279 , pp. 527-533
    • Mermall, V.1    Post, P.L.2    Mooseker, M.S.3
  • 27
    • 0028177082 scopus 로고
    • Targeting of G alpha i2 to the Golgi by alternative spliced carboxyl-terminal region
    • Montmayeur, J.P., and Borrelli, E. (1994). Targeting of G alpha i2 to the Golgi by alternative spliced carboxyl-terminal region. Science 263, 95-98.
    • (1994) Science , vol.263 , pp. 95-98
    • Montmayeur, J.P.1    Borrelli, E.2
  • 28
    • 0026094996 scopus 로고
    • Predominant and developmentally regulated expression of dynamin in neurons
    • Nakata, T., Iwamoto, A., Noda, Y., Takemura, R., Yoshikura, H., and Hirokawa, N. (1991). Predominant and developmentally regulated expression of dynamin in neurons. Neuron 7, 461-469.
    • (1991) Neuron , vol.7 , pp. 461-469
    • Nakata, T.1    Iwamoto, A.2    Noda, Y.3    Takemura, R.4    Yoshikura, H.5    Hirokawa, N.6
  • 29
    • 0027155543 scopus 로고
    • A novel member of the dynamin family of GTP-binding proteins is expressed specifically in the testis
    • Nakata, T., Takemura, R., and Hirokawa, N. (1993). A novel member of the dynamin family of GTP-binding proteins is expressed specifically in the testis. J. Cell Sci. 105, 1-5.
    • (1993) J. Cell Sci. , vol.105 , pp. 1-5
    • Nakata, T.1    Takemura, R.2    Hirokawa, N.3
  • 30
    • 0032489880 scopus 로고    scopus 로고
    • Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium
    • Oh, P., McIntosh, O.P., and Schnitzer, J.E. (1998). Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium. J. Cell Biol. 141, 101-114.
    • (1998) J. Cell Biol. , vol.141 , pp. 101-114
    • Oh, P.1    McIntosh, O.P.2    Schnitzer, J.E.3
  • 32
    • 9044241677 scopus 로고    scopus 로고
    • Primate homologues of rat TGN38: Primary structure, expression and functional implications
    • Ponnambalam, S., Girotti, M., Yaspo, M.L., Owen, C.W., Perry, A.C.F., and Suganuma, T. (1996). Primate homologues of rat TGN38: primary structure, expression and functional implications. J. Cell Sci. 109, 675-685.
    • (1996) J. Cell Sci. , vol.109 , pp. 675-685
    • Ponnambalam, S.1    Girotti, M.2    Yaspo, M.L.3    Owen, C.W.4    Perry, A.C.F.5    Suganuma, T.6
  • 36
    • 0028363432 scopus 로고
    • Growth factor-induced binding of dynamin to signal transduction proteins involves sorting to distinct and separate proline-rich dynamin sequences
    • Scaife, R., Gout, I., Waterfield, M.D., and Margolis, R.L. (1994). Growth factor-induced binding of dynamin to signal transduction proteins involves sorting to distinct and separate proline-rich dynamin sequences. EMBO J. 13, 2574-2582.
    • (1994) EMBO J. , vol.13 , pp. 2574-2582
    • Scaife, R.1    Gout, I.2    Waterfield, M.D.3    Margolis, R.L.4
  • 37
    • 0025605785 scopus 로고
    • Biochemical and immunochemical analysis of rat brain dynamin interaction with microtubules and organelles in vivo and in vitro
    • Scaife, R., and Margolis, R.L. (1990). Biochemical and immunochemical analysis of rat brain dynamin interaction with microtubules and organelles in vivo and in vitro. J. Cell Biol. 111, 3023-3033.
    • (1990) J. Cell Biol. , vol.111 , pp. 3023-3033
    • Scaife, R.1    Margolis, R.L.2
  • 38
    • 0029809310 scopus 로고    scopus 로고
    • Role of GTP hydrolysis in fission of caveolae directly from plasma membranes
    • Schnitzer, J.E., Oh, P., and McIntosh, D.P. (1996). Role of GTP hydrolysis in fission of caveolae directly from plasma membranes. Science 274, 239-242.
    • (1996) Science , vol.274 , pp. 239-242
    • Schnitzer, J.E.1    Oh, P.2    McIntosh, D.P.3
  • 39
    • 0030042938 scopus 로고    scopus 로고
    • A binding site for SH3 domains targets dynamin to coated pits
    • Shpetner, H.S., Herskovits, J.S., and Vallee, R.B. (1996). A binding site for SH3 domains targets dynamin to coated pits. J. Biol. Chem. 271, 13-16.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13-16
    • Shpetner, H.S.1    Herskovits, J.S.2    Vallee, R.B.3
  • 40
    • 0024342278 scopus 로고
    • Identification of dynamin, a novel mechanochemical enzyme that mediates interactions between microtubules
    • Shpetner, H.S., and Vallee, R.B. (1989). Identification of dynamin, a novel mechanochemical enzyme that mediates interactions between microtubules. Cell 59, 421-432.
    • (1989) Cell , vol.59 , pp. 421-432
    • Shpetner, H.S.1    Vallee, R.B.2
  • 41
    • 0026530775 scopus 로고
    • Dynamin is a GTPase stimulated to high levels of activity by microtubules
    • Shpetner, H.S., and Vallee, R.B. (1992). Dynamin is a GTPase stimulated to high levels of activity by microtubules. Nature 355, 733-735.
    • (1992) Nature , vol.355 , pp. 733-735
    • Shpetner, H.S.1    Vallee, R.B.2
  • 43
    • 0028923349 scopus 로고
    • Tubular membrane invaginations coated by dynamin rings are induced by GTP
    • Takei, K., McPherson, P.S., Schmid, S.L., and De Camilli, P. (1995). Tubular membrane invaginations coated by dynamin rings are induced by GTP. Nature 374, 186-190.
    • (1995) Nature , vol.374 , pp. 186-190
    • Takei, K.1    McPherson, P.S.2    Schmid, S.L.3    De Camilli, P.4
  • 44
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T., and Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 45
    • 0027217188 scopus 로고
    • Activation of dynamin GTPase by acidic phospholipids and endogenous rat brain vesicles
    • Tuma, P.L., Stachniak, M.C., and Collins, C.A. (1993). Activation of dynamin GTPase by acidic phospholipids and endogenous rat brain vesicles. J. Biol. Chem. 268, 17240-17246.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17240-17246
    • Tuma, P.L.1    Stachniak, M.C.2    Collins, C.A.3
  • 46
    • 0031026631 scopus 로고    scopus 로고
    • The dynamins: Redundant or distinct functions for an expanding family of related GTPases?
    • Urrutia, R., Henley, J.R., Cook, T., and McNiven, M.A. (1997). The dynamins: redundant or distinct functions for an expanding family of related GTPases? Proc. Natl. Acad. Sci. USA 94, 377-384.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 377-384
    • Urrutia, R.1    Henley, J.R.2    Cook, T.3    McNiven, M.A.4
  • 47
    • 0029550849 scopus 로고
    • Targeting of cytoplasmic dynein to membranous organelles and kinetochores via dynactin
    • Vallee, R.B., Vaughan, K.T., and Echeverri, C.J. (1995). Targeting of cytoplasmic dynein to membranous organelles and kinetochores via dynactin. Cold Spring Harbor Symp. Quant. Biol. 60, 803-811.
    • (1995) Cold Spring Harbor Symp. Quant. Biol. , vol.60 , pp. 803-811
    • Vallee, R.B.1    Vaughan, K.T.2    Echeverri, C.J.3
  • 48
    • 0025810110 scopus 로고
    • Dynamin-like protein encoded by the Drosophila shibire gene associated with vesicular traffic
    • van der Bliek, A.M., and Meyerowitz, E.M. (1991). Dynamin-like protein encoded by the Drosophila shibire gene associated with vesicular traffic. Nature 351, 411-414.
    • (1991) Nature , vol.351 , pp. 411-414
    • Van Der Bliek, A.M.1    Meyerowitz, E.M.2
  • 50
    • 0030298146 scopus 로고    scopus 로고
    • Dynamin GTPase, a force-generating molecular switch
    • Warnock, D.E., and Schmid, S.L. (1996). Dynamin GTPase, a force-generating molecular switch. Bioessays 18, 885-893.
    • (1996) Bioessays , vol.18 , pp. 885-893
    • Warnock, D.E.1    Schmid, S.L.2
  • 51
    • 0019312570 scopus 로고
    • The use of networks of dissociated rat dorsal root ganglin neurons to induce myelination by oligodendrocytes in culture
    • Wood, P., Okada, E., and Bunge, R. (1980). The use of networks of dissociated rat dorsal root ganglin neurons to induce myelination by oligodendrocytes in culture. Brain Res. 196, 247-252.
    • (1980) Brain Res. , vol.196 , pp. 247-252
    • Wood, P.1    Okada, E.2    Bunge, R.3
  • 52
    • 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, 1-14.
    • (1998) J. Cell Biol. , vol.140 , pp. 1-14
    • Yoon, Y.1    Pitts, K.R.2    Dahan, S.3    McNiven, M.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.