메뉴 건너뛰기




Volumn 10, Issue 4, 1999, Pages 1105-1118

Detyrosination of tubulin regulates the interaction of intermediate filaments with microtubules in vivo via a kinesin-dependent mechanism

Author keywords

[No Author keywords available]

Indexed keywords

KINESIN; TUBULIN; TYROSINE;

EID: 0032941748     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.10.4.1105     Document Type: Article
Times cited : (175)

References (59)
  • 2
    • 0025313509 scopus 로고
    • Individual microtubules in the axon consist of domains that differ in both composition and stability
    • Baas, P.W., and Black, M.M. (1990). Individual microtubules in the axon consist of domains that differ in both composition and stability. J. Cell Biol. 111, 495-509.
    • (1990) J. Cell Biol. , vol.111 , pp. 495-509
    • Baas, P.W.1    Black, M.M.2
  • 3
    • 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
  • 5
    • 0023053369 scopus 로고
    • Carboxy-terminal regions on the surface of tubulin and microtubules. Epitope locations of YOL1/34, DM1A and DM1B
    • Breitling, F., and Little, M. (1986). Carboxy-terminal regions on the surface of tubulin and microtubules. Epitope locations of YOL1/34, DM1A and DM1B. J. Mol. Biol. 189, 367-370.
    • (1986) J. Mol. Biol. , vol.189 , pp. 367-370
    • Breitling, F.1    Little, M.2
  • 6
    • 0028117919 scopus 로고
    • Purification and characterization of ensconsin, a novel microtubule stabilizing protein
    • Bulinski, J.C., and Bossler, A. (1994). Purification and characterization of ensconsin, a novel microtubule stabilizing protein. J. Cell Sci. 107, 2389-2349.
    • (1994) J. Cell Sci. , vol.107 , pp. 2389-12349
    • Bulinski, J.C.1    Bossler, A.2
  • 7
    • 0026181461 scopus 로고
    • Stabilization and posttranslational modification of microtubules during cellular morphogenesis
    • Bulinski, J.C., and Gundersen, G.G. (1991). Stabilization and posttranslational modification of microtubules during cellular morphogenesis. Bioessays 13, 285-293.
    • (1991) Bioessays , vol.13 , pp. 285-293
    • Bulinski, J.C.1    Gundersen, G.G.2
  • 8
    • 0023705297 scopus 로고
    • Colocalisation of acetylated microtubules, glial filaments, and mitochondria in astrocytes in vitro
    • Cambray-Deakin, M.A., Robson, S.J., and Burgoyne, R.D. (1988). Colocalisation of acetylated microtubules, glial filaments, and mitochondria in astrocytes in vitro. Cell Motil. Cytoskeleton 10, 438-449.
    • (1988) Cell Motil. Cytoskeleton , vol.10 , pp. 438-449
    • Cambray-Deakin, M.A.1    Robson, S.J.2    Burgoyne, R.D.3
  • 9
    • 0025806830 scopus 로고
    • Preparation and functional assay of pure populations of tyrosinated and detyrosinated tubulin
    • Chapin, S., and Bulinski, J.C. (1991). Preparation and functional assay of pure populations of tyrosinated and detyrosinated tubulin. Methods Enzymol. 196, 254-264.
    • (1991) Methods Enzymol. , vol.196 , pp. 254-264
    • Chapin, S.1    Bulinski, J.C.2
  • 10
    • 0028140020 scopus 로고
    • Cellular microtubules heterogenous in their content of microtubule-associated protein 4 (MAP4)
    • Chapin, S.J., and Bulinski, J.C. (1994). Cellular microtubules heterogenous in their content of microtubule-associated protein 4 (MAP4). Cell Motil. Cytoskeleton 27, 133-149.
    • (1994) Cell Motil. Cytoskeleton , vol.27 , pp. 133-149
    • Chapin, S.J.1    Bulinski, J.C.2
  • 11
    • 0032489802 scopus 로고    scopus 로고
    • Rho guanosine triphosphatase mediates the selective stabilization of microtubules induced by lysophosphatidic acid
    • Cook, T.A., Nagasaki, T., and Gundersen, G.G. (1998). Rho guanosine triphosphatase mediates the selective stabilization of microtubules induced by lysophosphatidic acid. J. Cell Biol. 141, 175-185.
    • (1998) J. Cell Biol. , vol.141 , pp. 175-185
    • Cook, T.A.1    Nagasaki, T.2    Gundersen, G.G.3
  • 12
    • 0024041810 scopus 로고
    • The microtubule-dependent formation of a tubulovesicular network with characteristics of the ER from cultured cell extracts
    • Dabora, S.L., and Sheetz, M.P. (1988). The microtubule-dependent formation of a tubulovesicular network with characteristics of the ER from cultured cell extracts. Cell 54, 27-35.
    • (1988) Cell , vol.54 , pp. 27-35
    • Dabora, S.L.1    Sheetz, M.P.2
  • 14
    • 0015385595 scopus 로고
    • Rat brain microtubule protein: Purification and determination of covalently bound phosphate and carbohydrate
    • Eipper, B.A. (1972). Rat brain microtubule protein: purification and determination of covalently bound phosphate and carbohydrate. Proc. Natl. Acad. Sci. USA 69, 2283-2287.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 2283-2287
    • Eipper, B.A.1
  • 16
    • 0025903440 scopus 로고
    • Intermediate filament-associated proteins
    • Foisner, R., and Wiche, G. (1991). Intermediate filament-associated proteins. Curr. Opin. Cell Biol. 3, 75-81.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 75-81
    • Foisner, R.1    Wiche, G.2
  • 17
    • 0023794840 scopus 로고
    • Selective stabilization of microtubules oriented toward the direction of cell migration
    • Gundersen, G.G., and Bulinski, J.C. (1988). Selective stabilization of microtubules oriented toward the direction of cell migration. Proc. Natl. Acad. Sci. USA 85, 5946-5950.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5946-5950
    • Gundersen, G.G.1    Bulinski, J.C.2
  • 18
    • 0021752265 scopus 로고
    • Distinct populations of microtubules: Tyrosinated and nontyrosinated α-tubulin are distributed differently in cells
    • Gundersen, G.G., Kalnoski, M.H., and Bulinski, J.C. (1984). Distinct populations of microtubules: tyrosinated and nontyrosinated α-tubulin are distributed differently in cells. Cell 38, 779-789.
    • (1984) Cell , vol.38 , pp. 779-789
    • Gundersen, G.G.1    Kalnoski, M.H.2    Bulinski, J.C.3
  • 19
    • 0023371190 scopus 로고
    • Postpolymerization detyrosination of α-tubulin: A mechanism for subcellular differentiation of microtubules
    • Gundersen, G.G., Khawaja, S., and Bulinski, J.C. (1987). Postpolymerization detyrosination of α-tubulin: a mechanism for subcellular differentiation of microtubules. J. Cell Biol. 105, 251-264.
    • (1987) J. Cell Biol. , vol.105 , pp. 251-264
    • Gundersen, G.G.1    Khawaja, S.2    Bulinski, J.C.3
  • 20
    • 0024453421 scopus 로고
    • Generation of a stable, posttranslationally modified microtubule array is an early event in myogenic differentiation
    • Gundersen, G.G., Khawaja, S., and Bulinski, J.C. (1989). Generation of a stable, posttranslationally modified microtubule array is an early event in myogenic differentiation. J. Cell Biol. 109, 2275-2288.
    • (1989) J. Cell Biol. , vol.109 , pp. 2275-2288
    • Gundersen, G.G.1    Khawaja, S.2    Bulinski, J.C.3
  • 21
    • 0028274116 scopus 로고
    • Regulation of microtubule stability in fibroblasts by serum and TGF-β
    • Gundersen, G.G., Kim, I., and Chapin, C.J. (1994). Regulation of microtubule stability in fibroblasts by serum and TGF-β. J. Cell Sci. 107, 645-659.
    • (1994) J. Cell Sci. , vol.107 , pp. 645-659
    • Gundersen, G.G.1    Kim, I.2    Chapin, C.J.3
  • 22
    • 0027515613 scopus 로고
    • Protein phosphatase inhibitors induce the selective breakdown of stable microtubules in fibroblasts and epithelial cells
    • Gurland, G., and Gundersen, G.G. (1993). Protein phosphatase inhibitors induce the selective breakdown of stable microtubules in fibroblasts and epithelial cells. Proc. Natl. Acad. Sci. USA 90, 8827-8831.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8827-8831
    • Gurland, G.1    Gundersen, G.G.2
  • 23
    • 0028883469 scopus 로고
    • Stable, detyrosinated microtubules function to localize vimentin intermediate filaments
    • Gurland, G., and Gundersen, G.G. (1995). Stable, detyrosinated microtubules function to localize vimentin intermediate filaments. J. Cell Biol. 131, 1275-1290.
    • (1995) J. Cell Biol. , vol.131 , pp. 1275-1290
    • Gurland, G.1    Gundersen, G.G.2
  • 24
    • 0025743437 scopus 로고
    • Coalignment of vimentin intermediate filaments with microtubules depends on kinesin
    • Gyoeva, F.K., and Gelfand, V.I. (1991). Coalignment of vimentin intermediate filaments with microtubules depends on kinesin. Nature 353, 445-448.
    • (1991) Nature , vol.353 , pp. 445-448
    • Gyoeva, F.K.1    Gelfand, V.I.2
  • 25
    • 0017577442 scopus 로고
    • Release of tyrosine from tubulin. Some common factors that affect this process and the assembly of tubulin
    • Hallak, M.E., Rodriguez, J.A., Barra, H.S., and Caputto, R. (1977). Release of tyrosine from tubulin. Some common factors that affect this process and the assembly of tubulin. FEBS Lett. 73, 147-150.
    • (1977) FEBS Lett. , vol.73 , pp. 147-150
    • Hallak, M.E.1    Rodriguez, J.A.2    Barra, H.S.3    Caputto, R.4
  • 26
    • 0029882116 scopus 로고    scopus 로고
    • Organelle transport along microtubules - The role of KIFs
    • Hirokawa, N. (1996). Organelle transport along microtubules - the role of KIFs. Trends Cell Biol. 6, 135-141.
    • (1996) Trends Cell Biol. , vol.6 , pp. 135-141
    • Hirokawa, N.1
  • 27
    • 0031826844 scopus 로고    scopus 로고
    • Novel features of intermediate filament dynamics revealed by green fluorescent protein fusion proteins
    • Ho, C.-L., Martys, J., Mikhailov, A., Gundersen, G.G., and Liem, R.K.H. (1998). Novel features of intermediate filament dynamics revealed by green fluorescent protein fusion proteins. J. Cell Sci. 111, 1767-1778.
    • (1998) J. Cell Sci. , vol.111 , pp. 1767-1778
    • Ho, C.-L.1    Martys, J.2    Mikhailov, A.3    Gundersen, G.G.4    Liem, R.K.H.5
  • 29
    • 0024581772 scopus 로고
    • Posttranslational modification of distinct microtubule subpopulations during cell polarization and differentiation in the mouse preimplantation embryo
    • Houliston, E., and Maro, B. (1989). Posttranslational modification of distinct microtubule subpopulations during cell polarization and differentiation in the mouse preimplantation embryo. J. Cell Biol. 108, 543-551.
    • (1989) J. Cell Biol. , vol.108 , pp. 543-551
    • Houliston, E.1    Maro, B.2
  • 30
    • 0025837147 scopus 로고
    • Characterization of a panel of neurofilament antibodies recognizing N-terminal epitopes
    • Kaplan, M., Chin, S.S.M., Maciose, P., Srinawasan, J., Hashim, G., and Liem, R.K.H. (1991). Characterization of a panel of neurofilament antibodies recognizing N-terminal epitopes. J. Neurosci. Res. 30, 545-554.
    • (1991) J. Neurosci. Res. , vol.30 , pp. 545-554
    • Kaplan, M.1    Chin, S.S.M.2    Maciose, P.3    Srinawasan, J.4    Hashim, G.5    Liem, R.K.H.6
  • 31
    • 0023877365 scopus 로고
    • Enhanced stability of microtubules enriched in detyrosinated tubulin is not a direct function of detyrosination level
    • Khawaja, S., Gundersen, G.G., and Bulinski, J.C. (1988). Enhanced stability of microtubules enriched in detyrosinated tubulin is not a direct function of detyrosination level. J. Cell Biol. 106, 141-149.
    • (1988) J. Cell Biol. , vol.106 , pp. 141-149
    • Khawaja, S.1    Gundersen, G.G.2    Bulinski, J.C.3
  • 32
    • 0020265993 scopus 로고
    • Rat monoclonal anti-tubulin antibodies derived by using a new nonsecreting rat cell line
    • Kilmartin, J.V., Wright, B., and Milstein, C. (1982). Rat monoclonal anti-tubulin antibodies derived by using a new nonsecreting rat cell line. J. Cell Biol. 93, 576-582.
    • (1982) J. Cell Biol. , vol.93 , pp. 576-582
    • Kilmartin, J.V.1    Wright, B.2    Milstein, C.3
  • 33
    • 0019888294 scopus 로고
    • Preferential action of a brain detyrosinolating carboxypeptidase on polymerized tubulin
    • Kumar, N., and Flavin, M. (1981). Preferential action of a brain detyrosinolating carboxypeptidase on polymerized tubulin. J. Biol. Chem. 256, 7678-7686.
    • (1981) J. Biol. Chem. , vol.256 , pp. 7678-7686
    • Kumar, N.1    Flavin, M.2
  • 34
    • 0020403072 scopus 로고
    • Modulation of some parameters of assembly of microtubules in vitro by tyrosination of tubulin
    • Kumar, N., and Flavin, M. (1982). Modulation of some parameters of assembly of microtubules in vitro by tyrosination of tubulin. Eur. J. Biochem. 128, 215-222.
    • (1982) Eur. J. Biochem. , vol.128 , pp. 215-222
    • Kumar, N.1    Flavin, M.2
  • 35
    • 0021993649 scopus 로고
    • Chlamydomonas α-tubulin is posttranslationally modified by acetylation on the ∈-amino group of a lysine
    • L'Hernault, S., and Rosenbaum, J. (1985). Chlamydomonas α-tubulin is posttranslationally modified by acetylation on the ∈-amino group of a lysine. Biochemistry 24, 473-478.
    • (1985) Biochemistry , vol.24 , pp. 473-478
    • L'Hernault, S.1    Rosenbaum, J.2
  • 36
    • 0032540307 scopus 로고    scopus 로고
    • Kinesin is a candidate for cross-bridging microtubules and intermediate filaments: Selective binding of kinesin to detyrosinated tubulin and vimentin
    • Liao, G., and Gundersen, G.G. (1998). Kinesin is a candidate for cross-bridging microtubules and intermediate filaments: selective binding of kinesin to detyrosinated tubulin and vimentin. J. Biol. Chem. 273, 9797-9803.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9797-9803
    • Liao, G.1    Gundersen, G.G.2
  • 37
    • 0019466253 scopus 로고
    • Interaction of tubulin with drugs and alkylating agents. 2. Effects of colchicine, podophyllotoxin and vinblastine on the alkylation of tubulin
    • Luduena, R.F., and Roach, M.C. (1981). Interaction of tubulin with drugs and alkylating agents. 2. Effects of colchicine, podophyllotoxin and vinblastine on the alkylation of tubulin. Biochemistry 20, 4437-4444.
    • (1981) Biochemistry , vol.20 , pp. 4437-4444
    • Luduena, R.F.1    Roach, M.C.2
  • 38
    • 0032949408 scopus 로고    scopus 로고
    • IFs in motion: Observations of intermediate filaments in cells using GFP-vimentin
    • in press
    • Martys, J.L., Ho, C.L., Liem, R.K.H., and Gundersen, G.G. (1999). IFs in motion: observations of intermediate filaments in cells using GFP-vimentin. Mol. Biol. Cell (in press).
    • (1999) Mol. Biol. Cell
    • Martys, J.L.1    Ho, C.L.2    Liem, R.K.H.3    Gundersen, G.G.4
  • 40
    • 0028785435 scopus 로고
    • The centripetal transport of microtubules in motile cells
    • Mikhailov, A., and Gundersen, G.G. (1995). The centripetal transport of microtubules in motile cells. Cell Motil. Cytoskeleton 32, 173-186.
    • (1995) Cell Motil. Cytoskeleton , vol.32 , pp. 173-186
    • Mikhailov, A.1    Gundersen, G.G.2
  • 41
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison, T.J., and Kirschner, M.W. (1984). Dynamic instability of microtubule growth. Nature 312, 237-242.
    • (1984) Nature , vol.312 , pp. 237-242
    • Mitchison, T.J.1    Kirschner, M.W.2
  • 42
    • 0026793992 scopus 로고
    • Distribution of detyrosinated microtubules in motile NRK fibroblasts is rapidly altered upon cell-cell contact: Implications for contact inhibition of locomotion
    • Nagasaki, T., Chapin, C.J., and Gundersen, G.G. (1992). Distribution of detyrosinated microtubules in motile NRK fibroblasts is rapidly altered upon cell-cell contact: implications for contact inhibition of locomotion. Cell Motil. Cytoskeleton 23, 45-60.
    • (1992) Cell Motil. Cytoskeleton , vol.23 , pp. 45-60
    • Nagasaki, T.1    Chapin, C.J.2    Gundersen, G.G.3
  • 43
    • 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
  • 44
    • 0024583552 scopus 로고
    • Complete separation of tyrosinated, detyrosinated, and nontyrosinated brain tubulin subpopulations using affinity chromatography
    • Paturle, L., Wehland, J., Margolis, R.L., and Job, D. (1989). Complete separation of tyrosinated, detyrosinated, and nontyrosinated brain tubulin subpopulations using affinity chromatography. Biochemistry 21, 2698-2704.
    • (1989) Biochemistry , vol.21 , pp. 2698-2704
    • Paturle, L.1    Wehland, J.2    Margolis, R.L.3    Job, D.4
  • 45
    • 0032487522 scopus 로고    scopus 로고
    • Rapid movement of vimentin on microtubule tracks: Kinesin-dependent assembly of intermediate filament networks
    • Prahlad, V., Uyoon, N., Moir, R.D., Vale, R.D., and Goldman, R.D. (1998). Rapid movement of vimentin on microtubule tracks: kinesin-dependent assembly of intermediate filament networks. J. Cell Biol. 143, 159-170.
    • (1998) J. Cell Biol. , vol.143 , pp. 159-170
    • Prahlad, V.1    Uyoon, N.2    Moir, R.D.3    Vale, R.D.4    Goldman, R.D.5
  • 46
    • 0017406215 scopus 로고
    • Enzyme which adds tyrosine to the α-chain of tubulin
    • Raybin, D., and Flavin, M. (1977). Enzyme which adds tyrosine to the α-chain of tubulin. Biochemistry 16, 2189-2194.
    • (1977) Biochemistry , vol.16 , pp. 2189-2194
    • Raybin, D.1    Flavin, M.2
  • 48
    • 0021953936 scopus 로고
    • Purification of brain tubulin-tyrosine ligase by biochemical and immunological methods
    • Schroder, H.C., Wehland, J., and Weber, K. (1985). Purification of brain tubulin-tyrosine ligase by biochemical and immunological methods. J. Cell Biol. 106, 276-281.
    • (1985) J. Cell Biol. , vol.106 , pp. 276-281
    • Schroder, H.C.1    Wehland, J.2    Weber, K.3
  • 49
    • 0023608861 scopus 로고
    • Posttranslational modifications and microtubule stability
    • Schulze, E., Asai, D.J., Bulinski, J.C., and Kirschner, M. (1987). Posttranslational modifications and microtubule stability. J. Cell Biol. 105, 2167-2177.
    • (1987) J. Cell Biol. , vol.105 , pp. 2167-2177
    • Schulze, E.1    Asai, D.J.2    Bulinski, J.C.3    Kirschner, M.4
  • 50
    • 0021215332 scopus 로고
    • Limited proteolysis of tubulin and the localization of the binding site for colchicine
    • Serrano, L., Avila, J., and Maccioni, R.B. (1984). Limited proteolysis of tubulin and the localization of the binding site for colchicine. J. Biol. Chem. 259, 6607-6611.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6607-6611
    • Serrano, L.1    Avila, J.2    Maccioni, R.B.3
  • 51
    • 0027405349 scopus 로고
    • Recombinant kinesin motor domain binds to β-tubulin and decorates microtubules with a B surface lattice
    • Song, Y.H., and Mandelkow, E. (1993). Recombinant kinesin motor domain binds to β-tubulin and decorates microtubules with a B surface lattice. Proc. Natl. Acad. Sci. USA 90, 1671-1675.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1671-1675
    • Song, Y.H.1    Mandelkow, E.2
  • 52
    • 0029805514 scopus 로고    scopus 로고
    • Plectin sidearms mediate the interaction of intermediate filaments with microtubules and other components of the cytoskeleton
    • Svitkina, T.M., Verkovsky, A.B., and Borisy, G.G. (1996). Plectin sidearms mediate the interaction of intermediate filaments with microtubules and other components of the cytoskeleton. J. Cell Biol. 135, 991-1007.
    • (1996) J. Cell Biol. , vol.135 , pp. 991-1007
    • Svitkina, T.M.1    Verkovsky, A.B.2    Borisy, G.G.3
  • 53
    • 0023025842 scopus 로고
    • Microtubules and the endoplasmic reticulum are highly interdependent structures
    • Terasaki, M., Chen, L.B., and Fujiwara, K. (1986). Microtubules and the endoplasmic reticulum are highly interdependent structures. J. Cell Biol. 103, 1557-1568.
    • (1986) J. Cell Biol. , vol.103 , pp. 1557-1568
    • Terasaki, M.1    Chen, L.B.2    Fujiwara, K.3
  • 54
    • 0031004776 scopus 로고    scopus 로고
    • Probing the kinesin-microtubule interaction
    • Tucker, C., and Goldstein, L.S.B. (1997). Probing the kinesin-microtubule interaction. J. Biol. Chem. 272, 9481-9488.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9481-9488
    • Tucker, C.1    Goldstein, L.S.B.2
  • 55
    • 0024211157 scopus 로고
    • Formation of membrane networks in vitro by kinesin-driven microtubule movement
    • Vale, R.D., and Hotani, H. (1988). Formation of membrane networks in vitro by kinesin-driven microtubule movement. J. Cell Biol. 107, 2233-2241.
    • (1988) J. Cell Biol. , vol.107 , pp. 2233-2241
    • Vale, R.D.1    Hotani, H.2
  • 58
    • 0025294639 scopus 로고
    • Detyrosination of α-tubulin does not stabilize MTs in vivo
    • Webster, D.R., Wheland, J., Weber, K., and Borisy, G.G. (1990). Detyrosination of α-tubulin does not stabilize MTs in vivo. J. Cell Biol. 112, 113-122.
    • (1990) J. Cell Biol. , vol.112 , pp. 113-122
    • Webster, D.R.1    Wheland, J.2    Weber, K.3    Borisy, G.G.4
  • 59
    • 0029155982 scopus 로고
    • KIF3A/B: A heterodimeric kinesin superfamily protein that works as a microtubule plus end-directed motor for membrane organelle transport
    • Yamazaki, H., Nakata, T., Okada, Y., and Hirokawa, N. (1995). KIF3A/B: a heterodimeric kinesin superfamily protein that works as a microtubule plus end-directed motor for membrane organelle transport. J. Cell Biol. 130, 1387-1399.
    • (1995) J. Cell Biol. , vol.130 , pp. 1387-1399
    • Yamazaki, H.1    Nakata, T.2    Okada, Y.3    Hirokawa, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.