메뉴 건너뛰기




Volumn 14, Issue 9, 2003, Pages 3636-3649

Expression of phosphatidylinositol (4,5) bisphosphate-specific pleckstrin homology domains alters direction but not the level of axonal transport of mitochondria

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHOLIPASE C; PLECKSTRIN; SPECTRIN;

EID: 0141521642     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E02-10-0638     Document Type: Article
Times cited : (68)

References (60)
  • 2
    • 0028816908 scopus 로고
    • Early immunohistochemical changes of microtubule based motor proteins in gerbil hippocampus after transient ischemia
    • Aoki, M., Abe, K., Yoshida, T., Hattori, A., Kogure, K., and Itoyama, Y. (1995). Early immunohistochemical changes of microtubule based motor proteins in gerbil hippocampus after transient ischemia. Brain Res. 669, 189-196.
    • (1995) Brain Res. , vol.669 , pp. 189-196
    • Aoki, M.1    Abe, K.2    Yoshida, T.3    Hattori, A.4    Kogure, K.5    Itoyama, Y.6
  • 4
    • 0026793749 scopus 로고
    • Evidence for a new inositol phospholipid in rat brain mitochondria
    • Bothmer, J., Markerink, M., and Jolles, J. (1992). Evidence for a new inositol phospholipid in rat brain mitochondria. Biochem. Biophys. Res. Commun. 187, 1077-1082.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 1077-1082
    • Bothmer, J.1    Markerink, M.2    Jolles, J.3
  • 5
    • 0035802108 scopus 로고    scopus 로고
    • Phosphatidylinositol 4, 5-bisphosphate and Arf6-regulated membrane traffic
    • Brown, F.D., Rozelle, A.L., Yin, H.L., Balla, T., and Donaldson, J.G. (2001). Phosphatidylinositol 4, 5-bisphosphate and Arf6-regulated membrane traffic. J. Cell Biol. 154, 1007-1017.
    • (2001) J. Cell Biol. , vol.154 , pp. 1007-1017
    • Brown, F.D.1    Rozelle, A.L.2    Yin, H.L.3    Balla, T.4    Donaldson, J.G.5
  • 6
    • 0029004898 scopus 로고
    • Defective axonal transport in a transgenic mouse model of amyotrophic lateral sclerosis
    • Collard, J.F., Cote, F., and Julien, J.P. (1995). Defective axonal transport in a transgenic mouse model of amyotrophic lateral sclerosis. Nature 375, 61-64.
    • (1995) Nature , vol.375 , pp. 61-64
    • Collard, J.F.1    Cote, F.2    Julien, J.P.3
  • 7
    • 0027226155 scopus 로고
    • Concomitant changes in mitochondria and intermediate filaments during heat shock and recovery of chicken embryo fibroblasts
    • Collier, N.C., Sheetz, M.P., and Schlesinger, M.J. (1993). Concomitant changes in mitochondria and intermediate filaments during heat shock and recovery of chicken embryo fibroblasts. J. Cell Biochem. 52, 297-307.
    • (1993) J. Cell Biochem. , vol.52 , pp. 297-307
    • Collier, N.C.1    Sheetz, M.P.2    Schlesinger, M.J.3
  • 8
    • 0028106091 scopus 로고
    • Identification of coelomocyte unconventional myosin and its association with in vivo particle/vesicle motility
    • D'Andrea, L., Danon, M.A., Sgourdas, G.P., and Bonder, E.M. (1994). Identification of coelomocyte unconventional myosin and its association with in vivo particle/vesicle motility. J. Cell Sci. 107, 2081-2094.
    • (1994) J. Cell Sci. , vol.107 , pp. 2081-2094
    • D'Andrea, L.1    Danon, M.A.2    Sgourdas, G.P.3    Bonder, E.M.4
  • 9
    • 0028169731 scopus 로고
    • Identification of two regions of beta G spectrin that bind to distinct sites in brain membranes
    • Davis, L.H., and Bennett, V. (1994). Identification of two regions of beta G spectrin that bind to distinct sites in brain membranes. J. Biol. Chem. 269, 4409-4416.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4409-4416
    • Davis, L.H.1    Bennett, V.2
  • 10
    • 0034641135 scopus 로고    scopus 로고
    • Tumor necrosis factor induces hyperphosphorylation of kinesin light chain and inhibits kinesin-mediated transport of mitochondria
    • De Vos, K., Severin, F., Van Herreweghe, F., Vancompernolle, K., Goossens, V., Hyman, A., and Grooten, J. (2000). Tumor necrosis factor induces hyperphosphorylation of kinesin light chain and inhibits kinesin-mediated transport of mitochondria. J. Cell Biol. 149, 1207-1214.
    • (2000) J. Cell Biol. , vol.149 , pp. 1207-1214
    • De Vos, K.1    Severin, F.2    Van Herreweghe, F.3    Vancompernolle, K.4    Goossens, V.5    Hyman, A.6    Grooten, J.7
  • 11
    • 0032476645 scopus 로고    scopus 로고
    • Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: Implications for Alzheimer's disease
    • Ebneth, A., Godemann, R., Stamer, K., Illenberger, S., Trinczek, B., and Mandelkow, E. (1998). Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: implications for Alzheimer's disease. J. Cell Biol. 143, 777-794.
    • (1998) J. Cell Biol. , vol.143 , pp. 777-794
    • Ebneth, A.1    Godemann, R.2    Stamer, K.3    Illenberger, S.4    Trinczek, B.5    Mandelkow, E.6
  • 12
    • 0028787055 scopus 로고
    • The pleckstrin homology domain of phospholipase C-delta 1 binds with high affinity to phosphatidylinositol 4, 5-bisphosphate in bilayer membranes
    • Garcia, P., Gupta, R., Shah, S., Morris, A.J., Rudge, S.A., Scarlata, S., Petrova, V., McLaughlin, S., and Rebecchi, M.J. (1995). The pleckstrin homology domain of phospholipase C-delta 1 binds with high affinity to phosphatidylinositol 4, 5-bisphosphate in bilayer membranes. Biochemistry 34, 16228-16234.
    • (1995) Biochemistry , vol.34 , pp. 16228-16234
    • Garcia, P.1    Gupta, R.2    Shah, S.3    Morris, A.J.4    Rudge, S.A.5    Scarlata, S.6    Petrova, V.7    McLaughlin, S.8    Rebecchi, M.J.9
  • 15
    • 0037128208 scopus 로고    scopus 로고
    • Coordination of opposite-polarity microtubule motors
    • Gross, S.P., Welte, M.A., Block, S.M., and Wieschaus, E.F. (2002b). Coordination of opposite-polarity microtubule motors. J. Cell Biol. 156, 715-724.
    • (2002) J. Cell Biol. , vol.156 , pp. 715-724
    • Gross, S.P.1    Welte, M.A.2    Block, S.M.3    Wieschaus, E.F.4
  • 16
    • 0035829720 scopus 로고    scopus 로고
    • Disruption of axonal transport and neuronal viability by amyloid precursor protein mutations in Drosophila
    • Gunawardena, S., and Goldstein, L.S. (2001). Disruption of axonal transport and neuronal viability by amyloid precursor protein mutations in Drosophila. Neuron 32, 389-401.
    • (2001) Neuron , vol.32 , pp. 389-401
    • Gunawardena, S.1    Goldstein, L.S.2
  • 17
    • 0027491245 scopus 로고
    • Regulation of vesicle transport in CV-1 cells and extracts
    • Hamm-Alvarez, S.F., Kim, P.Y., and Sheetz, M.P. (1993). Regulation of vesicle transport in CV-1 cells and extracts. J. Cell Sci. 106(Pt 3), 955-966.
    • (1993) J. Cell Sci. , vol.106 , Issue.PART 3 , pp. 955-966
    • Hamm-Alvarez, S.F.1    Kim, P.Y.2    Sheetz, M.P.3
  • 18
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol-4, 5-bisphosphate
    • Harlan, J.E., Hajduk, P.J., Yoon, H.S., and Fesik, S.W. (1994). Pleckstrin homology domains bind to phosphatidylinositol-4, 5-bisphosphate. Nature 371, 168-170.
    • (1994) Nature , vol.371 , pp. 168-170
    • Harlan, J.E.1    Hajduk, P.J.2    Yoon, H.S.3    Fesik, S.W.4
  • 19
    • 0025719245 scopus 로고
    • Synthesis of phosphatidylinositol 4, 5-bisphosphate in the endoplasmic reticulum of Chinese hamster ovary cells
    • Helms, J.B., de Vries, K.J., and Wirtz, K.W. (1991). Synthesis of phosphatidylinositol 4, 5-bisphosphate in the endoplasmic reticulum of Chinese hamster ovary cells. J. Biol. Chem. 266, 21368-21374.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21368-21374
    • Helms, J.B.1    De Vries, K.J.2    Wirtz, K.W.3
  • 20
    • 0034625410 scopus 로고    scopus 로고
    • A pleckstrin homology domain specific for phosphatidylinositol 4, 5-bisphosphate (Ptdlns-4, 5-P2) and fused to green fluorescent protein identifies plasma membrane PtdIns-4, 5-P2 as being important in exocytosis
    • Holz, R.W., Hlubek, M.D., Sorensen, S.D., Fisher, S.K., Balla, T., Ozaki, S., Prestwich, G.D., Stuenkel, E.L., and Bittner, M.A. (2000). A pleckstrin homology domain specific for phosphatidylinositol 4, 5-bisphosphate (Ptdlns-4, 5-P2) and fused to green fluorescent protein identifies plasma membrane PtdIns-4, 5-P2 as being important in exocytosis. J. Biol. Chem. 275, 17878-17885.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17878-17885
    • Holz, R.W.1    Hlubek, M.D.2    Sorensen, S.D.3    Fisher, S.K.4    Balla, T.5    Ozaki, S.6    Prestwich, G.D.7    Stuenkel, E.L.8    Bittner, M.A.9
  • 21
    • 0024251667 scopus 로고
    • Inhibition of kinesin-driven microtubule motility by monoclonal antibodies to kinesin heavy chains
    • Ingold, A.L., Cohn, S.A., and Scholey, J.M. (1988). Inhibition of kinesin-driven microtubule motility by monoclonal antibodies to kinesin heavy chains. J. Cell Biol. 107, 2657-2667.
    • (1988) J. Cell Biol. , vol.107 , pp. 2657-2667
    • Ingold, A.L.1    Cohn, S.A.2    Scholey, J.M.3
  • 23
    • 0033636136 scopus 로고    scopus 로고
    • Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-I
    • Kamal, A., Stokin, G.B., Yang, Z., Xia, C.H., and Goldstein, L.S. (2000). Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-I. Neuron 28, 449-459.
    • (2000) Neuron , vol.28 , pp. 449-459
    • Kamal, A.1    Stokin, G.B.2    Yang, Z.3    Xia, C.H.4    Goldstein, L.S.5
  • 25
    • 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
  • 26
    • 0028028022 scopus 로고
    • Phosphorylation, high ionic strength, and calmodulin reverse the binding of MARCKS to phospholipid vesicles
    • Kim, J., Shishido, T., Jiang, X., Aderem, A., and McLaughlin, S. (1994). Phosphorylation, high ionic strength, and calmodulin reverse the binding of MARCKS to phospholipid vesicles. J. Biol. Chem. 269, 28214-28219.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28214-28219
    • Kim, J.1    Shishido, T.2    Jiang, X.3    Aderem, A.4    McLaughlin, S.5
  • 27
    • 0034693264 scopus 로고    scopus 로고
    • Distinct polyphosphoinositide binding selectivities for pleckstrin homology domains of GRP1-like proteins based on diglycine versus triglycine motifs
    • Klarlund, J.K., Tsiaras, W., Holik, J.J., Chawla, A., and Czech, M.P. (2000). Distinct polyphosphoinositide binding selectivities for pleckstrin homology domains of GRP1-like proteins based on diglycine versus triglycine motifs. J. Biol. Chem. 275, 32816-32821.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32816-32821
    • Klarlund, J.K.1    Tsiaras, W.2    Holik, J.J.3    Chawla, A.4    Czech, M.P.5
  • 28
    • 0037013148 scopus 로고    scopus 로고
    • Role of phosphatidylinositol(4, 5)bisphosphate organization in membrane transport by the Unc104 kinesin motor
    • Klopfenstein, D.R., Tomishige, M., Stuurman, N., and Vale, R.D. (2002). Role of phosphatidylinositol(4, 5)bisphosphate organization in membrane transport by the Unc104 kinesin motor. Cell 109, 347-358.
    • (2002) Cell , vol.109 , pp. 347-358
    • Klopfenstein, D.R.1    Tomishige, M.2    Stuurman, N.3    Vale, R.D.4
  • 29
    • 0031926806 scopus 로고    scopus 로고
    • Disassembly of actin filaments leads to increased rate and frequency of mitochondrial movement along microtubules
    • Krendel, M., Sgourdas, G., and Bonder, E.M. (1998). Disassembly of actin filaments leads to increased rate and frequency of mitochondrial movement along microtubules. Cell Motil. Cytoskel. 40, 368-378.
    • (1998) Cell Motil. Cytoskel. , vol.40 , pp. 368-378
    • Krendel, M.1    Sgourdas, G.2    Bonder, E.M.3
  • 32
    • 0034694152 scopus 로고    scopus 로고
    • Role of microtubules and actin filaments in the movement of mitochondria in the axons and dendrites of cultured hippocampal neurons
    • Ligon, L.A., and Steward, O. (2000). Role of microtubules and actin filaments in the movement of mitochondria in the axons and dendrites of cultured hippocampal neurons. J. Comp. Neurol. 427, 351-361.
    • (2000) J. Comp. Neurol. , vol.427 , pp. 351-361
    • Ligon, L.A.1    Steward, O.2
  • 34
    • 0034683573 scopus 로고    scopus 로고
    • Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function
    • Milner, D.J., Mavroidis, M., Weisleder, N., and Capetanaki, Y. (2000). Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function. J. Cell Biol. 150, 1283-1298.
    • (2000) J. Cell Biol. , vol.150 , pp. 1283-1298
    • Milner, D.J.1    Mavroidis, M.2    Weisleder, N.3    Capetanaki, Y.4
  • 35
    • 0036469290 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 phosphorylates kinesin light chains and negatively regulates kinesin-based motility
    • Morfini, G., Szebenyi, G., Elluru, R., Ratner, N., and Brady, S.T. (2002). Glycogen synthase kinase 3 phosphorylates kinesin light chains and negatively regulates kinesin-based motility. EMBO J. 21, 281-293.
    • (2002) EMBO J. , vol.21 , pp. 281-293
    • Morfini, G.1    Szebenyi, G.2    Elluru, R.3    Ratner, N.4    Brady, S.T.5
  • 36
    • 0027210387 scopus 로고
    • The regulation of bidirectional mitochondrial transport is coordinated with axonal out-growth
    • Morris, R.L., and Hollenbeck, P.J. (1993). The regulation of bidirectional mitochondrial transport is coordinated with axonal out-growth. J. Cell Sci. 104(Pt 3), 917-927.
    • (1993) J. Cell Sci. , vol.104 , Issue.PART 3 , pp. 917-927
    • Morris, R.L.1    Hollenbeck, P.J.2
  • 37
    • 0028861992 scopus 로고
    • Axonal transport of mitochondria along microtubules and F-actin in living vertebrate neurons
    • Morris, R.L., and Hollenbeck, P.J. (1995). Axonal transport of mitochondria along microtubules and F-actin in living vertebrate neurons. J. Cell Biol. 131, 1315-1326.
    • (1995) J. Cell Biol. , vol.131 , pp. 1315-1326
    • Morris, R.L.1    Hollenbeck, P.J.2
  • 38
    • 0035104723 scopus 로고    scopus 로고
    • Dynactin-dependent, dynein-driven vesicle transport in the absence of membrane proteins: A role for spectrin and acidic phospholipids
    • Muresan, V., Stankewich, M.C., Steffen, W., Morrow, J.S., Holzbaur, E.L., and Schnapp, B.J. (2001). Dynactin-dependent, dynein-driven vesicle transport in the absence of membrane proteins: a role for spectrin and acidic phospholipids. Mol. Cell 7, 173-183.
    • (2001) Mol. Cell , vol.7 , pp. 173-183
    • Muresan, V.1    Stankewich, M.C.2    Steffen, W.3    Morrow, J.S.4    Holzbaur, E.L.5    Schnapp, B.J.6
  • 39
    • 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
  • 40
    • 0030820924 scopus 로고    scopus 로고
    • A comparative analysis of the phosphoinositide binding specificity of pleckstrin homology domains
    • Rameh, L.E. et al. (1997). A comparative analysis of the phosphoinositide binding specificity of pleckstrin homology domains. J. Biol. Chem. 272, 22059-22066.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22059-22066
    • Rameh, L.E.1
  • 41
    • 0034695461 scopus 로고    scopus 로고
    • Phosphatidylinositol 4, 5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion
    • Raucher, D., Stauffer, T., Chen, W., Shen, K., Guo, S., York, J.D., Sheetz, M.P., and Meyer, T. (2000). Phosphatidylinositol 4, 5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion. Cell 100, 221-228.
    • (2000) Cell , vol.100 , pp. 221-228
    • Raucher, D.1    Stauffer, T.2    Chen, W.3    Shen, K.4    Guo, S.5    York, J.D.6    Sheetz, M.P.7    Meyer, T.8
  • 42
    • 0027050183 scopus 로고
    • Phosphoinositide-specific phospholipase C-delta 1 binds with high affinity to phospholipid vesicles containing phosphatidylinositol 4, 5-bisphosphate
    • Rebecchi, M., Peterson, A., and McLaughlin, S. (1992). Phosphoinositide-specific phospholipase C-delta 1 binds with high affinity to phospholipid vesicles containing phosphatidylinositol 4, 5-bisphosphate. Biochemistry 31, 12742-12747.
    • (1992) Biochemistry , vol.31 , pp. 12742-12747
    • Rebecchi, M.1    Peterson, A.2    McLaughlin, S.3
  • 44
    • 0344462724 scopus 로고    scopus 로고
    • Association of mitochondria with plectin and desmin intermediate filaments in striated muscle
    • Reipert, S., Steinbock, F., Fischer, I., Bittner, R.E., Zeold, A., and Wiche, G. (1999). Association of mitochondria with plectin and desmin intermediate filaments in striated muscle. Exp. Cell Res. 252, 479-491.
    • (1999) Exp. Cell Res. , vol.252 , pp. 479-491
    • Reipert, S.1    Steinbock, F.2    Fischer, I.3    Bittner, R.E.4    Zeold, A.5    Wiche, G.6
  • 45
    • 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
  • 46
    • 0016613360 scopus 로고
    • The ultrastructure of mouse neuroblastoma cells in tissue culture
    • Ross, J., Olmsted, J.B., and Rosenbaum, J.L. (1975). The ultrastructure of mouse neuroblastoma cells in tissue culture. Tissue Cell 7, 107-135.
    • (1975) Tissue Cell , vol.7 , pp. 107-135
    • Ross, J.1    Olmsted, J.B.2    Rosenbaum, J.L.3
  • 47
    • 0021287579 scopus 로고
    • Subcellular incorporation of 32P into phosphoinositides and other phospholipids in isolated hepatocytes
    • Seyfred, M.A., and Wells, W.W. (1984). Subcellular incorporation of 32P into phosphoinositides and other phospholipids in isolated hepatocytes. J. Biol. Chem. 259, 7659-7665.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7659-7665
    • Seyfred, M.A.1    Wells, W.W.2
  • 48
    • 0033563024 scopus 로고    scopus 로고
    • Motor and cargo interactions
    • Sheetz, M.P. (1999). Motor and cargo interactions. Eur. J. Biochem. 262, 19-25.
    • (1999) Eur. J. Biochem. , vol.262 , pp. 19-25
    • Sheetz, M.P.1
  • 49
    • 0032510323 scopus 로고    scopus 로고
    • Receptor-induced transient reduction in plasma membrane PtdIns(4, 5)P2 concentration monitored in living cells
    • Stauffer, T.P., Ahn, S., and Meyer, T. (1998). Receptor-induced transient reduction in plasma membrane PtdIns(4, 5)P2 concentration monitored in living cells. Curr. Biol. 8, 343-346.
    • (1998) Curr. Biol. , vol.8 , pp. 343-346
    • Stauffer, T.P.1    Ahn, S.2    Meyer, T.3
  • 50
    • 0032568790 scopus 로고    scopus 로고
    • Targeted disruption of mouse conventional kinesin heavv 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 heavv 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
  • 51
    • 0027241408 scopus 로고
    • Interaction of myristoylated alanine-rich protein kinase C substrate (MARCKS) with membrane phospholipids
    • Taniguchi, H., and Manenti, S. (1993). Interaction of myristoylated alanine-rich protein kinase C substrate (MARCKS) with membrane phospholipids. J. Biol. Chem. 268, 9960-9963.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9960-9963
    • Taniguchi, H.1    Manenti, S.2
  • 52
    • 0019226175 scopus 로고
    • Association of mitochondria with intermediate filaments and of polyribosomes with cytoplasmic actin
    • Toh, B.H., Lolait, S.J., Mathy, J.P., and Baum, R. (1980). Association of mitochondria with intermediate filaments and of polyribosomes with cytoplasmic actin. Cell Tissue Res. 211, 163-169.
    • (1980) Cell Tissue Res. , vol.211 , pp. 163-169
    • Toh, B.H.1    Lolait, S.J.2    Mathy, J.P.3    Baum, R.4
  • 53
    • 0033529031 scopus 로고    scopus 로고
    • Neuronal overexpression of APPL, the Drosophila homologue of the amyloid precursor protein (APP), disrupts axonal transport
    • Torroja, L., Chu, H., Kotovsky, I., and White, K. (1999). Neuronal overexpression of APPL, the Drosophila homologue of the amyloid precursor protein (APP), disrupts axonal transport. Curr. Biol. 9, 489-492.
    • (1999) Curr. Biol. , vol.9 , pp. 489-492
    • Torroja, L.1    Chu, H.2    Kotovsky, I.3    White, K.4
  • 55
    • 0033545698 scopus 로고    scopus 로고
    • Importance of the pleckstrin homology domain of dynamin in clathrin-mediated endocytosis
    • Vallis, Y., Wigge, P., Marks, B., Evans, P.R., and McMahon, H.T. (1999). Importance of the pleckstrin homology domain of dynamin in clathrin-mediated endocytosis. Curr. Biol. 9, 257-260.
    • (1999) Curr. Biol. , vol.9 , pp. 257-260
    • Vallis, Y.1    Wigge, P.2    Marks, B.3    Evans, P.R.4    McMahon, H.T.5
  • 57
    • 0033514366 scopus 로고    scopus 로고
    • Differential association of the pleckstrin homology domains of phospholipases C-beta 1, C-beta 2, and C-delta 1 with lipid bilayers and the beta gamma subunits of heterotrimeric G proteins
    • Wang, T., Pentyala, S., Rebecchi, M.J., and Scarlata, S. (1999). Differential association of the pleckstrin homology domains of phospholipases C-beta 1, C-beta 2, and C-delta 1 with lipid bilayers and the beta gamma subunits of heterotrimeric G proteins. Biochemistry 38, 1517-1524.
    • (1999) Biochemistry , vol.38 , pp. 1517-1524
    • Wang, T.1    Pentyala, S.2    Rebecchi, M.J.3    Scarlata, S.4
  • 58
    • 0036566427 scopus 로고    scopus 로고
    • Subcellular localization of phosphatidylinositol 4, 5-bisphosphate using the pleckstrin homology domain of phospholipase C delta1
    • Watt, S.A., Kular, G., Fleming, I.N., Downes, C.P., and Lucocq, J.M. (2002). Subcellular localization of phosphatidylinositol 4, 5-bisphosphate using the pleckstrin homology domain of phospholipase C delta1. Biochem. J. 363, 657-666.
    • (2002) Biochem. J. , vol.363 , pp. 657-666
    • Watt, S.A.1    Kular, G.2    Fleming, I.N.3    Downes, C.P.4    Lucocq, J.M.5
  • 59
    • 0031050564 scopus 로고    scopus 로고
    • Inhibition of a mitotic motor compromises the formation of dendrite-like processes from neuroblastoma cells
    • Yu, W., Sharp, D.J., Kuriyama, R., Mallik, P., and Baas, P.W. (1997). Inhibition of a mitotic motor compromises the formation of dendrite-like processes from neuroblastoma cells. J. Cell Biol. 136, 659-668.
    • (1997) J. Cell Biol. , vol.136 , pp. 659-668
    • Yu, W.1    Sharp, D.J.2    Kuriyama, R.3    Mallik, P.4    Baas, P.W.5
  • 60
    • 0022518521 scopus 로고
    • Spectrin subtypes in mammalian brain: An immunoelectron microscopic study
    • Zagon, I.S., Higbee, R., Riederer, B.M., and Goodman, S.R. (1986). Spectrin subtypes in mammalian brain: an immunoelectron microscopic study. J. Neurosci. 6, 2977-2986.
    • (1986) J. Neurosci. , vol.6 , pp. 2977-2986
    • Zagon, I.S.1    Higbee, R.2    Riederer, B.M.3    Goodman, S.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.