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Volumn 17, Issue 7, 2006, Pages 3176-3186

CytLEK1 is a regulator of plasma membrane recycling through its interaction with SNAP-25

Author keywords

[No Author keywords available]

Indexed keywords

CYTOPLASM PROTEIN; CYTOPLASMIC LEK1 PROTEIN; LEK1 PROTEIN; MYOSIN V; MYOSIN VB; RAB PROTEIN; RAB11A PROTEIN; SNARE PROTEIN; SYNAPTOBREVIN 2; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNTAXIN; SYNTAXIN 4; TRANSFERRIN; UNCLASSIFIED DRUG;

EID: 33745608087     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E05-12-1127     Document Type: Article
Times cited : (19)

References (77)
  • 1
    • 31944441121 scopus 로고    scopus 로고
    • SNAP25, but not syntaxin 1A, recycles via an ARF6-regulated pathway in neuroendocrine cells
    • Aikawa, Y., Xia, X., and Martin, T.F.J. (2006). SNAP25, but not syntaxin 1A, recycles via an ARF6-regulated pathway in neuroendocrine cells. Mol. Biol. Cell 17, 711-722.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 711-722
    • Aikawa, Y.1    Xia, X.2    Martin, T.F.J.3
  • 3
    • 0028346520 scopus 로고
    • Receptor-mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes
    • Apodaca, G., Katz, L. A., and Mostov, K. E. (1994). Receptor-mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes. J. Cell Biol. 125, 67-86.
    • (1994) J. Cell Biol. , vol.125 , pp. 67-86
    • Apodaca, G.1    Katz, L.A.2    Mostov, K.E.3
  • 4
    • 0347052864 scopus 로고    scopus 로고
    • LEK1 is a potential inhibitor of pocket protein-mediated cellular processes
    • Ashe, M., Pabon-Pena, L. M., Dees, E., Price, K. L., and Bader, D. M. (2004). LEK1 is a potential inhibitor of pocket protein-mediated cellular processes. J. Cell Biol. 279, 664-676.
    • (2004) J. Cell Biol. , vol.279 , pp. 664-676
    • Ashe, M.1    Pabon-Pena, L.M.2    Dees, E.3    Price, K.L.4    Bader, D.M.5
  • 5
    • 0037145811 scopus 로고    scopus 로고
    • Endogenous plasma membrane t-SNARE syntaxin 4 is present in rab11 positive endosomal membranes and associates with cortical actin cytoskeleton
    • Band, A. M., Ali, H., Vartiainen, M. K., Welti, S., Lappalainen, P., Olkkonen, V. M., and Kuismanen, E. (2002). Endogenous plasma membrane t-SNARE syntaxin 4 is present in rab11 positive endosomal membranes and associates with cortical actin cytoskeleton. FEBS Lett. 531, 513-519.
    • (2002) FEBS Lett. , vol.531 , pp. 513-519
    • Band, A.M.1    Ali, H.2    Vartiainen, M.K.3    Welti, S.4    Lappalainen, P.5    Olkkonen, V.M.6    Kuismanen, E.7
  • 6
    • 0035916323 scopus 로고    scopus 로고
    • Chromosome movement: Dynein-out at the kinetochore
    • Banks, J. D., and Heald, R. (2001). Chromosome movement: dynein-out at the kinetochore. Curr. Biol. 11, R128-R131.
    • (2001) Curr. Biol. , vol.11
    • Banks, J.D.1    Heald, R.2
  • 7
    • 33745608928 scopus 로고    scopus 로고
    • Evidence for targeted vesicular glutamate exocytosis in osteoblasts
    • discussion 1327-1328
    • Bhangu, P. S., Genever, P. G., Spencer, G. J., Grewal, T. S., and Skerry, T. M. (2003). Evidence for targeted vesicular glutamate exocytosis in osteoblasts. Br. Med. J. 326, 1326; discussion 1327-1328.
    • (2003) Br. Med. J. , vol.326 , pp. 1326
    • Bhangu, P.S.1    Genever, P.G.2    Spencer, G.J.3    Grewal, T.S.4    Skerry, T.M.5
  • 8
    • 2942601325 scopus 로고    scopus 로고
    • Syntaxin 8 impairs trafficking of cystic fibrosis transmembrane conductance regulator (CFTR) and inhibits its channel activity
    • Bilan, F. Thoreau, V. Nacfer, M., Derand, R., Norez, C., Cantereau, A., Garcia, M., Becq, F., and Kitzis, A. (2004). syntaxin 8 impairs trafficking of cystic fibrosis transmembrane conductance regulator (CFTR) and inhibits its channel activity. J. Cell Sci. 117, 1923-1935.
    • (2004) J. Cell Sci. , vol.117 , pp. 1923-1935
    • Bilan, F.1    Thoreau, V.2    Nacfer, M.3    Derand, R.4    Norez, C.5    Cantereau, A.6    Garcia, M.7    Becq, F.8    Kitzis, A.9
  • 9
    • 0028815453 scopus 로고
    • The t-SNAREs syntaxin 1 and SNAP-25 are present on organelles that participate in synaptic vesicle recycling
    • Blasi, J., Edelmann, L., Chapman, E. R., von Mollard, G. F., Jahn, R., and Walch-Solimena, C. (1995). The t-SNAREs syntaxin 1 and SNAP-25 are present on organelles that participate in synaptic vesicle recycling. J. Cell Biol. 128, 637-645.
    • (1995) J. Cell Biol. , vol.128 , pp. 637-645
    • Blasi, J.1    Edelmann, L.2    Chapman, E.R.3    Von Mollard, G.F.4    Jahn, R.5    Walch-Solimena, C.6
  • 10
    • 0039228647 scopus 로고
    • Fusion between endocytic vesicles in a cell-free system
    • Braell, W. A. (1987). Fusion between endocytic vesicles in a cell-free system. Proc. Natl. Acad. Sci. USA 84, 1137-1141.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1137-1141
    • Braell, W.A.1
  • 11
    • 4644363334 scopus 로고    scopus 로고
    • Characterization of early endosome antigen 1 in neural tissues
    • Braun, J. E., Fritzler, M. J., and Selak, S. (2004). Characterization of early endosome antigen 1 in neural tissues. Biochem. Biophys. Res. Commun. 323, 1334-1342.
    • (2004) Biochem. Biophys. Res. Commun. , vol.323 , pp. 1334-1342
    • Braun, J.E.1    Fritzler, M.J.2    Selak, S.3
  • 12
    • 0030751653 scopus 로고    scopus 로고
    • Two Rab proteins, vesicle-associated membrane protein 2 (VAMP-2) and secretory carrier membrane proteins (SCAMPs), are present on immunoisolated parietal cell tubulovesicles
    • Calhoun, B. C., and Goldenring, J. R. (1997). Two Rab proteins, vesicle-associated membrane protein 2 (VAMP-2) and secretory carrier membrane proteins (SCAMPs), are present on immunoisolated parietal cell tubulovesicles. Biochem. J. 325, 559-564.
    • (1997) Biochem. J. , vol.325 , pp. 559-564
    • Calhoun, B.C.1    Goldenring, J.R.2
  • 14
    • 0027973132 scopus 로고
    • SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils
    • Chapman, E. R., An, S., Barton, N., and Jahn, R. (1994). SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils. J. Biol. Chem. 269, 27427-27432.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27427-27432
    • Chapman, E.R.1    An, S.2    Barton, N.3    Jahn, R.4
  • 16
    • 0023745656 scopus 로고
    • Dynamic behavior of the transferrin receptor followed in living epidermoid carcinoma (A431) cells with nanovid microscopy
    • De Brabander, M., Nuydens, R., Geerts, H., and Hopkins, C. R. (1988). Dynamic behavior of the transferrin receptor followed in living epidermoid carcinoma (A431) cells with nanovid microscopy. Cell Motil. Cytoskelet. 9, 30-47.
    • (1988) Cell Motil. Cytoskelet. , vol.9 , pp. 30-47
    • De Brabander, M.1    Nuydens, R.2    Geerts, H.3    Hopkins, C.R.4
  • 18
    • 0033774834 scopus 로고    scopus 로고
    • Characterization of CMF1 in avian skeletal muscle
    • Dees, E., Pabon-Pena, L. M., Goodwin, R. L., and Bader, D. (2000). Characterization of CMF1 in avian skeletal muscle. Dev. Dynam. 219, 169-181.
    • (2000) Dev. Dynam. , vol.219 , pp. 169-181
    • Dees, E.1    Pabon-Pena, L.M.2    Goodwin, R.L.3    Bader, D.4
  • 20
    • 0033777678 scopus 로고    scopus 로고
    • A role for the lissencephaly gene LIS1 in mitosis and cytoplasmic dynein function
    • see comment
    • Faulkner, N. E. (2000). A role for the lissencephaly gene LIS1 in mitosis and cytoplasmic dynein function.[see comment]. Nat. Cell Biol. 2, 784-791.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 784-791
    • Faulkner, N.E.1
  • 21
    • 33745591347 scopus 로고    scopus 로고
    • Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes
    • Foletti, D. L., Scheller, R. H., and Prekeris, R. (1999). syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes. J. Neurosci. 19, 10324-10337.
    • (1999) J. Neurosci. , vol.19 , pp. 10324-10337
    • Foletti, D.L.1    Scheller, R.H.2    Prekeris, R.3
  • 22
    • 0028085865 scopus 로고
    • Quantification of low density lipoprotein and transferrin endocytic sorting HEp2 cells using confocal microscopy
    • Ghosh, R. N., Gelman, D. L., and Maxfield, F. R. (1994). Quantification of low density lipoprotein and transferrin endocytic sorting HEp2 cells using confocal microscopy. J. Cell Sci. 107, 2177-2189.
    • (1994) J. Cell Sci. , vol.107 , pp. 2177-2189
    • Ghosh, R.N.1    Gelman, D.L.2    Maxfield, F.R.3
  • 23
    • 0030460756 scopus 로고    scopus 로고
    • The role of dynein in microtubule-based motility
    • Gibbons, I. R. (1996). The role of dynein in microtubule-based motility. Cell Struct. Funct. 21, 331-342.
    • (1996) Cell Struct. Funct. , vol.21 , pp. 331-342
    • Gibbons, I.R.1
  • 24
    • 0040737599 scopus 로고    scopus 로고
    • The cloning and analysis of LEK1 identifies variations in the LEK/centromere protein F/mitosin gene family
    • Goodwin, R. L., Pabon-Pena, L., Dees, E., Price, K. L., and Bader, D. (1999). The cloning and analysis of LEK1 identifies variations in the LEK/centromere protein F/mitosin gene family. J. Biol. Chem. 274, 664-676.
    • (1999) J. Biol. Chem. , vol.274 , pp. 664-676
    • Goodwin, R.L.1    Pabon-Pena, L.2    Dees, E.3    Price, K.L.4    Bader, D.5
  • 26
    • 0024517745 scopus 로고
    • Characterization of the early endosome and putative endocytic carrier vesicles in vivo and with an assay of vesicle fusion in vitro
    • Gruenberg, J., Griffiths, G., and Howell, K. E. (1989). Characterization of the early endosome and putative endocytic carrier vesicles in vivo and with an assay of vesicle fusion in vitro. J. Cell Biol. 108, 1301-1316.
    • (1989) J. Cell Biol. , vol.108 , pp. 1301-1316
    • Gruenberg, J.1    Griffiths, G.2    Howell, K.E.3
  • 27
    • 0037184989 scopus 로고    scopus 로고
    • Rab11 family interacting protein 2 associates with Myosin Vb and regulates plasma membrane recycling
    • Hales, C. M., Vaerman, J. P., and Goldenring, J. R. (2002). Rab11 family interacting protein 2 associates with Myosin Vb and regulates plasma membrane recycling. J. Biol. Chem. 277, 50415-50421.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50415-50421
    • Hales, C.M.1    Vaerman, J.P.2    Goldenring, J.R.3
  • 28
    • 0034046587 scopus 로고    scopus 로고
    • Syntaxin 13 is a developmentally regulated SNARE involved in neurite outgrowth and endosomal trafficking
    • Hirling, H., Steiner, P., Chaperon, C., Marsault, R., Regazzi, R., and Catsicas, S. (2000). syntaxin 13 is a developmentally regulated SNARE involved in neurite outgrowth and endosomal trafficking. European J. Neurosci. 12, 1913-1923.
    • (2000) European J. Neurosci. , vol.12 , pp. 1913-1923
    • Hirling, H.1    Steiner, P.2    Chaperon, C.3    Marsault, R.4    Regazzi, R.5    Catsicas, S.6
  • 29
    • 20444407298 scopus 로고    scopus 로고
    • SNAREs and traffic
    • Hong, W. (2005). SNAREs and traffic. Biochim. Biophys. Acta 1744, 493-517.
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 493-517
    • Hong, W.1
  • 30
    • 0029817806 scopus 로고    scopus 로고
    • Insulin-responsive tissues contain the core complex protein SNAP-25 (synaptosomal-associated protein 25) a and B isoforms in addition to syntaxin 4 and synaptobrevins 1 and 2
    • Jagadish, M. N. et al. (1996). Insulin-responsive tissues contain the core complex protein SNAP-25 (synaptosomal-associated protein 25) A and B isoforms in addition to syntaxin 4 and synaptobrevins 1 and 2. Biochem. J. 317, 945-954.
    • (1996) Biochem. J. , vol.317 , pp. 945-954
    • Jagadish, M.N.1
  • 31
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn, R., and Sudhof, T. C. (1999). Membrane fusion and exocytosis. Annu. Rev. Biochem. 68, 863-911.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 863-911
    • Jahn, R.1    Sudhof, T.C.2
  • 32
    • 4043181982 scopus 로고    scopus 로고
    • Molecular characterization of Rab11 interactions with members of the family of Rab11-interacting proteins
    • Junutula, J. R., Schonteich, E., Wilson, G. M., Peden, A. A., Scheller, R. H., and Prekeris, R. (2004). Molecular characterization of Rab11 interactions with members of the family of Rab11-interacting proteins. J. Biol. Chem. 279, 33430-33437.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33430-33437
    • Junutula, J.R.1    Schonteich, E.2    Wilson, G.M.3    Peden, A.A.4    Scheller, R.H.5    Prekeris, R.6
  • 33
    • 0037147142 scopus 로고    scopus 로고
    • Localization and function of soluble N-ethylmaleimide-sensitive factor attachment protein-25 and vesicle-associated membrane protein-2 in functioning gastric parietal cells
    • Karvar, S., Yao, X., Crothers, J. M., Jr., Liu, Y., and Forte, J. G. (2002). Localization and function of soluble N-ethylmaleimide-sensitive factor attachment protein-25 and vesicle-associated membrane protein-2 in functioning gastric parietal cells. J. Biol. Chem. 277, 50030-50035.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50030-50035
    • Karvar, S.1    Yao, X.2    Crothers Jr., J.M.3    Liu, Y.4    Forte, J.G.5
  • 34
    • 0034089050 scopus 로고    scopus 로고
    • Nerve growth factor-induced phosphorylation of SNAP-25 in PC12 cells: A possible involvement in the regulation of SNAP-25 localization
    • Kataoka, M., Kuwahara, R., Iwasaki, S., Shoji-Kasai, Y., and Takahashi, M. (2000). Nerve growth factor-induced phosphorylation of SNAP-25 in PC12 cells: a possible involvement in the regulation of SNAP-25 localization. J. Neurochem. 74, 2058-2066.
    • (2000) J. Neurochem. , vol.74 , pp. 2058-2066
    • Kataoka, M.1    Kuwahara, R.2    Iwasaki, S.3    Shoji-Kasai, Y.4    Takahashi, M.5
  • 35
    • 33745632587 scopus 로고    scopus 로고
    • Syntaxin 7 and VAMP-7 are soluble N-ethylmaleimide-sensitive factor attachment protein receptors required for late endosome-lysosome and homotypic lysosome fusion in alveolar macrophages
    • Kodrik, D., Yang, C., Sehnal, F., Scheller, K., and Ward, D. M. (1998). syntaxin 7 and VAMP-7 are soluble N-ethylmaleimide-sensitive factor attachment protein receptors required for late endosome-lysosome and homotypic lysosome fusion in alveolar macrophages. Mol. Gen. Genet. 257, 264-270.
    • (1998) Mol. Gen. Genet. , vol.257 , pp. 264-270
    • Kodrik, D.1    Yang, C.2    Sehnal, F.3    Scheller, K.4    Ward, D.M.5
  • 36
    • 0034078261 scopus 로고    scopus 로고
    • Localization and physiological regulation of the exocytosis protein SNAP-25 in the brain and pituitary gland of Xenopus laevis
    • Kolk, S. M., Nordquist, R., Tuinhof, R., Gagliardini, L., Thompson, B., Cools, A. R., and Roubos, E. W. (2000). Localization and physiological regulation of the exocytosis protein SNAP-25 in the brain and pituitary gland of Xenopus laevis. J. Neuroendocrinol. 12, 694-706.
    • (2000) J. Neuroendocrinol. , vol.12 , pp. 694-706
    • Kolk, S.M.1    Nordquist, R.2    Tuinhof, R.3    Gagliardini, L.4    Thompson, B.5    Cools, A.R.6    Roubos, E.W.7
  • 39
    • 1242285142 scopus 로고    scopus 로고
    • Nudel functions in membrane traffic mainly through association with Lis1 and cytoplasmic dynein
    • Liang, Y., Yu, W., Li, Y., Yang, Z., Yan, X., Huang, Q., and Zhu, X. (2004b). Nudel functions in membrane traffic mainly through association with Lis1 and cytoplasmic dynein. J. Cell Biol. 164, 557-566.
    • (2004) J. Cell Biol. , vol.164 , pp. 557-566
    • Liang, Y.1    Yu, W.2    Li, Y.3    Yang, Z.4    Yan, X.5    Huang, Q.6    Zhu, X.7
  • 40
    • 33745613768 scopus 로고
    • CENP-F is a protein of the nuclear matrix that assembles onto kinetochores at late G2 and is rapidly degraded after mitosis
    • Liao, H., Yen, T. J., and Cleveland, D. W. (1995). CENP-F is a protein of the nuclear matrix that assembles onto kinetochores at late G2 and is rapidly degraded after mitosis. J. Cell Biol. 112, 1083-1097.
    • (1995) J. Cell Biol. , vol.112 , pp. 1083-1097
    • Liao, H.1    Yen, T.J.2    Cleveland, D.W.3
  • 41
    • 0037178832 scopus 로고    scopus 로고
    • Rab11-FIP2 functions in transferrin recycling and associates with endosomal membranes via its COOH-terminal domain
    • Lindsay, A. J., and McCaffrey, M. W. (2002). Rab11-FIP2 functions in transferrin recycling and associates with endosomal membranes via its COOH-terminal domain. J. Biol. Chem. 277, 27193-27199.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27193-27199
    • Lindsay, A.J.1    McCaffrey, M.W.2
  • 42
    • 0033520460 scopus 로고    scopus 로고
    • Rab11BP/Rabphilin-11, a downstream target of rab11 small G protein implicated in vesicle recycling
    • Mammoto, A., Ohtsuka, T., Hotta, I., Sasaki, T., and Takai, Y. (1999). Rab11BP/Rabphilin-11, a downstream target of rab11 small G protein implicated in vesicle recycling. J. Biol. Chem. 274, 25517-25524.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25517-25524
    • Mammoto, A.1    Ohtsuka, T.2    Hotta, I.3    Sasaki, T.4    Takai, Y.5
  • 43
    • 0029098787 scopus 로고
    • Characterization of a novel 350-kilodalton nuclear phosphoprotein that is specifically involved in mitotic-phase progression
    • Mancini, M. A., Chang, K. H., Liu, C. Y., Chen, C. F., Shan, B., Jones, D., Yang-Feng, T. L., Lee, W. H., and Zhu, X. (1995). Characterization of a novel 350-kilodalton nuclear phosphoprotein that is specifically involved in mitotic-phase progression. Mol. Cell. Biol. 15, 5017-5029.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5017-5029
    • Mancini, M.A.1    Chang, K.H.2    Liu, C.Y.3    Chen, C.F.4    Shan, B.5    Jones, D.6    Yang-Feng, T.L.7    Lee, W.H.8    Zhu, X.9
  • 44
    • 0036902478 scopus 로고    scopus 로고
    • Bicaudal-D regulates COPI-independent Golgi-ER transport by recruiting the dynein-dynactin motor complex
    • Matanis, T., et al. (2003). Bicaudal-D regulates COPI-independent Golgi-ER transport by recruiting the dynein-dynactin motor complex. Nat. Cell Biol. 4, 986-992.
    • (2003) Nat. Cell Biol. , vol.4 , pp. 986-992
    • Matanis, T.1
  • 45
    • 0027265710 scopus 로고
    • Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a putative synaptic vesicle fusion protein
    • McMahon, H. T. (1993). Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a putative synaptic vesicle fusion protein. Nature 364.
    • (1993) Nature , pp. 364
    • McMahon, H.T.1
  • 46
    • 33745635008 scopus 로고    scopus 로고
    • Isolation of a new set of Aspergillus nidulans mutants defective in nuclear migration
    • Morris, N. R., and Xiang, X. (2000). Isolation of a new set of Aspergillus nidulans mutants defective in nuclear migration. J. Cell Biol. 150, 681-688.
    • (2000) J. Cell Biol. , vol.150 , pp. 681-688
    • Morris, N.R.1    Xiang, X.2
  • 47
    • 33745595567 scopus 로고    scopus 로고
    • Syntaxin 7 is localized to late endosome compartments, associates with Vamp 8, and is required for late endosome-lysosome fusion
    • Mullock, B. M., Pryor, P. R., Lindsay, M. R., James, D. E., and Piper, R. C. (2001). syntaxin 7 is localized to late endosome compartments, associates with Vamp 8, and is required for late endosome-lysosome fusion. Biochem. Soc. Trans. 29, 476-480.
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 476-480
    • Mullock, B.M.1    Pryor, P.R.2    Lindsay, M.R.3    James, D.E.4    Piper, R.C.5
  • 48
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • see comment
    • Nagai, T., Kirino, Y., Mizuno, H., and Miyawaki, A. (2002). A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications.[see comment]. Nat. Biotechnol. 20, 87-90.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 87-90
    • Nagai, T.1    Kirino, Y.2    Mizuno, H.3    Miyawaki, A.4
  • 49
    • 0035151221 scopus 로고    scopus 로고
    • Localization of cellubrevin-related peptide, endobrevin, in the early endosome in pancreatic beta cells and its physiological function in exo-endocytosis of secretory granules
    • Nagamatsu, S., Nakamichi, Y., Watanabe, T. Matsushima, S. Yamaguchi, J., Ni, J., Itagaki, E., and Ishida, H. (2001). Localization of cellubrevin-related peptide, endobrevin, in the early endosome in pancreatic beta cells and its physiological function in exo-endocytosis of secretory granules. J. Cell Sci. 114, 219-227.
    • (2001) J. Cell Sci. , vol.114 , pp. 219-227
    • Nagamatsu, S.1    Nakamichi, Y.2    Watanabe, T.3    Matsushima, S.4    Yamaguchi, J.5    Ni, J.6    Itagaki, E.7    Ishida, H.8
  • 50
    • 16344381891 scopus 로고    scopus 로고
    • MARCH-II is a syntaxin-6-binding protein involved in endosomal trafficking
    • Nakamura, N., Fukuda, H., Kato, A., and Hirose, S. (2005). MARCH-II is a syntaxin-6-binding protein involved in endosomal trafficking. Mol. Biol. Cell 16, 1696-1710.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1696-1710
    • Nakamura, N.1    Fukuda, H.2    Kato, A.3    Hirose, S.4
  • 51
    • 0030860083 scopus 로고    scopus 로고
    • The diversity of Rab proteins in vesicle transport
    • Novick, P., and Zerial, M. (1997). The diversity of Rab proteins in vesicle transport. Curr. Opin. Cell Biol. 9, 496-504.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 496-504
    • Novick, P.1    Zerial, M.2
  • 52
    • 33745605140 scopus 로고    scopus 로고
    • Characterization of CMF1 in avian skeletal muscle
    • Pabon-Pena, L. M., Foster, G. C., Bader, D., and Dees, E. (1999). Characterization of CMF1 in avian skeletal muscle. J. Biol. Chem. 274, 18597-18604.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18597-18604
    • Pabon-Pena, L.M.1    Foster, G.C.2    Bader, D.3    Dees, E.4
  • 53
    • 18944364763 scopus 로고    scopus 로고
    • Interplay between the retinoblastoma protein and LEK1 specifies stem cells toward the cardiac lineage
    • Papadimou, E., Menard, C., Grey, C., and Puceat, M. (2005). Interplay between the retinoblastoma protein and LEK1 specifies stem cells toward the cardiac lineage. EMBO J. 24, 1750-1761.
    • (2005) EMBO J. , vol.24 , pp. 1750-1761
    • Papadimou, E.1    Menard, C.2    Grey, C.3    Puceat, M.4
  • 54
    • 1842424983 scopus 로고    scopus 로고
    • An improved cyan fluorescent protein variant useful for FRET
    • Piston, D. W., and Rizzo, M. A. (2004). An improved cyan fluorescent protein variant useful for FRET. Nat. Biotechnol. 22, 445-449.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 445-449
    • Piston, D.W.1    Rizzo, M.A.2
  • 55
    • 0032538835 scopus 로고    scopus 로고
    • Molecular analysis of the interactions between protein kinase C-epsilon and filamentous actin
    • Prekeris, R., Klumperman, J., and Scheller, R. H. (1998). Molecular analysis of the interactions between protein kinase C-epsilon and filamentous actin. J. Cell Biol. 143, 957-971.
    • (1998) J. Cell Biol. , vol.143 , pp. 957-971
    • Prekeris, R.1    Klumperman, J.2    Scheller, R.H.3
  • 56
    • 33745620423 scopus 로고    scopus 로고
    • Functional studies in 3T3L1 cells support a role for SNARE proteins in insulin stimulation of GLUT4 translocation
    • Rea, S., Gough, K. H., Ward, C. W., James, D. E., and Macaulay, S. L. (1997). Functional studies in 3T3L1 cells support a role for SNARE proteins in insulin stimulation of GLUT4 translocation. Biochem. Biophys. Res. Commun. 237, 388-393.
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , pp. 388-393
    • Rea, S.1    Gough, K.H.2    Ward, C.W.3    James, D.E.4    Macaulay, S.L.5
  • 58
    • 0032568657 scopus 로고    scopus 로고
    • Hydrolysis of GTP on rab11 is required for the direct delivery of transferrin from the pericentriolar recycling compartment to the cell surface but not from sorting endosomes
    • Ren, M., Xu, G., Zeng, J., De Lemos-Chiarandini, C., Adesnik, M., and Sabatini, D. D. (1998). Hydrolysis of GTP on rab11 is required for the direct delivery of transferrin from the pericentriolar recycling compartment to the cell surface but not from sorting endosomes. Proc. Natl. Acad. Sci. USA 95, 6187-6192.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6187-6192
    • Ren, M.1    Xu, G.2    Zeng, J.3    De Lemos-Chiarandini, C.4    Adesnik, M.5    Sabatini, D.D.6
  • 59
    • 33745584317 scopus 로고
    • Evidence that the leucine zipper is a coiled coil
    • Rutkowski, R. Stafford, W. F., 3rd, Kim, P. S., and O'Shea, E. K. (1989). Evidence that the leucine zipper is a coiled coil. Science 245, 646-648.
    • (1989) Science , vol.245 , pp. 646-648
    • Rutkowski, R.1    Stafford III, W.F.2    Kim, P.S.3    O'Shea, E.K.4
  • 60
    • 0026168089 scopus 로고
    • Role of microtubule cytoskeletons in the transduction of growth signals
    • Sakai, H. (1991). Role of microtubule cytoskeletons in the transduction of growth signals. Human Cell 4, 93-99.
    • (1991) Human Cell , vol.4 , pp. 93-99
    • Sakai, H.1
  • 61
    • 0023887115 scopus 로고
    • Intracellular fusion of sequentially formed endocytic compartments
    • Salzman, N. H., and Maxfield, F. R. (1988). Intracellular fusion of sequentially formed endocytic compartments. J. Cell Biol. 106, 1083-1091.
    • (1988) J. Cell Biol. , vol.106 , pp. 1083-1091
    • Salzman, N.H.1    Maxfield, F.R.2
  • 62
    • 0035109941 scopus 로고    scopus 로고
    • Rab3a and SNARE proteins: Potential regulators of melanosome movement
    • Scott, G., and Zhoa, Q. (2001). Rab3a and SNARE proteins: potential regulators of melanosome movement. J. Invest. Dermatol. 116, 296-304.
    • (2001) J. Invest. Dermatol. , vol.116 , pp. 296-304
    • Scott, G.1    Zhoa, Q.2
  • 63
    • 8244241098 scopus 로고    scopus 로고
    • Characterization of two distinct intracellular GLUT4 membrane populations in muscle fiber. Differential protein composition and sensitivity to insulin
    • Sevilla, L. et al. (1997). Characterization of two distinct intracellular GLUT4 membrane populations in muscle fiber. Differential protein composition and sensitivity to insulin. Endocrinology 138, 3006-3015.
    • (1997) Endocrinology , vol.138 , pp. 3006-3015
    • Sevilla, L.1
  • 64
    • 0037018151 scopus 로고    scopus 로고
    • Transferrin receptor recycling in the absence of perinuclear recycling endosomes
    • Sheff, D., Pelletier, L., O'Connell, C. B., Warren, G., and Mellman, I. (2002). Transferrin receptor recycling in the absence of perinuclear recycling endosomes. J. Cell Biol. 156, 797-804.
    • (2002) J. Cell Biol. , vol.156 , pp. 797-804
    • Sheff, D.1    Pelletier, L.2    O'Connell, C.B.3    Warren, G.4    Mellman, I.5
  • 65
    • 0033769717 scopus 로고    scopus 로고
    • Regulation of cytoplasmic dynein behaviour and microtubule organization by mammalian Lis1
    • Smith, D. S. (2000). Regulation of cytoplasmic dynein behaviour and microtubule organization by mammalian Lis1 [comment]. Nat. Cell Biol. 2, 767-775.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 767-775
    • Smith, D.S.1
  • 67
    • 0242446165 scopus 로고    scopus 로고
    • Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11
    • Sonnichsen, B., De Renzis, S., Nielsen, E., Rietdorf, J., and Zerial, M. (2000). Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11. J. Cell Biol. 149, 901-914.
    • (2000) J. Cell Biol. , vol.149 , pp. 901-914
    • Sonnichsen, B.1    De Renzis, S.2    Nielsen, E.3    Rietdorf, J.4    Zerial, M.5
  • 68
    • 20844434818 scopus 로고    scopus 로고
    • Cytoplasmic LEK1 is a regulator of microtubule function through its interaction with the LIS1 pathway
    • Soukoulis, V. Reddy, S. Pooley, R. D. Feng, Y. Walsh, C. A., and Bader, D. M. (2005). Cytoplasmic LEK1 is a regulator of microtubule function through its interaction with the LIS1 pathway. Proc. Natl. Acad. Sci. USA 102, 8549-8554.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 8549-8554
    • Soukoulis, V.1    Reddy, S.2    Pooley, R.D.3    Feng, Y.4    Walsh, C.A.5    Bader, D.M.6
  • 69
    • 33745614280 scopus 로고    scopus 로고
    • Snares for GLUT4-mechanisms directing vesicular trafficking of GLUT4
    • Stoichevska, V., Grusovin, J., Gough, K. H., Castelli, L. A., and Ward, C. W. (2003). Snares for GLUT4-mechanisms directing vesicular trafficking of GLUT4. Biochem. J. 376, 123-134.
    • (2003) Biochem. J. , vol.376 , pp. 123-134
    • Stoichevska, V.1    Grusovin, J.2    Gough, K.H.3    Castelli, L.A.4    Ward, C.W.5
  • 70
    • 0038825173 scopus 로고    scopus 로고
    • Hrs regulates early endosome fusion by inhibiting formation of an endosomal SNARE complex
    • Sun, W., Yan, Q., Vida, T. A., and Bean, A. J. (2003). Hrs regulates early endosome fusion by inhibiting formation of an endosomal SNARE complex. J. Cell Biol. 162, 125-137.
    • (2003) J. Cell Biol. , vol.162 , pp. 125-137
    • Sun, W.1    Yan, Q.2    Vida, T.A.3    Bean, A.J.4
  • 71
    • 33745605491 scopus 로고    scopus 로고
    • Visualization of slow axonal transport in vivo
    • Terada, S., Nakata, T., Peterson, A. C., and Hirokawa, N. (1998). Visualization of slow axonal transport in vivo. Science 279, 519-526.
    • (1998) Science , vol.279 , pp. 519-526
    • Terada, S.1    Nakata, T.2    Peterson, A.C.3    Hirokawa, N.4
  • 72
    • 0029850677 scopus 로고    scopus 로고
    • Rab11 regulates recycling through the pericentriolar recycling endosome
    • Ullrich, O., Reinsch, S., Urbe, S., Zerial, M., and Parton, R. G. (1996). Rab11 regulates recycling through the pericentriolar recycling endosome. J. Cell Biol. 135, 913-924.
    • (1996) J. Cell Biol. , vol.135 , pp. 913-924
    • Ullrich, O.1    Reinsch, S.2    Urbe, S.3    Zerial, M.4    Parton, R.G.5
  • 73
    • 0034666356 scopus 로고    scopus 로고
    • Regulation of vesicle trafficking in madin-darby canine kidney cells by Rab11a and Rab25
    • Wang, X., Kumar, R., Navarre, J., Casanova, J. E., and Goldenring, J. R. (2000). Regulation of vesicle trafficking in madin-darby canine kidney cells by Rab11a and Rab25. J. Biol. Chem. 275, 29138-29146.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29138-29146
    • Wang, X.1    Kumar, R.2    Navarre, J.3    Casanova, J.E.4    Goldenring, J.R.5
  • 74
    • 0029793644 scopus 로고    scopus 로고
    • Identification of a novel cardiac-specific transcript critical for cardiac myocyte differentiation
    • Wei, Y., Bader, D., and Litvin, J. (1996). Identification of a novel cardiac-specific transcript critical for cardiac myocyte differentiation. Dev. Biol. 122, 2779-2789.
    • (1996) Dev. Biol. , vol.122 , pp. 2779-2789
    • Wei, Y.1    Bader, D.2    Litvin, J.3
  • 75
    • 0345737131 scopus 로고    scopus 로고
    • An immunohistochemical method that distinguishes free from complexed SNAP-25
    • Xiao, J., Xia, Z., Pradhan, A., Zhou, Q., and Liu, Y. (2004). An immunohistochemical method that distinguishes free from complexed SNAP-25. J. Neurosci. Res. 75, 143-151.
    • (2004) J. Neurosci. Res. , vol.75 , pp. 143-151
    • Xiao, J.1    Xia, Z.2    Pradhan, A.3    Zhou, Q.4    Liu, Y.5
  • 76
    • 2442492169 scopus 로고    scopus 로고
    • Ca2+ and N-ethylmaleimide-sensitive factor differentially regulate disassembly of SNARE complexes on early endosomes
    • Yan, Q., Sun, W., McNew, J. A., Vida, T. A., and Bean, A. J. (2004). Ca2+ and N-ethylmaleimide-sensitive factor differentially regulate disassembly of SNARE complexes on early endosomes. J. Biol. Chem. 279, 18270-18276.
    • (2004) J. Biol. Chem. , vol.279 , pp. 18270-18276
    • Yan, Q.1    Sun, W.2    McNew, J.A.3    Vida, T.A.4    Bean, A.J.5
  • 77
    • 13044280807 scopus 로고    scopus 로고
    • Identification of a putative effector protein for rab11 that participates in transferrin recycling
    • Zeng, J. et al. (1999). Identification of a putative effector protein for rab11 that participates in transferrin recycling. Proc. Natl. Acad. Sci. USA 96, 2840-2845.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2840-2845
    • Zeng, J.1


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