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Volumn 65, Issue 15, 2008, Pages 2419-2430

Molecular mechanism underlying the association of Coronin-7 with Golgi membranes

Author keywords

Coronin family; Golgi complex; Membrane binding; Phosphorylation; Src

Indexed keywords

2,3 DIHYDRO 2 OXO 3 (4,5,6,7 TETRAHYDRO 1H INDOL 2 YLMETHYLENE) 1H INDOLE 5 SULFONIC ACID DIMETHYLAMIDE; MEMBRANE PROTEIN; MU ADAPTIN; PROTEIN CORONIN 7; PROTEIN TYROSINE KINASE; SIGNAL PEPTIDE; TYROSINE; UNCLASSIFIED DRUG;

EID: 49249098379     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-008-8278-9     Document Type: Article
Times cited : (15)

References (56)
  • 1
    • 21244477562 scopus 로고    scopus 로고
    • Coronin proteins as multifunctional regulators of the cytoskeleton and membrane trafficking
    • Rybakin, V. and Clemen, C. S. (2005). Coronin proteins as multifunctional regulators of the cytoskeleton and membrane trafficking. Bioessays 27, 625-632.
    • (2005) Bioessays , vol.27 , pp. 625-632
    • Rybakin, V.1    Clemen, C.S.2
  • 2
    • 33746375657 scopus 로고    scopus 로고
    • Coronins: The return of the crown
    • Uetrecht, A. C. and Bear, J. E. (2006). Coronins: the return of the crown. Trends Cell Biol 16, 421-426.
    • (2006) Trends Cell Biol , vol.16 , pp. 421-426
    • Uetrecht, A.C.1    Bear, J.E.2
  • 3
    • 33644798295 scopus 로고    scopus 로고
    • The crystal structure of murine coronin-1: A regulator of actin cytoskeletal dynamics in lymphocytes
    • Appleton, B. A., Wu, P. and Wiesmann, C. (2006). The crystal structure of murine coronin-1: a regulator of actin cytoskeletal dynamics in lymphocytes. Structure 14, 87-96.
    • (2006) Structure , vol.14 , pp. 87-96
    • Appleton, B.A.1    Wu, P.2    Wiesmann, C.3
  • 4
    • 0032702584 scopus 로고    scopus 로고
    • The coronin-like protein POD-1 is required for anterior-posterior axis formation and cellular architecture in the nematode caenorhabditis elegans
    • Rappleye, C. A., Paredez, A. R., Smith, C. W., McDonald, K. L. and Aroian, R. V. (1999). The coronin-like protein POD-1 is required for anterior-posterior axis formation and cellular architecture in the nematode caenorhabditis elegans. Genes Dev 13, 2838-2851.
    • (1999) Genes Dev , vol.13 , pp. 2838-2851
    • Rappleye, C.A.1    Paredez, A.R.2    Smith, C.W.3    McDonald, K.L.4    Aroian, R.V.5
  • 5
    • 0042882289 scopus 로고    scopus 로고
    • Drosophila pod-1 crosslinks both actin and microtubules and controls the targeting of axons
    • Rothenberg, M. E., Rogers, S. L., Vale, R. D., Jan, L. Y. and Jan, Y. N. (2003). Drosophila pod-1 crosslinks both actin and microtubules and controls the targeting of axons. Neuron 39, 779-791.
    • (2003) Neuron , vol.39 , pp. 779-791
    • Rothenberg, M.E.1    Rogers, S.L.2    Vale, R.D.3    Jan, L.Y.4    Jan, Y.N.5
  • 6
    • 4344660477 scopus 로고    scopus 로고
    • Coronin 7, the mammalian POD-1 homologue, localizes to the Golgi apparatus
    • Rybakin, V., Stumpf, M., Schulze, A., Majoul, I. V., Noegel, A. A. and Hasse, A. (2004). Coronin 7, the mammalian POD-1 homologue, localizes to the Golgi apparatus. FEBS Lett 573, 161-167.
    • (2004) FEBS Lett , vol.573 , pp. 161-167
    • Rybakin, V.1    Stumpf, M.2    Schulze, A.3    Majoul, I.V.4    Noegel, A.A.5    Hasse, A.6
  • 7
    • 33750086026 scopus 로고    scopus 로고
    • Crn7 interacts with AP-1 and is required for the maintenance of Golgi morphology and protein export from the Golgi
    • Rybakin, V., Gounko, N. V., Spate, K., Honing, S., Majoul, I. V., Duden, R. and Noegel, A. A. (2006). Crn7 interacts with AP-1 and is required for the maintenance of Golgi morphology and protein export from the Golgi. J Biol Chem 281, 31070-31078.
    • (2006) J Biol Chem , vol.281 , pp. 31070-31078
    • Rybakin, V.1    Gounko, N.V.2    Spate, K.3    Honing, S.4    Majoul, I.V.5    Duden, R.6    Noegel, A.A.7
  • 8
    • 0037073706 scopus 로고    scopus 로고
    • Oligomerization, F-actin interaction, and membrane association of the ubiquitous mammalian coronin 3 are mediated by its carboxyl terminus
    • Spoerl, Z., Stumpf, M., Noegel, A. A. and Hasse, A. (2002). Oligomerization, F-actin interaction, and membrane association of the ubiquitous mammalian coronin 3 are mediated by its carboxyl terminus. J Biol Chem 277, 48858-48867.
    • (2002) J Biol Chem , vol.277 , pp. 48858-48867
    • Spoerl, Z.1    Stumpf, M.2    Noegel, A.A.3    Hasse, A.4
  • 11
    • 37249016585 scopus 로고    scopus 로고
    • Dimeric PKD regulates membrane fission to form transport carriers at the TGN
    • Bossard, C., Bresson, D., Polishchuk, R. S. and Malhotra, V. (2007). Dimeric PKD regulates membrane fission to form transport carriers at the TGN. J Cell Biol 179, 1123-1131.
    • (2007) J Cell Biol , vol.179 , pp. 1123-1131
    • Bossard, C.1    Bresson, D.2    Polishchuk, R.S.3    Malhotra, V.4
  • 12
    • 0033043944 scopus 로고    scopus 로고
    • A 60 kDa plasma membrane protein changes its localization to autophagosome and autolysosome membranes during induction of autophagy in rat hepatoma cell line, H-4-II-E cells
    • Tagawa, Y., Yamamoto, A., Yoshimori, T., Masaki, R., Omori, K., Himeno, M., Inoue, K. and Tashiro, Y. (1999). A 60 kDa plasma membrane protein changes its localization to autophagosome and autolysosome membranes during induction of autophagy in rat hepatoma cell line, H-4-II-E cells. Cell Struct Funct 24, 59-70.
    • (1999) Cell Struct Funct , vol.24 , pp. 59-70
    • Tagawa, Y.1    Yamamoto, A.2    Yoshimori, T.3    Masaki, R.4    Omori, K.5    Himeno, M.6    Inoue, K.7    Tashiro, Y.8
  • 13
    • 0024237306 scopus 로고
    • Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum
    • Fujiwara, T., Oda, K., Yokota, S., Takatsuki, A. and Ikehara, Y. (1988). Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum. J Biol Chem 263, 18545-18552.
    • (1988) J Biol Chem , vol.263 , pp. 18545-18552
    • Fujiwara, T.1    Oda, K.2    Yokota, S.3    Takatsuki, A.4    Ikehara, Y.5
  • 14
    • 0024591235 scopus 로고
    • Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: Evidence for membrane cycling from Golgi to ER
    • Lippincott-Schwartz, J., Yuan, L. C., Bonifacino, J. S. and Klausner, R. D. (1989). Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER. Cell 56, 801-813.
    • (1989) Cell , vol.56 , pp. 801-813
    • Lippincott-Schwartz, J.1    Yuan, L.C.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 15
    • 0021873217 scopus 로고
    • Biosynthesis and modification of Golgi mannosidase II in HeLa and 3T3 cells
    • Moremen, K. W. and Touster, O. (1985). Biosynthesis and modification of Golgi mannosidase II in HeLa and 3T3 cells. J Biol Chem 260, 6654-6662.
    • (1985) J Biol Chem , vol.260 , pp. 6654-6662
    • Moremen, K.W.1    Touster, O.2
  • 16
    • 0022973089 scopus 로고
    • Topology of mannosidase II in rat liver Golgi membranes and release of the catalytic domain by selective proteolysis
    • Moremen, K. W. and Touster, O. (1986). Topology of mannosidase II in rat liver Golgi membranes and release of the catalytic domain by selective proteolysis. J Biol Chem 261, 10945-10951.
    • (1986) J Biol Chem , vol.261 , pp. 10945-10951
    • Moremen, K.W.1    Touster, O.2
  • 17
    • 0343487717 scopus 로고    scopus 로고
    • Characterization of brefeldin A induced vesicular structures containing cycling proteins of the intermediate compartment/cis-Golgi network
    • Fullekrug, J., Sonnichsen, B., Schafer, U., Nguyen Van, P., Soling, H. D. and Mieskes, G. (1997). Characterization of brefeldin A induced vesicular structures containing cycling proteins of the intermediate compartment/cis-Golgi network. FEBS Lett 404, 75-81.
    • (1997) FEBS Lett , vol.404 , pp. 75-81
    • Fullekrug, J.1    Sonnichsen, B.2    Schafer, U.3    Nguyen Van, P.4    Soling, H.D.5    Mieskes, G.6
  • 18
    • 0034458943 scopus 로고    scopus 로고
    • SU6656, a selective src family kinase inhibitor, used to probe growth factor signaling
    • Blake, R. A., Broome, M. A., Liu, X., Wu, J., Gishizky, M., Sun, L. and Courtneidge, S. A. (2000). SU6656, a selective src family kinase inhibitor, used to probe growth factor signaling. Mol Cell Biol 20, 9018-9027.
    • (2000) Mol Cell Biol , vol.20 , pp. 9018-9027
    • Blake, R.A.1    Broome, M.A.2    Liu, X.3    Wu, J.4    Gishizky, M.5    Sun, L.6    Courtneidge, S.A.7
  • 19
    • 0026077454 scopus 로고
    • Structural basis of specific and efficient phosphorylation of peptides derived from p34cdc2 by a pp60src-related protein tyrosine kinase
    • Cheng, H. C., Litwin, C. M., Hwang, D. M. and Wang, J. H. (1991). Structural basis of specific and efficient phosphorylation of peptides derived from p34cdc2 by a pp60src-related protein tyrosine kinase. J Biol Chem 266, 17919-17925.
    • (1991) J Biol Chem , vol.266 , pp. 17919-17925
    • Cheng, H.C.1    Litwin, C.M.2    Hwang, D.M.3    Wang, J.H.4
  • 20
    • 0026612694 scopus 로고
    • A synthetic peptide derived from p34cdc2 is a specific and efficient substrate of src-family tyrosine kinases
    • Cheng, H. C., Nishio, H., Hatase, O., Ralph, S. and Wang, J. H. (1992). A synthetic peptide derived from p34cdc2 is a specific and efficient substrate of src-family tyrosine kinases. J Biol Chem 267, 9248-9256.
    • (1992) J Biol Chem , vol.267 , pp. 9248-9256
    • Cheng, H.C.1    Nishio, H.2    Hatase, O.3    Ralph, S.4    Wang, J.H.5
  • 21
    • 0027997875 scopus 로고
    • Transport into and out of the Golgi complex studied by transfecting cells with cDNAs encoding horseradish peroxidase
    • Connolly, C. N., Futter, C. E., Gibson, A., Hopkins, C. R. and Cutler, D. F. (1994). Transport into and out of the Golgi complex studied by transfecting cells with cDNAs encoding horseradish peroxidase. J Cell Biol 127, 641-652.
    • (1994) J Cell Biol , vol.127 , pp. 641-652
    • Connolly, C.N.1    Futter, C.E.2    Gibson, A.3    Hopkins, C.R.4    Cutler, D.F.5
  • 23
    • 1842556279 scopus 로고    scopus 로고
    • Adaptable adaptors for coated vesicles
    • Robinson, M. S. (2004). Adaptable adaptors for coated vesicles. Trends Cell Biol 14, 167-174.
    • (2004) Trends Cell Biol , vol.14 , pp. 167-174
    • Robinson, M.S.1
  • 24
    • 0035920124 scopus 로고    scopus 로고
    • Ykt6 forms a SNAREcomplex with syntaxin 5, GS28, and Bet1 and participates in a late stage in endoplasmic reticulum-Golgi transport
    • Zhang, T. and Hong, W. (2001). Ykt6 forms a SNAREcomplex with syntaxin 5, GS28, and Bet1 and participates in a late stage in endoplasmic reticulum-Golgi transport. J Biol Chem 276, 27480-27487.
    • (2001) J Biol Chem , vol.276 , pp. 27480-27487
    • Zhang, T.1    Hong, W.2
  • 25
    • 0030863058 scopus 로고    scopus 로고
    • An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signal
    • Hui, N., Nakamura, N., Sonnichsen, B., Shima, D. T., Nilsson, T. and Warren, G. (1997). An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signal. Mol Biol Cell 8, 1777-1787.
    • (1997) Mol Biol Cell , vol.8 , pp. 1777-1787
    • Hui, N.1    Nakamura, N.2    Sonnichsen, B.3    Shima, D.T.4    Nilsson, T.5    Warren, G.6
  • 26
    • 0028028178 scopus 로고
    • Syntaxin 5 regulates endoplasmic reticulum to Golgi transport
    • Dascher, C., Matteson, J. and Balch, W. E. (1994). Syntaxin 5 regulates endoplasmic reticulum to Golgi transport. J Biol Chem 269, 29363-29366.
    • (1994) J Biol Chem , vol.269 , pp. 29363-29366
    • Dascher, C.1    Matteson, J.2    Balch, W.E.3
  • 27
    • 0022187987 scopus 로고
    • Exit of newly synthesized membrane proteins from the trans cisterna of the Golgi complex to the plasma membrane
    • Griffiths, G., Pfeiffer, S., Simons, K. and Matlin, K. (1985). Exit of newly synthesized membrane proteins from the trans cisterna of the Golgi complex to the plasma membrane. J Cell Biol 101, 949-964.
    • (1985) J Cell Biol , vol.101 , pp. 949-964
    • Griffiths, G.1    Pfeiffer, S.2    Simons, K.3    Matlin, K.4
  • 28
    • 0031743659 scopus 로고    scopus 로고
    • Overexpression of the ARF1 exchange factor ARNO inhibits the early secretory pathway and causes the disassembly of the Golgi complex
    • Monier, S., Chardin, P., Robineau, S. and Goud, B. (1998). Overexpression of the ARF1 exchange factor ARNO inhibits the early secretory pathway and causes the disassembly of the Golgi complex. J Cell Sci 111 ( Pt 22), 3427-3436.
    • (1998) J Cell Sci , vol.111 , Issue.PART 22 , pp. 3427-3436
    • Monier, S.1    Chardin, P.2    Robineau, S.3    Goud, B.4
  • 30
    • 0035503293 scopus 로고    scopus 로고
    • Recruitment of protein kinase D to the trans-Golgi network via the first cysteine-rich domain
    • Maeda, Y., Beznoussenko, G. V., Van Lint, J., Mironov, A. A. and Malhotra, V. (2001). Recruitment of protein kinase D to the trans-Golgi network via the first cysteine-rich domain. Embo J 20, 5982-5990.
    • (2001) Embo J , vol.20 , pp. 5982-5990
    • Maeda, Y.1    Beznoussenko, G.V.2    Van Lint, J.3    Mironov, A.A.4    Malhotra, V.5
  • 31
    • 0035830496 scopus 로고    scopus 로고
    • Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network
    • Liljedahl, M., Maeda, Y., Colanzi, A., Ayala, I., Van Lint, J. and Malhotra, V. (2001). Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network. Cell 104, 409-420.
    • (2001) Cell , vol.104 , pp. 409-420
    • Liljedahl, M.1    Maeda, Y.2    Colanzi, A.3    Ayala, I.4    Van Lint, J.5    Malhotra, V.6
  • 32
    • 0033538345 scopus 로고    scopus 로고
    • Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D
    • Jamora, C., Yamanouye, N., Van Lint, J., Laudenslager, J., Vandenheede, J. R., Faulkner, D. J. and Malhotra, V. (1999). Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D. Cell 98, 59-68.
    • (1999) Cell , vol.98 , pp. 59-68
    • Jamora, C.1    Yamanouye, N.2    Van Lint, J.3    Laudenslager, J.4    Vandenheede, J.R.5    Faulkner, D.J.6    Malhotra, V.7
  • 34
    • 0037059451 scopus 로고    scopus 로고
    • Role of diacylglycerol in PKD recruitment to the TGN and protein transport to the plasma membrane
    • Baron, C. L. and Malhotra, V. (2002). Role of diacylglycerol in PKD recruitment to the TGN and protein transport to the plasma membrane. Science 295, 325-328.
    • (2002) Science , vol.295 , pp. 325-328
    • Baron, C.L.1    Malhotra, V.2
  • 35
    • 15544389207 scopus 로고    scopus 로고
    • Novel insights into c-Src
    • Alper, O. and Bowden, E. T. (2005). Novel insights into c-Src. Curr Pharm Des 11, 1119-1130.
    • (2005) Curr Pharm Des , vol.11 , pp. 1119-1130
    • Alper, O.1    Bowden, E.T.2
  • 36
    • 13544256790 scopus 로고    scopus 로고
    • Src protein-tyrosine kinase structure and regulation
    • Roskoski, R., Jr. (2004). Src protein-tyrosine kinase structure and regulation. Biochem Biophys Res Commun 324, 1155-1164.
    • (2004) Biochem Biophys Res Commun , vol.324 , pp. 1155-1164
    • Roskoski Jr., R.1
  • 37
    • 1642565264 scopus 로고    scopus 로고
    • Osteopontin induces AP-1-mediated secretion of urokinase-type plasminogen activator through c-Src-dependent epidermal growth factor receptor transactivation in breast cancer cells
    • Das, R., Mahabeleshwar, G. H. and Kundu, G. C. (2004). Osteopontin induces AP-1-mediated secretion of urokinase-type plasminogen activator through c-Src-dependent epidermal growth factor receptor transactivation in breast cancer cells. J Biol Chem 279, 11051-11064.
    • (2004) J Biol Chem , vol.279 , pp. 11051-11064
    • Das, R.1    Mahabeleshwar, G.H.2    Kundu, G.C.3
  • 38
    • 0034720481 scopus 로고    scopus 로고
    • Regulation of collagenolytic protease secretion through c-Src in osteoclasts
    • Furuyama, N. and Fujisawa, Y. (2000). Regulation of collagenolytic protease secretion through c-Src in osteoclasts. Biochem Biophys Res Commun 272, 116-124.
    • (2000) Biochem Biophys Res Commun , vol.272 , pp. 116-124
    • Furuyama, N.1    Fujisawa, Y.2
  • 39
    • 33749847235 scopus 로고    scopus 로고
    • Serotonin stimulates GnRH secretion through the c-Src-PLC gamma1 pathway in GT1-7 hypothalamic cells
    • Kim, H. S., Yumkham, S., Choi, J. H., Son, G. H., Kim, K., Ryu, S. H. and Suh, P. G. (2006). Serotonin stimulates GnRH secretion through the c-Src-PLC gamma1 pathway in GT1-7 hypothalamic cells. J Endocrinol 190, 581-591.
    • (2006) J Endocrinol , vol.190 , pp. 581-591
    • Kim, H.S.1    Yumkham, S.2    Choi, J.H.3    Son, G.H.4    Kim, K.5    Ryu, S.H.6    Suh, P.G.7
  • 40
    • 27944487579 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced c-Src expression plays a role in nitric oxide and TNFalpha secretion in macrophages
    • Leu, T. H., Charoenfuprasert, S., Yen, C. K., Fan, C. W. and Maa, M. C. (2006). Lipopolysaccharide-induced c-Src expression plays a role in nitric oxide and TNFalpha secretion in macrophages. Mol Immunol 43, 308-316.
    • (2006) Mol Immunol , vol.43 , pp. 308-316
    • Leu, T.H.1    Charoenfuprasert, S.2    Yen, C.K.3    Fan, C.W.4    Maa, M.C.5
  • 41
    • 33748995139 scopus 로고    scopus 로고
    • Ionizing Radiation Enhances Matrix Metalloproteinase-2 Secretion and Invasion of GliomaCells through Src/Epidermal Growth Factor Receptor-Mediated p38/Akt and Phosphatidylinositol 3-Kinase/Akt Signaling Pathways
    • Park, C. M., Park, M. J., Kwak, H. J., Lee, H. C., Kim, M. S., Lee, S. H., Park, I. C., Rhee, C. H. and Hong, S. I. (2006). Ionizing Radiation Enhances Matrix Metalloproteinase-2 Secretion and Invasion of GliomaCells through Src/Epidermal Growth Factor Receptor-Mediated p38/Akt and Phosphatidylinositol 3-Kinase/Akt Signaling Pathways. Cancer Res 66, 8511-8519.
    • (2006) Cancer Res , vol.66 , pp. 8511-8519
    • Park, C.M.1    Park, M.J.2    Kwak, H.J.3    Lee, H.C.4    Kim, M.S.5    Lee, S.H.6    Park, I.C.7    Rhee, C.H.8    Hong, S.I.9
  • 42
    • 0036451583 scopus 로고    scopus 로고
    • Src/ERK but not phospholipase D is involved in keratinocyte growth factor-stimulated secretion of matrix metalloprotease-9 and urokinase-type plasminogen activator in SNU-16 human stomach cancer cell
    • Shin, E. Y., Ma, E. K., Kim, C. K., Kwak, S. J. and Kim, E. G. (2002). Src/ERK but not phospholipase D is involved in keratinocyte growth factor-stimulated secretion of matrix metalloprotease-9 and urokinase-type plasminogen activator in SNU-16 human stomach cancer cell. J Cancer Res Clin Oncol 128, 596-602.
    • (2002) J Cancer Res Clin Oncol , vol.128 , pp. 596-602
    • Shin, E.Y.1    Ma, E.K.2    Kim, C.K.3    Kwak, S.J.4    Kim, E.G.5
  • 43
    • 1942424869 scopus 로고    scopus 로고
    • Salivary phospholipid secretion in response to beta-adrenergic stimulation is mediated by Src kinase-dependent epidermal growth factor receptor transactivation
    • Slomiany, B. L. and Slomiany, A. (2004). Salivary phospholipid secretion in response to beta-adrenergic stimulation is mediated by Src kinase-dependent epidermal growth factor receptor transactivation. Biochem Biophys Res Commun 318, 247-252.
    • (2004) Biochem Biophys Res Commun , vol.318 , pp. 247-252
    • Slomiany, B.L.1    Slomiany, A.2
  • 44
    • 21344441234 scopus 로고    scopus 로고
    • Gastric mucin secretion in response to beta-adrenergic G protein-coupled receptor activation is mediated by SRC kinase-dependent epidermal growth factor receptor transactivation
    • Slomiany, B. L. and Slomiany, A. (2005). Gastric mucin secretion in response to beta-adrenergic G protein-coupled receptor activation is mediated by SRC kinase-dependent epidermal growth factor receptor transactivation. J Physiol Pharmacol 56, 247-258.
    • (2005) J Physiol Pharmacol , vol.56 , pp. 247-258
    • Slomiany, B.L.1    Slomiany, A.2
  • 45
    • 33748423394 scopus 로고    scopus 로고
    • Involvement of JAK2 and Src kinase tyrosine phosphorylation in human growth hormone-stimulated increases in cytosolic free Ca2+ and insulin secretion
    • Zhang, F., Zhang, Q., Tengholm, A. and Sjoholm, A. (2006). Involvement of JAK2 and Src kinase tyrosine phosphorylation in human growth hormone-stimulated increases in cytosolic free Ca2+ and insulin secretion. Am J Physiol Cell Physiol 291, C466-C475.
    • (2006) Am J Physiol Cell Physiol , vol.291
    • Zhang, F.1    Zhang, Q.2    Tengholm, A.3    Sjoholm, A.4
  • 46
    • 0036181534 scopus 로고    scopus 로고
    • Molecular complexes that contain both c-Cbl and c-Src associate with Golgi membranes
    • Bard, F., Patel, U., Levy, J. B., Jurdic, P., Horne, W. C. and Baron, R. (2002). Molecular complexes that contain both c-Cbl and c-Src associate with Golgi membranes. Eur J Cell Biol 81, 26-35.
    • (2002) Eur J Cell Biol , vol.81 , pp. 26-35
    • Bard, F.1    Patel, U.2    Levy, J.B.3    Jurdic, P.4    Horne, W.C.5    Baron, R.6
  • 47
    • 0025605786 scopus 로고
    • Immunolocalization of the cellular src protein in interphase and mitotic NIH c-src overexpresser cells
    • David-Pfeuty, T. and Nouvian-Dooghe, Y. (1990). Immunolocalization of the cellular src protein in interphase and mitotic NIH c-src overexpresser cells. J Cell Biol 111, 3097-3116.
    • (1990) J Cell Biol , vol.111 , pp. 3097-3116
    • David-Pfeuty, T.1    Nouvian-Dooghe, Y.2
  • 49
    • 0344012542 scopus 로고    scopus 로고
    • Src regulates Golgi structure and KDEL receptor-dependent retrograde transport to the endoplasmic reticulum
    • Bard, F., Mazelin, L., Pechoux-Longin, C., Malhotra, V. and Jurdic, P. (2003). Src regulates Golgi structure and KDEL receptor-dependent retrograde transport to the endoplasmic reticulum. J Biol Chem 278, 46601-46606.
    • (2003) J Biol Chem , vol.278 , pp. 46601-46606
    • Bard, F.1    Mazelin, L.2    Pechoux-Longin, C.3    Malhotra, V.4    Jurdic, P.5
  • 50
    • 0034651872 scopus 로고    scopus 로고
    • An EGF receptor/Ral-GTPase signaling cascade regulates c-Src activity and substrate specificity
    • Goi, T., Shipitsin, M., Lu, Z., Foster, D. A., Klinz, S. G. and Feig, L. A. (2000). An EGF receptor/Ral-GTPase signaling cascade regulates c-Src activity and substrate specificity. Embo J 19, 623-630.
    • (2000) Embo J , vol.19 , pp. 623-630
    • Goi, T.1    Shipitsin, M.2    Lu, Z.3    Foster, D.A.4    Klinz, S.G.5    Feig, L.A.6
  • 51
    • 0033546315 scopus 로고    scopus 로고
    • ErbB receptor-induced activation of stat transcription factors is mediated by Src tyrosine kinases
    • Olayioye, M. A., Beuvink, I., Horsch, K., Daly, J. M. and Hynes, N. E. (1999). ErbB receptor-induced activation of stat transcription factors is mediated by Src tyrosine kinases. J Biol Chem 274, 17209-17218.
    • (1999) J Biol Chem , vol.274 , pp. 17209-17218
    • Olayioye, M.A.1    Beuvink, I.2    Horsch, K.3    Daly, J.M.4    Hynes, N.E.5
  • 52
    • 0029904262 scopus 로고    scopus 로고
    • Requirement for c-Src catalytic activity and the SH3 domain in platelet-derived growth factor BB and epidermal growth factor mitogenic signaling
    • Broome, M. A. and Hunter, T. (1996). Requirement for c-Src catalytic activity and the SH3 domain in platelet-derived growth factor BB and epidermal growth factor mitogenic signaling. J Biol Chem 271, 16798-16806.
    • (1996) J Biol Chem , vol.271 , pp. 16798-16806
    • Broome, M.A.1    Hunter, T.2
  • 53
    • 0028795721 scopus 로고
    • DNA synthesis induced by some but not all growth factors requires Src family protein tyrosine kinases
    • Roche, S., Koegl, M., Barone, M. V., Roussel, M. F. and Courtneidge, S. A. (1995). DNA synthesis induced by some but not all growth factors requires Src family protein tyrosine kinases. Mol Cell Biol 15, 1102-1109.
    • (1995) Mol Cell Biol , vol.15 , pp. 1102-1109
    • Roche, S.1    Koegl, M.2    Barone, M.V.3    Roussel, M.F.4    Courtneidge, S.A.5
  • 54
    • 0027172209 scopus 로고
    • The Src family tyrosine kinases are required for platelet-derived growth factor-mediated signal transduction in NIH 3T3 cells
    • Twamley-Stein, G. M., Pepperkok, R., Ansorge, W. and Courtneidge, S. A. (1993). The Src family tyrosine kinases are required for platelet-derived growth factor-mediated signal transduction in NIH 3T3 cells. Proc Natl Acad Sci U S A 90, 7696-7700.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 7696-7700
    • Twamley-Stein, G.M.1    Pepperkok, R.2    Ansorge, W.3    Courtneidge, S.A.4
  • 55
    • 0025172811 scopus 로고
    • Association between the PDGF receptor and members of the src family of tyrosine kinases
    • Kypta, R. M., Goldberg, Y., Ulug, E. T. and Courtneidge, S. A. (1990). Association between the PDGF receptor and members of the src family of tyrosine kinases. Cell 62, 481-492.
    • (1990) Cell , vol.62 , pp. 481-492
    • Kypta, R.M.1    Goldberg, Y.2    Ulug, E.T.3    Courtneidge, S.A.4
  • 56
    • 0030921043 scopus 로고    scopus 로고
    • Sequence and overexpression of GPP130/GIMPc: Evidence for saturable pH-sensitive targeting of a type II early Golgi membrane protein
    • Linstedt, A. D., Mehta, A., Suhan, J., Reggio, H. and Hauri, H. P. (1997). Sequence and overexpression of GPP130/GIMPc: evidence for saturable pH-sensitive targeting of a type II early Golgi membrane protein. Mol Biol Cell 8, 1073-1087.
    • (1997) Mol Biol Cell , vol.8 , pp. 1073-1087
    • Linstedt, A.D.1    Mehta, A.2    Suhan, J.3    Reggio, H.4    Hauri, H.P.5


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