메뉴 건너뛰기




Volumn 124, Issue 2, 2011, Pages 171-180

Signalling to and from the secretory pathway

Author keywords

Endoplasmic reticulum exit sites; Golgi; Signal transduction

Indexed keywords

CD135 ANTIGEN; CELL PROTEIN; CHAPERONE; COAT PROTEIN COMPLEX II; CYCLIC AMP DEPENDENT PROTEIN KINASE; LIPID; MAMMALIAN TARGET OF RAPAMYCIN; MATRIX PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE P38; PHOSPHATIDYLINOSITOL 4 PHOSPHATE; PROTEIN GM130; PROTEIN KINASE D; PROTEIN TYROSINE KINASE; RAS PROTEIN; RECEPTOR PROTEIN; RECEPTOR PROTEIN KDEL; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 79251585226     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.076455     Document Type: Note
Times cited : (115)

References (97)
  • 2
    • 33745485316 scopus 로고    scopus 로고
    • The ER-Golgi intermediate compartment (ERGIC): In search of its identity and function
    • Appenzeller-Herzog, C. and Hauri, H. P. (2006). The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function. J. Cell Sci. 119, 2173-2183.
    • (2006) J. Cell Sci. , vol.119 , pp. 2173-2183
    • Appenzeller-Herzog, C.1    Hauri, H.P.2
  • 3
    • 0034680777 scopus 로고    scopus 로고
    • Kinase signaling initiates coat complex II (COPII) recruitment and export from the mammalian endoplasmic reticulum
    • Arido, R. M. and Balch, W. E. (2000). Kinase signaling initiates coat complex II (COPII) recruitment and export from the mammalian endoplasmic reticulum. J. Biol. Chem. 275, 35673-35676.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35673-35676
    • Arido, R.M.1    Balch, W.E.2
  • 7
    • 33750332048 scopus 로고    scopus 로고
    • Golgi structural stability and biogenesis depend on associated PKA activity
    • Bejarano, E., Cabrera, M., Vega, L., Hidalgo, J. and Velasco, A. (2006). Golgi structural stability and biogenesis depend on associated PKA activity. J. Cell Sci. 119, 3764-3775.
    • (2006) J. Cell Sci. , vol.119 , pp. 3764-3775
    • Bejarano, E.1    Cabrera, M.2    Vega, L.3    Hidalgo, J.4    Velasco, A.5
  • 12
    • 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
  • 13
    • 53049108504 scopus 로고    scopus 로고
    • Scyl1, mutated in a recessive form of spinocerebellar neurodegeneration, regulates COPI-mediated retrograde traffic
    • Burman, J. L., Bourbonniere, L., Philie, J., Stroh, T., Dejgaard, S. Y., Presley, J. F. and McPherson, P. S. (2008). Scyl1, mutated in a recessive form of spinocerebellar neurodegeneration, regulates COPI-mediated retrograde traffic. J. Biol. Chem. 283, 22774-22786.
    • (2008) J. Biol. Chem. , vol.283 , pp. 22774-22786
    • Burman, J.L.1    Bourbonniere, L.2    Philie, J.3    Stroh, T.4    Dejgaard, S.Y.5    Presley, J.F.6    McPherson, P.S.7
  • 14
    • 0141429975 scopus 로고    scopus 로고
    • The retrieval function of the KDEL receptor requires PKA phosphorylation of its Cterminus
    • Cabrera, M., Muniz, M., Hidalgo, J., Vega, L., Martin, M. E. and Velasco, A. (2003). The retrieval function of the KDEL receptor requires PKA phosphorylation of its Cterminus. Mol. Biol. Cell 14, 4114-4125.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4114-4125
    • Cabrera, M.1    Muniz, M.2    Hidalgo, J.3    Vega, L.4    Martin, M.E.5    Velasco, A.6
  • 15
    • 71749088618 scopus 로고    scopus 로고
    • Calnexin phosphorylation attenuates the release of partially misfolded alpha1-antitrypsin to the secretory pathway
    • Cameron, P. H., Chevet, E., Pluquet, O., Thomas, D. Y. and Bergeron, J. J. (2009). Calnexin phosphorylation attenuates the release of partially misfolded alpha1-antitrypsin to the secretory pathway. J. Biol. Chem. 284, 34570-34579.
    • (2009) J. Biol. Chem. , vol.284 , pp. 34570-34579
    • Cameron, P.H.1    Chevet, E.2    Pluquet, O.3    Thomas, D.Y.4    Bergeron, J.J.5
  • 16
    • 61749103498 scopus 로고    scopus 로고
    • Ras subcellular localization defines extracellular signal-regulated kinase 1 and 2 substrate specificity through distinct utilization of scaffold proteins
    • Casar, B., Arozarena, I., Sanz-Moreno, V., Pinto, A., Agudo-Ibáñez, L., Marais, R., Lewis, R. E., Berciano, M. T. and Crespo, P. (2009). Ras subcellular localization defines extracellular signal-regulated kinase 1 and 2 substrate specificity through distinct utilization of scaffold proteins. Mol. Cell. Biol. 29, 1338-1353.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1338-1353
    • Casar, B.1    Arozarena, I.2    Sanz-Moreno, V.3    Pinto, A.4    Agudo-Ibáñez, L.5    Marais, R.6    Lewis, R.E.7    Berciano, M.T.8    Crespo, P.9
  • 20
    • 34548024889 scopus 로고    scopus 로고
    • Mitosis controls the Golgi and the Golgi controls mitosis
    • Colanzi, A. and Corda, D. (2007). Mitosis controls the Golgi and the Golgi controls mitosis. Curr. Opin. Cell Biol. 19, 386-393.
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 386-393
    • Colanzi, A.1    Corda, D.2
  • 24
    • 0027179841 scopus 로고
    • Receptor and protein kinase C-mediated regulation of ARF binding to the Golgi complex
    • De Matteis, M. A., Santini, G., Kahn, R. A., Di Tullio, G. and Luini, A. (1993). Receptor and protein kinase C-mediated regulation of ARF binding to the Golgi complex. Nature 364, 818-821.
    • (1993) Nature , vol.364 , pp. 818-821
    • De Matteis, M.A.1    Santini, G.2    Kahn, R.A.3    Di Tullio, G.4    Luini, A.5
  • 25
    • 0041737795 scopus 로고    scopus 로고
    • Signal transduction: Life on Mars, cellularly speaking
    • Di Fiore, P. P. (2003). Signal transduction: life on Mars, cellularly speaking. Nature 424, 624-625.
    • (2003) Nature , vol.424 , pp. 624-625
    • Di Fiore, P.P.1
  • 27
    • 0346422440 scopus 로고    scopus 로고
    • FKBP12-rapamycin-associated protein or mammalian target of rapamycin (FRAP/mTOR) localization in the endoplasmic reticulum and the Golgi apparatus
    • Drenan, R. M., Liu, X., Bertram, P. G. and Zheng, X. F. (2004). FKBP12-rapamycin-associated protein or mammalian target of rapamycin (FRAP/mTOR) localization in the endoplasmic reticulum and the Golgi apparatus. J. Biol. Chem. 279, 772-778.
    • (2004) J. Biol. Chem. , vol.279 , pp. 772-778
    • Drenan, R.M.1    Liu, X.2    Bertram, P.G.3    Zheng, X.F.4
  • 28
    • 1542298251 scopus 로고    scopus 로고
    • Regulation of a COPII component by cytosolic O-glycosylation during mitosis
    • Dudognon, P., Maeder-Garavaglia, C., Carpentier, J. L. and Paccaud, J. P. (2004). Regulation of a COPII component by cytosolic O-glycosylation during mitosis. FEBS Lett. 561, 44-50.
    • (2004) FEBS Lett. , vol.561 , pp. 44-50
    • Dudognon, P.1    Maeder-Garavaglia, C.2    Carpentier, J.L.3    Paccaud, J.P.4
  • 29
    • 0036569782 scopus 로고    scopus 로고
    • Ecdysone triggers the expression of Golgi genes in Drosophila imaginal discs via broad-complex
    • Dunne, J. C., Kondylis, V. and Rabouille, C. (2002). Ecdysone triggers the expression of Golgi genes in Drosophila imaginal discs via broad-complex. Dev. Biol. 245, 172-186.
    • (2002) Dev. Biol. , vol.245 , pp. 172-186
    • Dunne, J.C.1    Kondylis, V.2    Rabouille, C.3
  • 30
    • 2342432240 scopus 로고    scopus 로고
    • Cdc42-the centre of polarity
    • Etienne-Manneville, S. (2004). Cdc42-the centre of polarity. J. Cell Sci. 117, 1291-1300.
    • (2004) J. Cell Sci. , vol.117 , pp. 1291-1300
    • Etienne-Manneville, S.1
  • 31
    • 49149100705 scopus 로고    scopus 로고
    • Adaptation of endoplasmic reticulum exit sites to acute and chronic increases in cargo load
    • Farhan, H., Weiss, M., Tani, K., Kaufman, R. J. and Hauri, H. P. (2008). Adaptation of endoplasmic reticulum exit sites to acute and chronic increases in cargo load. EMBO. J. 27, 2043-2054.
    • (2008) EMBO. J. , vol.27 , pp. 2043-2054
    • Farhan, H.1    Weiss, M.2    Tani, K.3    Kaufman, R.J.4    Hauri, H.P.5
  • 33
    • 35348910763 scopus 로고    scopus 로고
    • Growth control of Golgi phosphoinositides by reciprocal localization of sac1 lipid phosphatase and pik1 4-kinase
    • Faulhammer, F., Kanjilal-Kolar, S., Knödler, A,, Lo, J., Lee, Y., Konrad, G., and Mayinger, P. (2007). Growth control of Golgi phosphoinositides by reciprocal localization of sac1 lipid phosphatase and pik1 4-kinase. Traffic 8, 1554-1567.
    • (2007) Traffic , vol.8 , pp. 1554-1567
    • Faulhammer, F.1    Kanjilal-Kolar, S.2    Knödler, A.3    Lo, J.4    Lee, Y.5    Konrad, G.6    Mayinger, P.7
  • 35
    • 77951194603 scopus 로고    scopus 로고
    • CCM3/PDCD10 stabilizes GCKIII proteins to promote Golgi assembly and cell orientation
    • Fidalgo, M., Fraile, M., Pires, A., Force, T., Pombo, C. and Zalvide, J. (2010). CCM3/PDCD10 stabilizes GCKIII proteins to promote Golgi assembly and cell orientation. J. Cell Sci. 123, 1274-1284.
    • (2010) J. Cell Sci. , vol.123 , pp. 1274-1284
    • Fidalgo, M.1    Fraile, M.2    Pires, A.3    Force, T.4    Pombo, C.5    Zalvide, J.6
  • 38
    • 33745617044 scopus 로고    scopus 로고
    • COPII-Golgi protein interactions regulate COPII coat assembly and Golgi size
    • Guo, Y. and Linstedt, A. D. (2006). COPII-Golgi protein interactions regulate COPII coat assembly and Golgi size. J. Cell Biol. 174, 53-63.
    • (2006) J. Cell Biol. , vol.174 , pp. 53-63
    • Guo, Y.1    Linstedt, A.D.2
  • 39
    • 0037542854 scopus 로고    scopus 로고
    • Ras proteins: Different signals from different locations
    • Hancock, J. F. (2003). Ras proteins: different signals from different locations. Nat. Rev. Mol. Cell Biol. 4, 373-384.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 373-384
    • Hancock, J.F.1
  • 40
    • 26944446652 scopus 로고    scopus 로고
    • Protein kinase D regulates vesicular transport by phosphorylating and activating phosphatidylinositol-4 kinase IIIbeta at the Golgi complex
    • Hausser, A., Storz, P., Märtens, S., Link, G., Toker, A. and Pfizenmaier, K. (2005). Protein kinase D regulates vesicular transport by phosphorylating and activating phosphatidylinositol-4 kinase IIIbeta at the Golgi complex. Nat. Cell Biol. 7, 880-886.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 880-886
    • Hausser, A.1    Storz, P.2    Märtens, S.3    Link, G.4    Toker, A.5    Pfizenmaier, K.6
  • 42
    • 0344663968 scopus 로고    scopus 로고
    • Phosphorylation-dependent binding of 14-3-3 to the polarity protein Par3 regulates cell polarity in mammalian epithelia
    • Hurd, T. W., Fan, S., Liu, C. J., Kweon, H. K., Hakansson, K. and Margolis, B. (2003). Phosphorylation-dependent binding of 14-3-3 to the polarity protein Par3 regulates cell polarity in mammalian epithelia. Curr. Biol. 13, 2082-2090.
    • (2003) Curr. Biol. , vol.13 , pp. 2082-2090
    • Hurd, T.W.1    Fan, S.2    Liu, C.J.3    Kweon, H.K.4    Hakansson, K.5    Margolis, B.6
  • 43
    • 57349165449 scopus 로고    scopus 로고
    • Drosophila Sec16 mediates the biogenesis of tER sites upstream of Sar1 through an arginine-rich motif
    • Ivan, V, de Voer, G., Xanthakis, D., Spoorendonk, K. M., Kondylis, V. and Rabouille, C. (2008). Drosophila Sec16 mediates the biogenesis of tER sites upstream of Sar1 through an arginine-rich motif. Mol. Biol. Cell 19, 4352-4365.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4352-4365
    • Ivan, V.1    De Voer, G.2    Xanthakis, D.3    Spoorendonk, K.M.4    Kondylis, V.5    Rabouille, C.6
  • 44
    • 0037385313 scopus 로고    scopus 로고
    • Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-1
    • Iwakoshi, N. N., Lee, A. H., Vallabhajosyula, P., Otipoby, K. L., Rajewsky, K. and Glimcher, L. H. (2003). Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-1. Nat. Immunol. 4, 321-329.
    • (2003) Nat. Immunol. , vol.4 , pp. 321-329
    • Iwakoshi, N.N.1    Lee, A.H.2    Vallabhajosyula, P.3    Otipoby, K.L.4    Rajewsky, K.5    Glimcher, L.H.6
  • 45
    • 64849104544 scopus 로고    scopus 로고
    • Mechanisms of transport through the Golgi complex
    • Jackson, C. L. (2009). Mechanisms of transport through the Golgi complex. J. Cell Sci. 122, 443-452.
    • (2009) J. Cell Sci. , vol.122 , pp. 443-452
    • Jackson, C.L.1
  • 46
    • 1542328956 scopus 로고    scopus 로고
    • A mitochondrial protein, Bit1, mediates apoptosis regulated by integrins and Groucho/TLE corepressors
    • Jan, Y., Matter, M., Pai, J. T., Chen, Y. L., Pilch, J., Komatsu, M., Ong, E., Fukuda, M., and Ruoslahti, E. (2004). A mitochondrial protein, Bit1, mediates apoptosis regulated by integrins and Groucho/TLE corepressors. Cell 116, 751-762.
    • (2004) Cell , vol.116 , pp. 751-762
    • Jan, Y.1    Matter, M.2    Pai, J.T.3    Chen, Y.L.4    Pilch, J.5    Komatsu, M.6    Ong, E.7    Fukuda, M.8    Ruoslahti, E.9
  • 47
    • 73549119237 scopus 로고    scopus 로고
    • Regulation of G-protein signaling by RKTG via sequestration of the G betagamma subunit to the Golgi apparatus
    • Jiang, Y., Xie, X., Zhang, Y., Luo, X., Wang, X., Fan, F., Zheng, D., Wang, Z. and Chen, Y. (2010). Regulation of G-protein signaling by RKTG via sequestration of the G betagamma subunit to the Golgi apparatus. Mol. Cell. Biol. 30, 78-90.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 78-90
    • Jiang, Y.1    Xie, X.2    Zhang, Y.3    Luo, X.4    Wang, X.5    Fan, F.6    Zheng, D.7    Wang, Z.8    Chen, Y.9
  • 49
    • 4344700328 scopus 로고    scopus 로고
    • Cdc2 kinase-dependent disassembly of endoplasmic reticulum (ER) exit sites inhibits ER-to-golgi vesicular transport during mitosis
    • Kano, F., Tanaka, A. R., Yamauchi, S., Kondo, H. and Murata, M. (2004). Cdc2 kinase-dependent disassembly of endoplasmic reticulum (ER) exit sites inhibits ER-to-golgi vesicular transport during mitosis. Mol. Biol. Cell 15, 4289-4298.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4289-4298
    • Kano, F.1    Tanaka, A.R.2    Yamauchi, S.3    Kondo, H.4    Murata, M.5
  • 51
    • 64149084265 scopus 로고    scopus 로고
    • GM130-dependent control of Cdc42 activity at the Golgi regulates centrosome organization
    • Kodani, A., Kristensen, I., Huang, L. and Sütterlin, C. (2009). GM130-dependent control of Cdc42 activity at the Golgi regulates centrosome organization. Mol. Biol. Cell 20, 1192-1200.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1192-1200
    • Kodani, A.1    Kristensen, I.2    Huang, L.3    Sütterlin, C.4
  • 52
    • 27644575157 scopus 로고    scopus 로고
    • Coordinating ERK/MAPK signalling through scaffolds and inhibitors
    • Kolch, W. (2005). Coordinating ERK/MAPK signalling through scaffolds and inhibitors. Nat. Rev. Mol. Cell Biol. 6, 827-837.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 827-837
    • Kolch, W.1
  • 53
    • 70450223327 scopus 로고    scopus 로고
    • The Golgi apparatus: Lessons from Drosophila
    • Kondylis, V. and Rabouille, C. (2009). The Golgi apparatus: lessons from Drosophila. FEBS Lett. 583, 3827-3838.
    • (2009) FEBS Lett. , vol.583 , pp. 3827-3838
    • Kondylis, V.1    Rabouille, C.2
  • 54
    • 34249316147 scopus 로고    scopus 로고
    • The golgi comprises a paired stack that is separated at G2 by modulation of the actin cytoskeleton through Abi and Scar/WAVE
    • Kondylis, V., van Nispen tot Pannerden, H. E., Herpers, B., Friggi-Grelin, F. and Rabouille, C. (2007). The golgi comprises a paired stack that is separated at G2 by modulation of the actin cytoskeleton through Abi and Scar/WAVE. Dev. Cell 12, 901-915.
    • (2007) Dev. Cell , vol.12 , pp. 901-915
    • Kondylis, V.1    Van Nispen Tot Pannerden, H.E.2    Herpers, B.3    Friggi-Grelin, F.4    Rabouille, C.5
  • 57
    • 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
  • 58
    • 33947145667 scopus 로고    scopus 로고
    • Endoplasmic reticulum and Golgi localization sequences for mammalian target of rapamycin
    • Liu, X. and Zheng, X. F. (2007). Endoplasmic reticulum and Golgi localization sequences for mammalian target of rapamycin. Mol. Biol. Cell 18, 1073-1082.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1073-1082
    • Liu, X.1    Zheng, X.F.2
  • 59
    • 33644856168 scopus 로고    scopus 로고
    • Distinct utilization of effectors and biological outcomes resulting from site-specific Ras activation: Ras functions in lipid rafts and Golgi complex are dispensable for proliferation and transformation
    • Matallanas, D., Sanz-Moreno, V., Arozarena, I., Calvo, F., Agudo-Ibáñez, L., Santos, E., Berciano, M. T. and Crespo, P. (2006). Distinct utilization of effectors and biological outcomes resulting from site-specific Ras activation: Ras functions in lipid rafts and Golgi complex are dispensable for proliferation and transformation. Mol. Cell. Biol. 26, 100-116.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 100-116
    • Matallanas, D.1    Sanz-Moreno, V.2    Arozarena, I.3    Calvo, F.4    Agudo- Ibáñez, L.5    Santos, E.6    Berciano, M.T.7    Crespo, P.8
  • 60
    • 18344405156 scopus 로고    scopus 로고
    • COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes
    • Matsuoka, K., Orci, L., Amherdt, M., Bednarek, S. Y., Hamamoto, S., Schekman, R. and Yeung, T. (1998). COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes. Cell 93, 263-275.
    • (1998) Cell , vol.93 , pp. 263-275
    • Matsuoka, K.1    Orci, L.2    Amherdt, M.3    Bednarek, S.Y.4    Hamamoto, S.5    Schekman, R.6    Yeung, T.7
  • 61
    • 71849112960 scopus 로고    scopus 로고
    • PKA-mediated Golgi remodeling during cAMP signal transmission
    • Mavillard, F., Hidalgo, J., Megias, D., Levitsky, K. L. and Velasco, A. (2010). PKA-mediated Golgi remodeling during cAMP signal transmission. Traffic 11, 90-109.
    • (2010) Traffic , vol.11 , pp. 90-109
    • Mavillard, F.1    Hidalgo, J.2    Megias, D.3    Levitsky, K.L.4    Velasco, A.5
  • 62
    • 0034614647 scopus 로고    scopus 로고
    • The road taken: Past and future foundations of membrane traffic
    • Mellman, I. and Warren, G. (2000). The road taken: past and future foundations of membrane traffic. Cell 100, 99-112.
    • (2000) Cell , vol.100 , pp. 99-112
    • Mellman, I.1    Warren, G.2
  • 64
    • 0031474609 scopus 로고    scopus 로고
    • Protein kinase A activity is required for the budding of constitutive transport vesicles from the trans-Golgi network
    • Muniz, M., Martin, M. E., Hidalgo, J. and Velasco, A. (1997). Protein kinase A activity is required for the budding of constitutive transport vesicles from the trans-Golgi network. Proc. Natl. Acad. Sci. USA 94, 14461-14466.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14461-14466
    • Muniz, M.1    Martin, M.E.2    Hidalgo, J.3    Velasco, A.4
  • 66
    • 26244442308 scopus 로고    scopus 로고
    • PCTAIRE protein kinases interact directly with the COPII complex and modulate secretory cargo transport
    • Palmer, K. J., Konkel, J. E. and Stephens, D. J. (2005). PCTAIRE protein kinases interact directly with the COPII complex and modulate secretory cargo transport. J. Cell Sci. 118, 3839-3847.
    • (2005) J. Cell Sci. , vol.118 , pp. 3839-3847
    • Palmer, K.J.1    Konkel, J.E.2    Stephens, D.J.3
  • 67
    • 21844440569 scopus 로고    scopus 로고
    • Genome-wide analysis of human kinases in clathrin- and caveolae/raft-mediated endocytosis
    • Pelkmans, L., Fava, E., Grabner, H., Hannus, M., Habermann, B., Krausz, E. and Zerial, M. (2005). Genome-wide analysis of human kinases in clathrin- and caveolae/raft-mediated endocytosis. Nature 436, 78-86.
    • (2005) Nature , vol.436 , pp. 78-86
    • Pelkmans, L.1    Fava, E.2    Grabner, H.3    Hannus, M.4    Habermann, B.5    Krausz, E.6    Zerial, M.7
  • 68
    • 63749105226 scopus 로고    scopus 로고
    • mTOR and the control of whole body metabolism
    • Polak, P. and Hall, M. N. (2009). mTOR and the control of whole body metabolism. Curr. Opin. Cell Biol. 21, 209-218.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 209-218
    • Polak, P.1    Hall, M.N.2
  • 69
    • 1842613600 scopus 로고    scopus 로고
    • YSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3zeta
    • Preisinger, C., Short, B., De Corte, V., Bruyneel, E., Haas, A., Kopajtich, R., Gettemans, J. and Barr, F. A. (2004). YSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3zeta. J. Cell Biol. 164, 1009-1020.
    • (2004) J. Cell Biol. , vol.164 , pp. 1009-1020
    • Preisinger, C.1    Short, B.2    De Corte, V.3    Bruyneel, E.4    Haas, A.5    Kopajtich, R.6    Gettemans, J.7    Barr, F.A.8
  • 70
    • 0031906429 scopus 로고    scopus 로고
    • Okadaic acid induces selective arrest of protein transport in the rough endoplasmic reticulum and prevents export into COPII-coated structures
    • Pryde, J. G., Farmaki, T. and Lucocq, J. M. (1998). Okadaic acid induces selective arrest of protein transport in the rough endoplasmic reticulum and prevents export into COPII-coated structures. Mol. Cell. Biol. 18, 1125-1135.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1125-1135
    • Pryde, J.G.1    Farmaki, T.2    Lucocq, J.M.3
  • 73
    • 37249078584 scopus 로고    scopus 로고
    • Golgi ribbon unlinking: An organelle-based G2/M checkpoint
    • Rabouille, C. and Kondylis, V. (2007). Golgi ribbon unlinking: an organelle-based G2/M checkpoint. Cell Cycle 6, 2723-2729.
    • (2007) Cell Cycle , vol.6 , pp. 2723-2729
    • Rabouille, C.1    Kondylis, V.2
  • 74
    • 58549114524 scopus 로고    scopus 로고
    • STAM adaptor proteins interact with COPII complexes and function in ER-to-Golgi trafficking
    • Rismanchi, N., Puertollano, R. and Blackstone, C. (2009). STAM adaptor proteins interact with COPII complexes and function in ER-to-Golgi trafficking. Traffic 10, 201-217.
    • (2009) Traffic , vol.10 , pp. 201-217
    • Rismanchi, N.1    Puertollano, R.2    Blackstone, C.3
  • 75
    • 0031018573 scopus 로고    scopus 로고
    • Sec31 encodes an essential component of the COPII coat required for transport vesicle budding from the endoplasmic reticulum
    • Salama, N. R., Chuang, J. S. and Schekman, R. W. (1997). Sec31 encodes an essential component of the COPII coat required for transport vesicle budding from the endoplasmic reticulum. Mol. Biol. Cell 8, 205-217.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 205-217
    • Salama, N.R.1    Chuang, J.S.2    Schekman, R.W.3
  • 77
    • 69549138483 scopus 로고    scopus 로고
    • Integrins mediate their unconventional, mechanical-stress-induced secretion via RhoA and PINCH in Drosophila
    • Schotman, H., Karhinen, L., and Rabouille, C. (2009). Integrins mediate their unconventional, mechanical-stress-induced secretion via RhoA and PINCH in Drosophila. J. Cell Sci. 122, 2662-2672.
    • (2009) J. Cell Sci. , vol.122 , pp. 2662-2672
    • Schotman, H.1    Karhinen, L.2    Rabouille, C.3
  • 78
    • 0023733211 scopus 로고
    • Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus
    • Schweizer, A., Fransen, J. A., Bächi, T., Ginsel, L. and Hauri, H. P. (1988). Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus. J. Cell Biol. 107, 1643-1653.
    • (1988) J. Cell Biol. , vol.107 , pp. 1643-1653
    • Schweizer, A.1    Fransen, J.A.2    Bächi, T.3    Ginsel, L.4    Hauri, H.P.5
  • 80
    • 79251574682 scopus 로고    scopus 로고
    • Akt phosphorylates Sec24: New clues into the regulation of ER-to-Golgi trafficking
    • epub ahead of print
    • Sharpe, L. J., Luu, W. and Brown, A. J. (2010). Akt phosphorylates Sec24: new clues into the regulation of ER-to-Golgi trafficking. Traffic epub ahead of print.
    • (2010) Traffic
    • Sharpe, L.J.1    Luu, W.2    Brown, A.J.3
  • 81
    • 77951710195 scopus 로고    scopus 로고
    • Requirements for transitional endoplasmic reticulum site structure and function in Saccharomyces cerevisiae
    • Shindiapina, P. and Barlowe, C. (2010). Requirements for transitional endoplasmic reticulum site structure and function in Saccharomyces cerevisiae. Mol. Biol. Cell 21, 1530-1545.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1530-1545
    • Shindiapina, P.1    Barlowe, C.2
  • 82
    • 67949124784 scopus 로고    scopus 로고
    • On vesicle formation and tethering in the ER-Golgi shuttle
    • Spang, A. (2009). On vesicle formation and tethering in the ER-Golgi shuttle. Curr. Opin. Cell Biol. 21, 531-536.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 531-536
    • Spang, A.1
  • 83
    • 0037296519 scopus 로고    scopus 로고
    • De novo formation, fusion and fission of mammalian COPII-coated endoplasmic reticulum exit sites
    • Stephens, D. J. (2003). De novo formation, fusion and fission of mammalian COPII-coated endoplasmic reticulum exit sites. EMBO Rep. 4, 210-217.
    • (2003) EMBO Rep. , vol.4 , pp. 210-217
    • Stephens, D.J.1
  • 85
    • 0037119988 scopus 로고    scopus 로고
    • Sec16p potentiates the action of COPII proteins to bud transport vesicles
    • Supek, F., Madden, D. T., Hamamoto, S., Orci, L. and Schekman, R. (2002). Sec16p potentiates the action of COPII proteins to bud transport vesicles. J. Cell Biol. 158, 1029-1038.
    • (2002) J. Cell Biol. , vol.158 , pp. 1029-1038
    • Supek, F.1    Madden, D.T.2    Hamamoto, S.3    Orci, L.4    Schekman, R.5
  • 86
    • 77952396703 scopus 로고    scopus 로고
    • Acute manipulation of Golgi phosphoinositides to assess their importance in cellular trafficking and signaling
    • Szentpetery, Z., Várnai, P. and Balla, T. (2010). Acute manipulation of Golgi phosphoinositides to assess their importance in cellular trafficking and signaling. Proc. Natl. Acad. Sci. USA 107, 8225-8230.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 8225-8230
    • Szentpetery, Z.1    Várnai, P.2    Balla, T.3
  • 88
    • 0034848865 scopus 로고    scopus 로고
    • Beta-adrenergic receptors (betaAR) regulate cardiomyocyte proliferation during early postnatal life
    • Tseng, Y. T., Kopel, R., Stabila, J. P., McGonnigal, B. G., Nguyen, T. T., Gruppuso, P. A. and Padbury, J. F. (2001). Beta-adrenergic receptors (betaAR) regulate cardiomyocyte proliferation during early postnatal life. FASEB J. 15, 1921-1926.
    • (2001) FASEB J. , vol.15 , pp. 1921-1926
    • Tseng, Y.T.1    Kopel, R.2    Stabila, J.P.3    McGonnigal, B.G.4    Nguyen, T.T.5    Gruppuso, P.A.6    Padbury, J.F.7
  • 89
    • 47749141468 scopus 로고    scopus 로고
    • Signal-mediated dynamic retention of glycosyltransferases in the Golgi
    • Tu, L., Tai, W. C., Chen, L. and Banfield, D. K. (2008). Signal-mediated dynamic retention of glycosyltransferases in the Golgi. Science 321, 404-407.
    • (2008) Science , vol.321 , pp. 404-407
    • Tu, L.1    Tai, W.C.2    Chen, L.3    Banfield, D.K.4
  • 90
    • 0037926394 scopus 로고    scopus 로고
    • A direct role for GRASP65 as a mitotically regulated Golgi stacking factor
    • Wang, Y., Seemann, J., Pypaert, M., Shorter, J. and Warren, G. (2003). A direct role for GRASP65 as a mitotically regulated Golgi stacking factor. EMBO J. 22, 3279-3290.
    • (2003) EMBO J. , vol.22 , pp. 3279-3290
    • Wang, Y.1    Seemann, J.2    Pypaert, M.3    Shorter, J.4    Warren, G.5
  • 91
    • 33750969692 scopus 로고    scopus 로고
    • Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells
    • Watson, P., Townley, A. K., Koka, P., Palmer, K. J. and Stephens, D. J. (2006). Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells. Traffic 7, 1678-1687.
    • (2006) Traffic , vol.7 , pp. 1678-1687
    • Watson, P.1    Townley, A.K.2    Koka, P.3    Palmer, K.J.4    Stephens, D.J.5
  • 94
    • 76149142505 scopus 로고    scopus 로고
    • PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase signaling to retrograde Golgi trafficking
    • Wood, C. S., Schmitz, K. R., Bessman, N. J., Setty, T. G., Ferguson, K. M. and Burd, C. G. (2009). PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase signaling to retrograde Golgi trafficking. J. Cell Biol. 187, 967-975.
    • (2009) J. Cell Biol. , vol.187 , pp. 967-975
    • Wood, C.S.1    Schmitz, K.R.2    Bessman, N.J.3    Setty, T.G.4    Ferguson, K.M.5    Burd, C.G.6
  • 95
    • 11244273061 scopus 로고    scopus 로고
    • Reconstitution of COPII vesicle fusion to generate a pre-Golgi intermediate compartment
    • Xu, D. and Hay, J. C. (2004). Reconstitution of COPII vesicle fusion to generate a pre-Golgi intermediate compartment. J. Cell Biol. 167, 997-1003.
    • (2004) J. Cell Biol. , vol.167 , pp. 997-1003
    • Xu, D.1    Hay, J.C.2
  • 96
    • 65249115901 scopus 로고    scopus 로고
    • A primary role for Golgi positioning in directed secretion, cell polarity, and wound healing
    • Yadav, S., Puri, S. and Linstedt, A. D. (2009). A primary role for Golgi positioning in directed secretion, cell polarity, and wound healing. Mol. Biol. Cell 20, 1728-1736.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1728-1736
    • Yadav, S.1    Puri, S.2    Linstedt, A.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.