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Volumn 30, Issue 16, 2010, Pages 3956-3969

The interaction of Epac1 and ran promotes Rap1 activation at the nuclear envelope

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CYCLIC AMP; GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN EPAC1; RAN BINDING PROTEIN 2; RAN PROTEIN; RAP1 PROTEIN; UNCLASSIFIED DRUG;

EID: 77955629623     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00242-10     Document Type: Article
Times cited : (49)

References (51)
  • 1
    • 62149131337 scopus 로고    scopus 로고
    • Compartmentalized signalling: Spatial regulation of cAMP by the action of compartmentalized phosphodiesterases
    • Baillie, G. S. 2009. Compartmentalized signalling: spatial regulation of cAMP by the action of compartmentalized phosphodiesterases. FEBS J. 276:1790-1799.
    • (2009) FEBS J. , vol.276 , pp. 1790-1799
    • Baillie, G.S.1
  • 3
    • 27744571333 scopus 로고    scopus 로고
    • Analysis of Ras and Rap activation in living cells using fluorescent Ras binding domains
    • Bivona, T. G., and M. R. Philips. 2005. Analysis of Ras and Rap activation in living cells using fluorescent Ras binding domains. Methods Enzymol. 37:138-145.
    • (2005) Methods Enzymol. , vol.37 , pp. 138-145
    • Bivona, T.G.1    Philips, M.R.2
  • 6
    • 51849113340 scopus 로고    scopus 로고
    • Knockdown of B-Raf impairs spindle formation and the mitotic checkpoint in human somatic cells
    • Borysova, M. K., Y. Cui, M. Snyder, and T. M. Guadagno. 2008. Knockdown of B-Raf impairs spindle formation and the mitotic checkpoint in human somatic cells. Cell Cycle 7:2894-2901.
    • (2008) Cell Cycle , vol.7 , pp. 2894-2901
    • Borysova, M.K.1    Cui, Y.2    Snyder, M.3    Guadagno, T.M.4
  • 7
    • 34247847951 scopus 로고    scopus 로고
    • N-terminal alpha-methylation of RCC1 is necessary for stable chromatin association and normal mitosis
    • Chen, T., T. L. Muratore, C. E. Schaner-Tooley, J. Shabanowitz, D. F. Hunt, and I. G. Macara. 2007. N-terminal alpha-methylation of RCC1 is necessary for stable chromatin association and normal mitosis. Nat. Cell Biol. 9:596-603.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 596-603
    • Chen, T.1    Muratore, T.L.2    Schaner-Tooley, C.E.3    Shabanowitz, J.4    Hunt, D.F.5    Macara, I.G.6
  • 9
    • 21644474823 scopus 로고    scopus 로고
    • Spatial and temporal control of nuclear envelope assembly by Ran GTPase
    • Clarke, P. R., and C. Zhang. 2004. Spatial and temporal control of nuclear envelope assembly by Ran GTPase. Symp. Soc. Exp. Biol. 2004:193-204.
    • (2004) Symp. Soc. Exp. Biol. , vol.2004 , pp. 193-204
    • Clarke, P.R.1    Zhang, C.2
  • 10
    • 33746469525 scopus 로고    scopus 로고
    • Epac1 and cAMP-dependent protein kinase holoenzyme have similar cAMP affinity, but their cAMP domains have distinct structural features and cyclic nucleotide recognition
    • Dao, K. K., K. Teigen, R. Kopperud, E. Hodneland, F. Schwede, A. E. Christensen, A. Martinez, and S. O. Doskeland. 2006. Epac1 and cAMP-dependent protein kinase holoenzyme have similar cAMP affinity, but their cAMP domains have distinct structural features and cyclic nucleotide recognition. J. Biol. Chem. 281:21500-21511.
    • (2006) J. Biol. Chem. , vol.281 , pp. 21500-21511
    • Dao, K.K.1    Teigen, K.2    Kopperud, R.3    Hodneland, E.4    Schwede, F.5    Christensen, A.E.6    Martinez, A.7    Doskeland, S.O.8
  • 11
    • 0030696935 scopus 로고    scopus 로고
    • RanGTP targets p97 to RanBP2, a filamentous protein localized at the cytoplasmic periphery of the nuclear pore complex
    • Delphin, C., T. Guan, F. Melchior, and L. Gerace. 1997. RanGTP targets p97 to RanBP2, a filamentous protein localized at the cytoplasmic periphery of the nuclear pore complex. Mol. Biol. Cell 8:2379-2390.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2379-2390
    • Delphin, C.1    Guan, T.2    Melchior, F.3    Gerace, L.4
  • 13
    • 0036789949 scopus 로고    scopus 로고
    • Ras and relatives - Job sharing and networking keep an old family together
    • Ehrhardt, A., G. Ehrhardt, X. Guo, and J. Schrader. 2002. Ras and relatives - job sharing and networking keep an old family together. Exp. Hematol. 30:1089.
    • (2002) Exp. Hematol. , vol.30 , pp. 1089
    • Ehrhardt, A.1    Ehrhardt, G.2    Guo, X.3    Schrader, J.4
  • 14
    • 0141995069 scopus 로고    scopus 로고
    • The nuclear pore complex: Nucleocytoplasmic transport and beyond
    • Fahrenkrog, B., and U. Aebi. 2003. The nuclear pore complex: nucleocytoplasmic transport and beyond. Nat. Rev. Mol. Cell Biol. 4:757-766.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 757-766
    • Fahrenkrog, B.1    Aebi, U.2
  • 15
  • 16
    • 33846136109 scopus 로고    scopus 로고
    • Differential roles of Rap1 and Rap2 small GTPases in neurite retraction and synapse elimination in hippocampal spiny neurons
    • DOI 10.1111/j.1471-4159.2006.04195.x
    • Fu, Z., S. H. Lee, A. Simonetta, J. Hansen, M. Sheng, and D. T. Pak. 2007. Differential roles of Rap1 and Rap2 small GTPases in neurite retraction and synapse elimination in hippocampal spiny neurons. J. Neurochem. 100:118-131. (Pubitemid 46085843)
    • (2007) Journal of Neurochemistry , vol.100 , Issue.1 , pp. 118-131
    • Fu, Z.1    Lee, S.H.2    Simonetta, A.3    Hansen, J.4    Sheng, M.5    Pak, D.T.S.6
  • 17
    • 75649097760 scopus 로고    scopus 로고
    • The role of Epac proteins, novel cAMP mediators, in the regulation of immune, lung and neuronal function
    • Grandoch, M., S. S. Roscioni, and M. Schmidt. 2010. The role of Epac proteins, novel cAMP mediators, in the regulation of immune, lung and neuronal function. Br. J. Pharmacol. 159:265-284
    • (2010) Br. J. Pharmacol. , vol.159 , pp. 265-284
    • Grandoch, M.1    Roscioni, S.S.2    Schmidt, M.3
  • 18
    • 51649110721 scopus 로고    scopus 로고
    • Regulation of chromatin binding by a conformational switch in the tail of the Ran exchange factor RCC1
    • Hao, Y., and I. G. Macara. 2008. Regulation of chromatin binding by a conformational switch in the tail of the Ran exchange factor RCC1. J. Cell Biol. 182:827-836.
    • (2008) J. Cell Biol. , vol.182 , pp. 827-836
    • Hao, Y.1    Macara, I.G.2
  • 19
    • 8644262258 scopus 로고    scopus 로고
    • Importin beta: Conducting a much larger cellular symphony
    • DOI 10.1016/j.molcel.2004.10.026, PII S1097276504006471
    • Harel, A., and D. J. Forbes. 2004. Importin beta: conducting a much larger cellular symphony. Mol. Cell 16:319-330. (Pubitemid 39504787)
    • (2004) Molecular Cell , vol.16 , Issue.3 , pp. 319-330
    • Harel, A.1    Forbes, D.J.2
  • 20
    • 75749117558 scopus 로고    scopus 로고
    • Underpinning compartmentalised cAMP signalling through targeted cAMP breakdown
    • Houslay, M. D. 2010. Underpinning compartmentalised cAMP signalling through targeted cAMP breakdown. Trends Biochem. Sci. 35:91-100.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 91-100
    • Houslay, M.D.1
  • 22
    • 70449448939 scopus 로고    scopus 로고
    • Dynamic localisation of Ran GTPase during the cell cycle
    • Hutchins, J. R., W. J. Moore, and P. R. Clarke. 2009. Dynamic localisation of Ran GTPase during the cell cycle. BMC Cell Biol. 10:66-76.
    • (2009) BMC Cell Biol. , vol.10 , pp. 66-76
    • Hutchins, J.R.1    Moore, W.J.2    Clarke, P.R.3
  • 24
    • 0035947724 scopus 로고    scopus 로고
    • Identification of the mechanisms regulating the differential activation of the MAPK cascade by epidermal growth factor and nerve growth factor in PC12 cells
    • Kao, S., R. K. Jaiswal, W. Kolch, and G. E. Landreth. 2001. Identification of the mechanisms regulating the differential activation of the MAPK cascade by epidermal growth factor and nerve growth factor in PC12 cells. J. Biol. Chem. 276:18169-18177.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18169-18177
    • Kao, S.1    Jaiswal, R.K.2    Kolch, W.3    Landreth, G.E.4
  • 25
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller, A., A. I. Nesvizhskii, E. Kolker, and R. Aebersold. 2002. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal. Chem. 74:5383-5392.
    • (2002) Anal. Chem. , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 27
    • 33646366678 scopus 로고    scopus 로고
    • The RAP1 guanine nucleotide exchange factor Epac2 couples cyclic AMP and Ras signals at the plasma membrane
    • Li, Y., S. Asuri, J. F. Rebhun, A. F. Castro, N. C. Paranavitana, and L. A. Quilliam. 2006. The RAP1 guanine nucleotide exchange factor Epac2 couples cyclic AMP and Ras signals at the plasma membrane. J. Biol. Chem. 281:2506-2514.
    • (2006) J. Biol. Chem. , vol.281 , pp. 2506-2514
    • Li, Y.1    Asuri, S.2    Rebhun, J.F.3    Castro, A.F.4    Paranavitana, N.C.5    Quilliam, L.A.6
  • 29
    • 0030462224 scopus 로고    scopus 로고
    • Mutations within the Ran/TC4 GTPase. Effects on regulatory factor interactions and subcellular localization
    • Lounsbury, K. M., S. A. Richards, K. L. Carey, and I. G. Macara. 1996. Mutations within the Ran/TC4 GTPase. Effects on regulatory factor interactions and subcellular localization. J. Biol. Chem. 271:32834-32841.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32834-32841
    • Lounsbury, K.M.1    Richards, S.A.2    Carey, K.L.3    Macara, I.G.4
  • 30
    • 0035203632 scopus 로고    scopus 로고
    • Transport into and out of the nucleus
    • Macara, I. G. 2001. Transport into and out of the nucleus. Microbiol. Mol. Biol. Rev. 65:570-594.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 570-594
    • Macara, I.G.1
  • 31
    • 1942533655 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase kinase kinase kinase 4 as a putative effector of Rap2 to activate the c-Jun N-terminal kinase
    • Machida, N., M. Umikawa, K. Takei, N. Sakima, B. E. Myagmar, K. Taira, H. Uezato, Y. Ogawa, and K. Kariya. 2004. Mitogen-activated protein kinase kinase kinase kinase 4 as a putative effector of Rap2 to activate the c-Jun N-terminal kinase. J. Biol. Chem. 279:15711-15714.
    • (2004) J. Biol. Chem. , vol.279 , pp. 15711-15714
    • Machida, N.1    Umikawa, M.2    Takei, K.3    Sakima, N.4    Myagmar, B.E.5    Taira, K.6    Uezato, H.7    Ogawa, Y.8    Kariya, K.9
  • 32
    • 4744349609 scopus 로고    scopus 로고
    • Exchange protein directly activated by cAMP (EPAC) interacts with the light chain (LC) 2 of MAP1A
    • Magiera, M. M., M. Gupta, C. J. Rundell, N. Satish, I. Ernens, and S. J. Yarwood. 2004. Exchange protein directly activated by cAMP (EPAC) interacts with the light chain (LC) 2 of MAP1A. Biochem. J. 382:803-810.
    • (2004) Biochem. J. , vol.382 , pp. 803-810
    • Magiera, M.M.1    Gupta, M.2    Rundell, C.J.3    Satish, N.4    Ernens, I.5    Yarwood, S.J.6
  • 33
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • Mahajan, R., C. Delphin, T. Guan, L. Gerace, and F. Melchior. 1997. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell 88:97-107. (Pubitemid 27180334)
    • (1997) Cell , vol.88 , Issue.1 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 34
    • 22744445886 scopus 로고    scopus 로고
    • Signaling interplay in Ras superfamily function
    • Mitin, N., K. L. Rossman, and C. J. Der. 2005. Signaling interplay in Ras superfamily function. Curr. Biol. 15:R563-R574.
    • (2005) Curr. Biol. , vol.15
    • Mitin, N.1    Rossman, K.L.2    Der, C.J.3
  • 35
    • 0032483384 scopus 로고    scopus 로고
    • Ran and nuclear transport
    • Moore, M. S. 1998. Ran and nuclear transport. J. Biol. Chem. 273:22857-22860.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22857-22860
    • Moore, M.S.1
  • 36
    • 0034658460 scopus 로고    scopus 로고
    • Nuclear import of the Ran exchange factor, RCC1, is mediated by at least two distinct mechanisms
    • Nemergut, M. E., and I. G. Macara. 2000. Nuclear import of the Ran exchange factor, RCC1, is mediated by at least two distinct mechanisms. J. Cell Biol. 149:835-850.
    • (2000) J. Cell Biol. , vol.149 , pp. 835-850
    • Nemergut, M.E.1    Macara, I.G.2
  • 37
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii, A. I., A. Keller, E. Kolker, and R. Aebersold. 2003. A statistical model for identifying proteins by tandem mass spectrometry. Anal. Chem. 75:4646-4658.
    • (2003) Anal. Chem. , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 39
    • 0030048696 scopus 로고    scopus 로고
    • Activation of brain B-Raf protein kinase by Rap1B small GTP-binding protein
    • Ohtsuka, T., K. Shimizu, B. Yamamori, S. Kuroda, and Y. Takai. 1996. Activation of brain B-Raf protein kinase by Rap1B small GTP-binding protein. J. Biol. Chem. 271:1258-1261.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1258-1261
    • Ohtsuka, T.1    Shimizu, K.2    Yamamori, B.3    Kuroda, S.4    Takai, Y.5
  • 41
    • 0037135592 scopus 로고    scopus 로고
    • Cell cycle-dependent subcellular localization of exchange factor directly activated by cAMP
    • Qiao, J., F. C. Mei, V. L. Popov, L. A. Vergara, and X. Cheng. 2002. Cell cycle-dependent subcellular localization of exchange factor directly activated by cAMP. J. Biol. Chem. 277:26581-26586.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26581-26586
    • Qiao, J.1    Mei, F.C.2    Popov, V.L.3    Vergara, L.A.4    Cheng, X.5
  • 42
    • 0141532168 scopus 로고    scopus 로고
    • Ligand-mediated activation of the cAMP-responsive guanine nucleotide exchange factor Epac
    • Rehmann, H., F. Schwede, S. O. Doskeland, A. Wittinghofer, and J. L. Bos. 2003. Ligand-mediated activation of the cAMP-responsive guanine nucleotide exchange factor Epac. J. Biol. Chem. 278:38548-38556.
    • (2003) J. Biol. Chem. , vol.278 , pp. 38548-38556
    • Rehmann, H.1    Schwede, F.2    Doskeland, S.O.3    Wittinghofer, A.4    Bos, J.L.5
  • 43
    • 70350228414 scopus 로고    scopus 로고
    • Importin beta regulates the seeding of chromatin with initiation sites for nuclear pore assembly
    • Rotem, A., R. Gruber, H. Shorer, L. Shaulov, E. Klein, and A. Harel. 2009. Importin beta regulates the seeding of chromatin with initiation sites for nuclear pore assembly. Mol. Biol. Cell 20:4031-4042.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4031-4042
    • Rotem, A.1    Gruber, R.2    Shorer, H.3    Shaulov, L.4    Klein, E.5    Harel, A.6
  • 44
    • 0141545024 scopus 로고    scopus 로고
    • Nup358 integrates nuclear envelope breakdown with kinetochore assembly
    • DOI 10.1083/jcb.200304080
    • Salina, D., P. Enarson, J. B. Rattner, and B. Burke. 2003. Nup358 integrates nuclear envelope breakdown with kinetochore assembly. J. Cell Biol. 162: 991-1001. (Pubitemid 37174183)
    • (2003) Journal of Cell Biology , vol.162 , Issue.6 , pp. 991-1001
    • Salina, D.1    Enarson, P.2    Rattner, J.B.3    Burke, B.4
  • 46
    • 0038741814 scopus 로고    scopus 로고
    • Does Rap1 deserve a bad Rap? Trends Biochem
    • Stork, P. J. S. 2003. Does Rap1 deserve a bad Rap? Trends Biochem. Sci. 28:267-275.
    • (2003) Sci. , vol.28 , pp. 267-275
    • Stork, P.J.S.1
  • 48
    • 0033612390 scopus 로고    scopus 로고
    • Structural view of the Ran-Importin beta interaction at 2.3 Å resolution
    • Vetter, I. R., A. Arndt, U. Kutay, D. Gorlich, and A. Wittinghofer. 1999. Structural view of the Ran-Importin beta interaction at 2.3 Å resolution. Cell 97:635-646.
    • (1999) Cell , vol.97 , pp. 635-646
    • Vetter, I.R.1    Arndt, A.2    Kutay, U.3    Gorlich, D.4    Wittinghofer, A.5
  • 49
    • 33644765206 scopus 로고    scopus 로고
    • Rap1-mediated activation of extracellular signal-regulated kinases by cyclic AMP is dependent on the mode of Rap1 activation
    • Wang, Z., T. J. Dillon, V. Pokala, S. Mishra, K. Labudda, B. Hunter, and P. J. Stork. 2006. Rap1-mediated activation of extracellular signal-regulated kinases by cyclic AMP is dependent on the mode of Rap1 activation. Mol. Cell. Biol. 26:2130-2145.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2130-2145
    • Wang, Z.1    Dillon, T.J.2    Pokala, V.3    Mishra, S.4    Labudda, K.5    Hunter, B.6    Stork, P.J.7
  • 50
    • 0029070074 scopus 로고
    • Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran- GTP binding sites, zinc fingers, a cyclophilin a homologous domain, and a leucine-rich region
    • Wu, J., M. J. Matunis, D. Kraemer, G. Blobel, and E. Coutavas. 1995. Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran- GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region. J. Biol. Chem. 270:14209-14213.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14209-14213
    • Wu, J.1    Matunis, M.J.2    Kraemer, D.3    Blobel, G.4    Coutavas, E.5


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