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Volumn 10, Issue 4, 2011, Pages 494-501

eIF2α kinases control chalone production in dictyostelium discoideum

Author keywords

[No Author keywords available]

Indexed keywords

CHALONE; INITIATION FACTOR 2; PROTOZOAL PROTEIN;

EID: 79955366731     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00270-10     Document Type: Article
Times cited : (9)

References (40)
  • 1
    • 50249176490 scopus 로고    scopus 로고
    • The secreted Dictyostelium protein CfaD is a chalone
    • Bakthavatsalam, D., et al. 2008. The secreted Dictyostelium protein CfaD is a chalone. J. Cell Sci. 121:2473-2480.
    • (2008) J. Cell Sci , vol.121 , pp. 2473-2480
    • Bakthavatsalam, D.1
  • 2
    • 68949215203 scopus 로고    scopus 로고
    • A Dictyostelium chalone uses G proteins to regulate proliferation
    • Bakthavatsalam, D., J. M. Choe, N. E. Hanson, and R. H. Gomer. 2009. A Dictyostelium chalone uses G proteins to regulate proliferation. BMC Biol. 7:44.
    • (2009) BMC Biol , vol.7 , pp. 44
    • Bakthavatsalam, D.1    Choe, J.M.2    Hanson, N.E.3    Gomer, R.H.4
  • 3
    • 77954737729 scopus 로고    scopus 로고
    • The secreted proteome profile of developing Dictyostelium discoideum cells
    • Bakthavatsalam, D., and R. H. Gomer. 2010. The secreted proteome profile of developing Dictyostelium discoideum cells. Proteomics 10:2556-2559.
    • (2010) Proteomics , vol.10 , pp. 2556-2559
    • Bakthavatsalam, D.1    Gomer, R.H.2
  • 4
    • 35748960252 scopus 로고    scopus 로고
    • The eIF2alpha kinases PERK and PKR activate glycogen synthase kinase 3 to promote the proteasomal degradation of p53
    • Baltzis, D., et al. 2007. The eIF2alpha kinases PERK and PKR activate glycogen synthase kinase 3 to promote the proteasomal degradation of p53. J. Biol. Chem. 282:31675-31687.
    • (2007) J. Biol. Chem , vol.282 , pp. 31675-31687
    • Baltzis, D.1
  • 5
    • 0033739622 scopus 로고    scopus 로고
    • PERK mediates cell-cycle exit during the mammalian unfolded protein response
    • Brewer, J. W., and J. A. Diehl. 2000. PERK mediates cell-cycle exit during the mammalian unfolded protein response. Proc. Natl. Acad. Sci. U. S. A. 97:12625-12630.
    • (2000) Proc. Natl. Acad. Sci. U. S. A , vol.97 , pp. 12625-12630
    • Brewer, J.W.1    Diehl, J.A.2
  • 6
    • 27744527109 scopus 로고    scopus 로고
    • A secreted factor represses cell proliferation in Dictyostelium
    • Brock, D. A., and R H. Gomer. 2005. A secreted factor represses cell proliferation in Dictyostelium. Development 132:4553-4562.
    • (2005) Development , vol.132 , pp. 4553-4562
    • Brock, D.A.1    Gomer, R.H.2
  • 7
    • 0000794993 scopus 로고
    • The control of mitotic activity in adult mammalian tissues
    • Bullough, W. S. 1962. The control of mitotic activity in adult mammalian tissues. Biol. Rev. 37:307-342.
    • (1962) Biol. Rev , vol.37 , pp. 307-342
    • Bullough, W.S.1
  • 8
    • 60649116315 scopus 로고    scopus 로고
    • Dictyostelium cells bind a secreted autocrine factor that represses cell proliferation
    • Choe, J. M., D. Bakthavatsalam, J. E. Phillips, and R. H. Gomer. 2009. Dictyostelium cells bind a secreted autocrine factor that represses cell proliferation. BMC Biochem. 10:4.
    • (2009) BMC Biochem , vol.10 , pp. 4
    • Choe, J.M.1    Bakthavatsalam, D.2    Phillips, J.E.3    Gomer, R.H.4
  • 9
    • 0014782521 scopus 로고
    • RNA in cytoplasmic and nuclear fractions of cellular slime mold amebae
    • Cocucci, S., and M. Sussman. 1970. RNA in cytoplasmic and nuclear fractions of cellular slime mold amebae. J. Cell Biol. 45:399-407.
    • (1970) J. Cell Biol , vol.45 , pp. 399-407
    • Cocucci, S.1    Sussman, M.2
  • 10
    • 0026556814 scopus 로고
    • Phosphorylation of initiation factor 2a by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast
    • Dever, T., et al. 1992. Phosphorylation of initiation factor 2a by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast. Cell 68:585-596.
    • (1992) Cell , vol.68 , pp. 585-596
    • Dever, T.1
  • 11
    • 0037154965 scopus 로고    scopus 로고
    • Gene-specific regulation by general translation factors
    • Dever, T. E. 2002. Gene-specific regulation by general translation factors. Cell 108:545-556.
    • (2002) Cell , vol.108 , pp. 545-556
    • Dever, T.E.1
  • 12
    • 0033635215 scopus 로고    scopus 로고
    • Uncharged tRNA activates GCN2 by displacing the protein kinase moiety from a bipartite tRNA-binding domain
    • Dong, J., H. Qiu, M. Garcia-Barrio, J. Anderson, and A. G. Hinnebusch. 2000. Uncharged tRNA activates GCN2 by displacing the protein kinase moiety from a bipartite tRNA-binding domain. Mol. Cell 6:269-279.
    • (2000) Mol. Cell , vol.6 , pp. 269-279
    • Dong, J.1    Qiu, H.2    Garcia-Barrio, M.3    Anderson, J.4    Hinnebusch, A.G.5
  • 13
    • 0028231283 scopus 로고
    • LagC is required for cell-cell interactions that are essential for cell-type differentiation in Dictyostelium
    • Dynes, J. L., et al. 1994. LagC is required for cell-cell interactions that are essential for cell-type differentiation in Dictyostelium. Genes Dev. 8:948-958.
    • (1994) Genes Dev , vol.8 , pp. 948-958
    • Dynes, J.L.1
  • 14
    • 2942657451 scopus 로고    scopus 로고
    • IfkA, a preumptive eIFalpha kinase of Dictyostelium, is required for proper timing of asggregation and regulation of mound size
    • Fang, R., Y. Xiong, and C. K. Singleton. 2003. IfkA, a preumptive eIFalpha kinase of Dictyostelium, is required for proper timing of asggregation and regulation of mound size. BMC Dev. Biol. 3:3.
    • (2003) BMC Dev. Biol , vol.3 , pp. 3
    • Fang, R.1    Xiong, Y.2    Singleton, C.K.3
  • 15
    • 0029807304 scopus 로고    scopus 로고
    • Activation of the Raf-1 kinase cascade by coumermycin-induced dimerization
    • Farrar, M. A., L. Albero, and R. M. Perlmutter. 1996. Activation of the Raf-1 kinase cascade by coumermycin-induced dimerization. Nature 383:178-181.
    • (1996) Nature , vol.383 , pp. 178-181
    • Farrar, M.A.1    Albero, L.2    Perlmutter, R.M.3
  • 16
    • 0037166289 scopus 로고    scopus 로고
    • Regulation of internal ribosomal entry site-mediated translation by phosphorylation of the translation initiation factor eIF2alpha
    • Fernandez, J., I. Yaman, P. Sarnow, M. Snider, and M. Hatzoglou. 2002. Regulation of internal ribosomal entry site-mediated translation by phosphorylation of the translation initiation factor eIF2alpha. J. Biol. Chem. 277:19198-19205.
    • (2002) J. Biol. Chem , vol.277 , pp. 19198-19205
    • Fernandez, J.1    Yaman, I.2    Sarnow, P.3    Snider, M.4    Hatzoglou, M.5
  • 17
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding, H., et al. 2000. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol. Cell 6:1099-1108.
    • (2000) Mol. Cell , vol.6 , pp. 1099-1108
    • Harding, H.1
  • 18
    • 0000729653 scopus 로고    scopus 로고
    • Translational control of GCN4: Gene-specific regulation by phosphorylation of eIF2
    • J. Hershey, M. Mathews, and N. Sonenberg (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Hinnenbusch, A. 1996. Translational control of GCN4: gene-specific regulation by phosphorylation of eIF2, p. 199-244. In J. Hershey, M. Mathews, and N. Sonenberg (ed.), Translational control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1996) Translational Control , pp. 199-244
    • Hinnenbusch, A.1
  • 19
    • 0024582782 scopus 로고
    • The phosphorylation of eukaryotic initiation factor 2 alters translational efficiency of specific mRNAs
    • Kaufman, R., M. Davies, V. Pathak, and J. Hershey. 1989. The phosphorylation of eukaryotic initiation factor 2 alters translational efficiency of specific mRNAs. Mol. Cell. Biol. 9:946-958.
    • (1989) Mol. Cell. Biol , vol.9 , pp. 946-958
    • Kaufman, R.1    Davies, M.2    Pathak, V.3    Hershey, J.4
  • 20
    • 34548511321 scopus 로고    scopus 로고
    • A novel function of eIF2alpha kinases as inducers of the phosphoinositide-3 kinase signaling pathway
    • Kazemi, S., et al. 2007. A novel function of eIF2alpha kinases as inducers of the phosphoinositide-3 kinase signaling pathway. Mol. Biol. Cell 18:3635-3644.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3635-3644
    • Kazemi, S.1
  • 21
    • 0018871291 scopus 로고
    • The effects of cell density and starvation on early developmental events in Dictyostelium discoideum
    • Margolskee, J. P., S. Froshauer, R Skrinska, and H. Lodish. 1980. The effects of cell density and starvation on early developmental events in Dictyostelium discoideum. Dev. Biol. 74:409-421.
    • (1980) Dev. Biol , vol.74 , pp. 409-421
    • Margolskee, J.P.1    Froshauer, S.2    Skrinska, R.3    Lodish, H.4
  • 22
    • 0017282206 scopus 로고
    • Regulation of development in Dictyostelium discoideum
    • Marin, F. T. 1976. Regulation of development in Dictyostelium discoideum. Dev. Biol. 48:110-117.
    • (1976) Dev. Biol , vol.48 , pp. 110-117
    • Marin, F.T.1
  • 23
    • 0017745827 scopus 로고
    • Regulation of development in Dictyostelium discoideum
    • Marin, F. T. 1977. Regulation of development in Dictyostelium discoideum. Dev. Biol. 60:389-395.
    • (1977) Dev. Biol , vol.60 , pp. 389-395
    • Marin, F.T.1
  • 24
    • 46049083013 scopus 로고    scopus 로고
    • Live imaging of the Dictyostelium cell cycle reveals widespread S phase during development, a G2 bias in spore differentiation and a premitotic checkpoint
    • Muramoto, T., and J. R. Chubb. 2008. Live imaging of the Dictyostelium cell cycle reveals widespread S phase during development, a G2 bias in spore differentiation and a premitotic checkpoint. Development 135:1647-1657.
    • (2008) Development , vol.135 , pp. 1647-1657
    • Muramoto, T.1    Chubb, J.R.2
  • 25
    • 0031896743 scopus 로고    scopus 로고
    • Thiamine deficiency decreases steady-state mRNA levels for transketolase and pyruvate dehydrogenase but not for a-ketoglutarate dehydrogenase in three human cell types
    • Pekovich, S. R., P. R. Martin, and C. K. Singleton. 1998. Thiamine deficiency decreases steady-state mRNA levels for transketolase and pyruvate dehydrogenase but not for a-ketoglutarate dehydrogenase in three human cell types. J. Nutr. 128:683-687.
    • (1998) J. Nutr , vol.128 , pp. 683-687
    • Pekovich, S.R.1    Martin, P.R.2    Singleton, C.K.3
  • 26
    • 77957801975 scopus 로고    scopus 로고
    • The ROCO kinase QkgA is necessary for proliferation inhibition by autocrine signals in Dictyostelium discoideum
    • Phillips, J. E., and R H. Gomer. 2010. The ROCO kinase QkgA is necessary for proliferation inhibition by autocrine signals in Dictyostelium discoideum. Eukaryot. Cell 9:1557-1565.
    • (2010) Eukaryot. Cell , vol.9 , pp. 1557-1565
    • Phillips, J.E.1    Gomer, R.H.2
  • 27
    • 0031946361 scopus 로고    scopus 로고
    • Dimerization by translation initiation factor 2 kinase GCN2 is mediated by interactions in the C-terminal ribosome-binding region and the protein kinase domain
    • Qiu, H., M. T. Garcia-Barrio, and A. G. Hinnebusch. 1998. Dimerization by translation initiation factor 2 kinase GCN2 is mediated by interactions in the C-terminal ribosome-binding region and the protein kinase domain. Mol. Cell. Biol. 18:2697-2711.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 2697-2711
    • Qiu, H.1    Garcia-Barrio, M.T.2    Hinnebusch, A.G.3
  • 28
    • 0037093333 scopus 로고    scopus 로고
    • Mutations that bypass tRNA binding activate the intrinsically defective kinase domain in GCN2
    • Qiu, H., C. Hu, J. Dong, and A. G. Hinnebusch. 2002. Mutations that bypass tRNA binding activate the intrinsically defective kinase domain in GCN2. Genes Dev. 16:1271-1280.
    • (2002) Genes Dev , vol.16 , pp. 1271-1280
    • Qiu, H.1    Hu, C.2    Dong, J.3    Hinnebusch, A.G.4
  • 29
    • 33845539293 scopus 로고    scopus 로고
    • Disruption of the ifkA and ifkB genes results in altered cell adhesion, morphological defects and a propensity to form pre-stalk O cells during development of Dictyostelium
    • Rai, M., Y. H. Xiong, and C. K. Singleton. 2006. Disruption of the ifkA and ifkB genes results in altered cell adhesion, morphological defects and a propensity to form pre-stalk O cells during development of Dictyostelium. Differentiation 74:583-595.
    • (2006) Differentiation , vol.74 , pp. 583-595
    • Rai, M.1    Xiong, Y.H.2    Singleton, C.K.3
  • 30
    • 41249089202 scopus 로고    scopus 로고
    • PKR and PKR-like endoplasmic reticulum kinase induce the proteasome-dependent degradation of cyclin D1 via a mechanism requiring eukaryotic initiation factor 2alpha phosphorylation
    • Raven, J. F., et al. 2008. PKR and PKR-like endoplasmic reticulum kinase induce the proteasome-dependent degradation of cyclin D1 via a mechanism requiring eukaryotic initiation factor 2alpha phosphorylation. J. Biol. Chem. 283:3097-3108.
    • (2008) J. Biol. Chem , vol.283 , pp. 3097-3108
    • Raven, J.F.1
  • 31
    • 0024005867 scopus 로고
    • Transcriptional-translational regulatory circuit in Saccharomyces cerevisiae which involves the GCN2 transcriptional activator and the GCN2 protein kinase
    • Roussou, I., G. Thireos, and B. Hauge. 1988. Transcriptional-translational regulatory circuit in Saccharomyces cerevisiae which involves the GCN2 transcriptional activator and the GCN2 protein kinase. Mol. Cell. Biol. 8:2132-2139.
    • (1988) Mol. Cell. Biol , vol.8 , pp. 2132-2139
    • Roussou, I.1    Thireos, G.2    Hauge, B.3
  • 32
    • 0029770049 scopus 로고    scopus 로고
    • Conserved residues are functionally distinct within transketolases of different species
    • Singleton, C. K., J. J.-L. Wang, L. Shen, and P. R Martin. 1996. Conserved residues are functionally distinct within transketolases of different species. Biochemistry 35:15865-15869.
    • (1996) Biochemistry , vol.35 , pp. 15865-15869
    • Singleton, C.K.1    Wang, J.J.-L.2    Shen, L.3    Martin, P.R.4
  • 33
    • 0032533694 scopus 로고    scopus 로고
    • The histidine kinase dhkC regulates the choice between migrating slugs and terminal differentiation in Dictyostelium discoideum
    • Singleton, C. K., M. J. Zinda, B. Mykytka, and P. Yang. 1998. The histidine kinase dhkC regulates the choice between migrating slugs and terminal differentiation in Dictyostelium discoideum. Dev. Biol. 203:345-357.
    • (1998) Dev. Biol , vol.203 , pp. 345-357
    • Singleton, C.K.1    Zinda, M.J.2    Mykytka, B.3    Yang, P.4
  • 34
    • 77956832090 scopus 로고
    • Biochemical and genetic methods in the study of cellular slime mold development
    • D. Prescott (ed.), Academic Press, New York, NY
    • Sussman, M. 1966. Biochemical and genetic methods in the study of cellular slime mold development, p. 397-410. In D. Prescott (ed.), Methods of cell physiology. Academic Press, New York, NY.
    • (1966) Methods of Cell Physiology , pp. 397-410
    • Sussman, M.1
  • 35
    • 0027217068 scopus 로고
    • A transformation vector for Dictyostelium discoideum with a new selectable marker Bsr
    • Sutoh, K. A. 1993. A transformation vector for Dictyostelium discoideum with a new selectable marker Bsr. Plasmid 30:150-154.
    • (1993) Plasmid , vol.30 , pp. 150-154
    • Sutoh, K.A.1
  • 36
    • 0035898611 scopus 로고    scopus 로고
    • Heterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR
    • Ung, T. L., C. Cao, J. Lu, K. Ozato, and T. E. Dever. 2001. Heterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR. EMBO J. 20:3728-3737.
    • (2001) EMBO J , vol.20 , pp. 3728-3737
    • Ung, T.L.1    Cao, C.2    Lu, J.3    Ozato, K.4    Dever, T.E.5
  • 37
    • 0002181419 scopus 로고
    • A model of growth and growth control in mathematical terms
    • Weiss, P., and J. L. Kavanau. 1957. A model of growth and growth control in mathematical terms. J. Gen. Physiol. 41:1-41.
    • (1957) J. Gen. Physiol , vol.41 , pp. 1-41
    • Weiss, P.1    Kavanau, J.L.2
  • 38
    • 0024381444 scopus 로고
    • Juxtaposition of domains homologous to protein kinases and histidyl-tRNA synthetases in GCN2 protein suggests a mechanism for coupling GCN4 expression to amino acid availablity
    • Wek, R., B. Jackson, and A. Hinnebusch. 1989. Juxtaposition of domains homologous to protein kinases and histidyl-tRNA synthetases in GCN2 protein suggests a mechanism for coupling GCN4 expression to amino acid availablity. Proc. Natl. Acad. Sci. U.S.A. 86:4579-4583.
    • (1989) Proc. Natl. Acad. Sci. U.S.A , vol.86 , pp. 4579-4583
    • Wek, R.1    Jackson, B.2    Hinnebusch, A.3
  • 39
    • 77953565102 scopus 로고    scopus 로고
    • The GCN2-ATF4 pathway is critical for tumour cell survival and proliferation in response to nutrient deprivation
    • Ye, J., et al. 2010. The GCN2-ATF4 pathway is critical for tumour cell survival and proliferation in response to nutrient deprivation. EMBO J. 29:2082-2096.
    • (2010) EMBO J , vol.29 , pp. 2082-2096
    • Ye, J.1
  • 40
    • 0010729648 scopus 로고
    • Studies of H7 gene function and regulation of its expression by a bidirectional promoter in Dictyostelium discoideum
    • Van-derbilt University, Nashville, TN.
    • Zhang, Q. 1995. Studies of H7 gene function and regulation of its expression by a bidirectional promoter in Dictyostelium discoideum. Ph.D. thesis. Van-derbilt University, Nashville, TN.
    • (1995) Ph.D. Thesis
    • Zhang, Q.1


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