메뉴 건너뛰기




Volumn 15, Issue 12, 1996, Pages 3028-3039

Oligomerization phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus

Author keywords

BiP; PDI; S.cerevisiae; Transmembrane receptor; Unfolded protein response

Indexed keywords

EUKARYOTA;

EID: 0029903049     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00666.x     Document Type: Article
Times cited : (466)

References (32)
  • 1
    • 0025998840 scopus 로고
    • Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates
    • Boyle,W.J., Van Der Geer,P. and Hunter,T. (1991) Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. Methods Enzymol., 201, 110-149.
    • (1991) Methods Enzymol. , vol.201 , pp. 110-149
    • Boyle, W.J.1    Van Der Geer, P.2    Hunter, T.3
  • 2
    • 0023652328 scopus 로고
    • Cell cycle control of the yeast HO gene: Cis- And trans-acting regulators
    • Breeden,L. and Nasmyth,K. (1987) Cell cycle control of the yeast HO gene: cis-and trans-acting regulators. Cell, 48, 389-397.
    • (1987) Cell , vol.48 , pp. 389-397
    • Breeden, L.1    Nasmyth, K.2
  • 3
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • Cox,J.S., Shamu,C.E. and Walter,P. (1993) Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell, 73, 1197-1206.
    • (1993) Cell , vol.73 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 5
    • 0028173316 scopus 로고
    • TGF-β-receptor-mediated signaling
    • Derynck,R. (1994) TGF-β-receptor-mediated signaling. Trends Biochem. Sci., 19, 548-553.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 548-553
    • Derynck, R.1
  • 6
    • 0022494971 scopus 로고
    • Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose
    • Ellis,L., Clauser,E., Morgan,D.O., Edery,M. Roth,R.R. and Rutter,W.J. (1986) Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose. Cell, 45, 721-732.
    • (1986) Cell , vol.45 , pp. 721-732
    • Ellis, L.1    Clauser, E.2    Morgan, D.O.3    Edery, M.4    Roth, R.R.5    Rutter, W.J.6
  • 7
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz,R.D. and Sugino,A. (1988) New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene, 74, 527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 8
    • 0029020282 scopus 로고
    • The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks,S.K. and Hunter,T. (1995) The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J., 9, 576-596.
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 9
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • Hanks,S.K., Quinn,A.M. and Hunter,T. (1988) The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science, 241, 42-52.
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 10
    • 0025949923 scopus 로고
    • The signal recognition particle in S.cerevisiae
    • Hann,B.C. and Walter,P. (1991) The signal recognition particle in S.cerevisiae. Cell, 67, 131-144.
    • (1991) Cell , vol.67 , pp. 131-144
    • Hann, B.C.1    Walter, P.2
  • 11
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin,C.-H. (1995) Dimerization of cell surface receptors in signal transduction. Cell. 80, 213-223.
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.-H.1
  • 12
    • 0028567874 scopus 로고
    • Constitutive activation of Mek1 by mutation of serine phosphorylation site
    • Huang,W. and Erikson,R.L. (1994) Constitutive activation of Mek1 by mutation of serine phosphorylation site. Proc. Natl Acad. Sci. USA, 91, 8960-8963.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 8960-8963
    • Huang, W.1    Erikson, R.L.2
  • 13
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the human insulin receptor
    • Hubbard,S.R., Wei,L., Ellis,L. and Hendrickson,W.A. (1994) Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature. 372, 746-754.
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 14
    • 0027465942 scopus 로고
    • The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum
    • Kohno,K., Normington,K., Sambrook,J., Gething,M.-J. and Mori,K. (1993) The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum. Mol. Cell. Biol., 13, 877-890.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 877-890
    • Kohno, K.1    Normington, K.2    Sambrook, J.3    Gething, M.-J.4    Mori, K.5
  • 15
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel,T.A., Roberts,J.D. and Zakour,R.A. (1987) Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol., 154, 367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 16
    • 0028179120 scopus 로고
    • The TGF-β family and its composite receptors
    • Massague, J., Attisano,L. and Wrana,J.L. (1994) The TGF-β family and its composite receptors. Trends Cell Biol., 4, 172-178.
    • (1994) Trends Cell Biol. , vol.4 , pp. 172-178
    • Massague, J.1    Attisano, L.2    Wrana, J.L.3
  • 17
    • 0028077034 scopus 로고
    • The cellular response to unfolded proteins: Intercompartmental signaling
    • McMillan,D.R., Gething,M.-J. and Sambrook,J. (1994) The cellular response to unfolded proteins: intercompartmental signaling. Curr. Opin. Biotechnol., 5, 540-545.
    • (1994) Curr. Opin. Biotechnol. , vol.5 , pp. 540-545
    • McMillan, D.R.1    Gething, M.-J.2    Sambrook, J.3
  • 18
    • 0028271690 scopus 로고
    • Protein kinase regulation: Insights from crystal structure analysis
    • Morgan,D.O. and De Bondt,H.L. (1994) Protein kinase regulation: insights from crystal structure analysis. Curr. Opin. Cell Biol., 6, 239-246.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 239-246
    • Morgan, D.O.1    De Bondt, H.L.2
  • 19
    • 0026628290 scopus 로고
    • A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins
    • Mori,K., Sant,A., Kohno,K., Normington,K., Gething,M.-J. and Sambrook,J.F (1992) A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins. EMBO J., 11, 2583-2593.
    • (1992) EMBO J. , vol.11 , pp. 2583-2593
    • Mori, K.1    Sant, A.2    Kohno, K.3    Normington, K.4    Gething, M.-J.5    Sambrook, J.F.6
  • 20
    • 0027305620 scopus 로고
    • A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus
    • Mori,K., Ma,W., Gething,M.-J. and Sambrook,J. (1993) A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus. Cell, 74, 743-756.
    • (1993) Cell , vol.74 , pp. 743-756
    • Mori, K.1    Ma, W.2    Gething, M.-J.3    Sambrook, J.4
  • 21
    • 0009353304 scopus 로고
    • Isolation and sequence of the gene for actin in Saccharomyces cerevisiae
    • Ng,R. and Abelson,J. (1980) Isolation and sequence of the gene for actin in Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA, 77, 3912-3916.
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 3912-3916
    • Ng, R.1    Abelson, J.2
  • 22
    • 0026710871 scopus 로고
    • IRE1 encodes a putative protein kinase containing a membrane-spanning domain and is required for inositol phototrophy in Saccharomyces cerevisiae
    • Nikawa,J.I. and Yamashita,S. (1992) IRE1 encodes a putative protein kinase containing a membrane-spanning domain and is required for inositol phototrophy in Saccharomyces cerevisiae. Mol. Microbiol., 6, 1441-1446.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1441-1446
    • Nikawa, J.I.1    Yamashita, S.2
  • 23
    • 0026671589 scopus 로고
    • Possible cross-regulation of phosphate and sulfate metabolism in Saccharomyces cerevisiae
    • O'Connell,K.F. and Baker,R.E. (1992) Possible cross-regulation of phosphate and sulfate metabolism in Saccharomyces cerevisiae. Genetics, 132, 63-73.
    • (1992) Genetics , vol.132 , pp. 63-73
    • O'Connell, K.F.1    Baker, R.E.2
  • 24
    • 0028084733 scopus 로고
    • The unfolded-protein-response-pathway in yeast
    • Shamu,C.E., Cox,J.S. and Walter,P. (1994) The unfolded-protein-response-pathway in yeast. Trends Cell Biol., 4, 56-60.
    • (1994) Trends Cell Biol. , vol.4 , pp. 56-60
    • Shamu, C.E.1    Cox, J.S.2    Walter, P.3
  • 25
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski,R.S. and Hieter,P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics, 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 26
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith,D.B. and Johnson,K.S. (1988) Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene, 67, 31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 27
    • 0022808489 scopus 로고
    • Mr 26,000 antigen of Schistosoma japonicum recognized by resistant WEHI 129/J mice is a parasite glutathione S-transferase
    • Smith,D.B., Davern,K.M., Board,P.G., Tiu,W.U., Garcia,E.G. and Mitchell,G.F. (1986) Mr 26,000 antigen of Schistosoma japonicum recognized by resistant WEHI 129/J mice is a parasite glutathione S-transferase. Proc. Natl Acad. Sci. USA, 83, 8703-8707.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 8703-8707
    • Smith, D.B.1    Davern, K.M.2    Board, P.G.3    Tiu, W.U.4    Garcia, E.G.5    Mitchell, G.F.6
  • 28
    • 0000967627 scopus 로고
    • A kinase that responds to stress
    • Sweet,D.J. (1993) A kinase that responds to stress. Curr. Biol., 3, 622-624.
    • (1993) Curr. Biol. , vol.3 , pp. 622-624
    • Sweet, D.J.1
  • 29
    • 0023834406 scopus 로고
    • A cascade of tyrosine autophosphorylation in the β-subunit activates the phosphotransferase of the insulin receptor
    • White,M.F., Shoelson,S.E., Keutmann,H. and Kahn,C.R. (1988) A cascade of tyrosine autophosphorylation in the β-subunit activates the phosphotransferase of the insulin receptor. J. Biol. Chem., 263, 2969-2980.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2969-2980
    • White, M.F.1    Shoelson, S.E.2    Keutmann, H.3    Kahn, C.R.4
  • 30
    • 0028295681 scopus 로고
    • 2.2 Mb of contiguous nucleotide sequence from chromosome III of C.elegans
    • Wilson,R. et al. (1994) 2.2 Mb of contiguous nucleotide sequence from chromosome III of C.elegans. Nature. 368, 32-38.
    • (1994) Nature , vol.368 , pp. 32-38
    • Wilson, R.1
  • 32
    • 0028157664 scopus 로고
    • Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution
    • Zhang,F. Strand,A., Robbins,D., Cobb,M. and Goldsmith,E. (1994) Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution. Nature, 367, 704-711.
    • (1994) Nature , vol.367 , pp. 704-711
    • Zhang, F.1    Strand, A.2    Robbins, D.3    Cobb, M.4    Goldsmith, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.