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Volumn 132, Issue 1, 2008, Pages 89-100

Structure of the Dual Enzyme Ire1 Reveals the Basis for Catalysis and Regulation in Nonconventional RNA Splicing

Author keywords

PROTEINS; RNA; SIGNALING

Indexed keywords

NUCLEOTIDE; PROTEIN IRE1; PROTEIN KINASE; RIBONUCLEASE; RIBONUCLEASE L;

EID: 37649004940     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2007.10.057     Document Type: Article
Times cited : (305)

References (41)
  • 1
    • 33751159209 scopus 로고    scopus 로고
    • Intracellular signaling by the unfolded protein response
    • Bernales S., Papa F.R., and Walter P. Intracellular signaling by the unfolded protein response. Annu. Rev. Cell Dev. Biol. 22 (2006) 487-508
    • (2006) Annu. Rev. Cell Dev. Biol. , vol.22 , pp. 487-508
    • Bernales, S.1    Papa, F.R.2    Walter, P.3
  • 3
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • Calfon M., Zeng H., Urano F., Till J.H., Hubbard S.R., Harding H.P., Clark S.G., and Ron D. IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 415 (2002) 92-96
    • (2002) Nature , vol.415 , pp. 92-96
    • Calfon, M.1    Zeng, H.2    Urano, F.3    Till, J.H.4    Hubbard, S.R.5    Harding, H.P.6    Clark, S.G.7    Ron, D.8
  • 5
    • 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. Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 73 (1993) 1197-1206
    • (1993) Cell , vol.73 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 8
    • 25144477805 scopus 로고    scopus 로고
    • Mechanistic link between PKR dimerization, autophosphorylation, and eIF2alpha substrate recognition
    • Dey M., Cao C., Dar A.C., Tamura T., Ozato K., Sicheri F., and Dever T.E. Mechanistic link between PKR dimerization, autophosphorylation, and eIF2alpha substrate recognition. Cell 122 (2005) 901-913
    • (2005) Cell , vol.122 , pp. 901-913
    • Dey, M.1    Cao, C.2    Dar, A.C.3    Tamura, T.4    Ozato, K.5    Sicheri, F.6    Dever, T.E.7
  • 9
    • 0035028045 scopus 로고    scopus 로고
    • Basis for regulated RNA cleavage by functional analysis of RNase L and Ire1p
    • Dong B., Niwa M., Walter P., and Silverman R.H. Basis for regulated RNA cleavage by functional analysis of RNase L and Ire1p. RNA 7 (2001) 361-373
    • (2001) RNA , vol.7 , pp. 361-373
    • Dong, B.1    Niwa, M.2    Walter, P.3    Silverman, R.H.4
  • 10
    • 0028909072 scopus 로고
    • 2-5A-dependent RNase molecules dimerize during activation by 2-5A
    • Dong B., and Silverman R.H. 2-5A-dependent RNase molecules dimerize during activation by 2-5A. J. Biol. Chem. 270 (1995) 4133-4137
    • (1995) J. Biol. Chem. , vol.270 , pp. 4133-4137
    • Dong, B.1    Silverman, R.H.2
  • 13
    • 0019794540 scopus 로고
    • Interferon action: RNA cleavage pattern of a (2′-5′)oligoadenylate-dependent endonuclease
    • Floyd-Smith G., Slattery E., and Lengyel P. Interferon action: RNA cleavage pattern of a (2′-5′)oligoadenylate-dependent endonuclease. Science 212 (1981) 1030-1032
    • (1981) Science , vol.212 , pp. 1030-1032
    • Floyd-Smith, G.1    Slattery, E.2    Lengyel, P.3
  • 14
    • 33745253917 scopus 로고    scopus 로고
    • A conserved dimer and global conformational changes in the structure of apo-PknE Ser/Thr protein kinase from Mycobacterium tuberculosis
    • Gay L.M., Ng H.L., and Alber T. A conserved dimer and global conformational changes in the structure of apo-PknE Ser/Thr protein kinase from Mycobacterium tuberculosis. J. Mol. Biol. 360 (2006) 409-420
    • (2006) J. Mol. Biol. , vol.360 , pp. 409-420
    • Gay, L.M.1    Ng, H.L.2    Alber, T.3
  • 15
    • 0033152626 scopus 로고    scopus 로고
    • Mechanism of non-spliceosomal mRNA splicing in the unfolded protein response pathway
    • Gonzalez T.N., Sidrauski C., Dorfler S., and Walter P. Mechanism of non-spliceosomal mRNA splicing in the unfolded protein response pathway. EMBO J. 18 (1999) 3119-3132
    • (1999) EMBO J. , vol.18 , pp. 3119-3132
    • Gonzalez, T.N.1    Sidrauski, C.2    Dorfler, S.3    Walter, P.4
  • 17
    • 85047696182 scopus 로고    scopus 로고
    • Allosteric activation by dimerization of the PknD receptor Ser/Thr protein kinase from Mycobacterium tuberculosis
    • Greenstein A.E., Echols N., Lombana T.N., King D.S., and Alber T. Allosteric activation by dimerization of the PknD receptor Ser/Thr protein kinase from Mycobacterium tuberculosis. J. Biol. Chem. 282 (2007) 11427-11435
    • (2007) J. Biol. Chem. , vol.282 , pp. 11427-11435
    • Greenstein, A.E.1    Echols, N.2    Lombana, T.N.3    King, D.S.4    Alber, T.5
  • 18
    • 0028871926 scopus 로고
    • Dali: a network tool for protein structure comparison
    • Holm L., and Sander C. Dali: a network tool for protein structure comparison. Trends Biochem. Sci. 20 (1995) 478-480
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 19
    • 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. Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 372 (1994) 746-754
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 20
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M., and Kuriyan J. The conformational plasticity of protein kinases. Cell 109 (2002) 275-282
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 21
    • 8444250981 scopus 로고    scopus 로고
    • A role for BiP as an adjustor for the endoplasmic reticulum stress-sensing protein Ire1
    • Kimata Y., Oikawa D., Shimizu Y., Ishiwata-Kimata Y., and Kohno K. A role for BiP as an adjustor for the endoplasmic reticulum stress-sensing protein Ire1. J. Cell Biol. 167 (2004) 445-456
    • (2004) J. Cell Biol. , vol.167 , pp. 445-456
    • Kimata, Y.1    Oikawa, D.2    Shimizu, Y.3    Ishiwata-Kimata, Y.4    Kohno, K.5
  • 22
    • 0037083755 scopus 로고    scopus 로고
    • IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response
    • Lee K., Tirasophon W., Shen X., Michalak M., Prywes R., Okada T., Yoshida H., Mori K., and Kaufman R.J. IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response. Genes Dev. 16 (2002) 452-466
    • (2002) Genes Dev. , vol.16 , pp. 452-466
    • Lee, K.1    Tirasophon, W.2    Shen, X.3    Michalak, M.4    Prywes, R.5    Okada, T.6    Yoshida, H.7    Mori, K.8    Kaufman, R.J.9
  • 23
    • 0028838717 scopus 로고
    • Threading a database of protein cores
    • Madej T., Gibrat J.F., and Bryant S.H. Threading a database of protein cores. Proteins 23 (1995) 356-369
    • (1995) Proteins , vol.23 , pp. 356-369
    • Madej, T.1    Gibrat, J.F.2    Bryant, S.H.3
  • 24
    • 0042812063 scopus 로고    scopus 로고
    • Frame switch splicing and regulated intramembrane proteolysis: key words to understand the unfolded protein response
    • Mori K. Frame switch splicing and regulated intramembrane proteolysis: key words to understand the unfolded protein response. Traffic 4 (2003) 519-528
    • (2003) Traffic , vol.4 , pp. 519-528
    • Mori, K.1
  • 25
    • 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. A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus. Cell 74 (1993) 743-756
    • (1993) Cell , vol.74 , pp. 743-756
    • Mori, K.1    Ma, W.2    Gething, M.J.3    Sambrook, J.4
  • 26
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases; controlling activity through activation segment conformation
    • Nolen B., Taylor S., and Ghosh G. Regulation of protein kinases; controlling activity through activation segment conformation. Mol. Cell 15 (2004) 661-675
    • (2004) Mol. Cell , vol.15 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 27
    • 0037969625 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis
    • Ortiz-Lombardia M., Pompeo F., Boitel B., and Alzari P.M. Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis. J. Biol. Chem. 278 (2003) 13094-13100
    • (2003) J. Biol. Chem. , vol.278 , pp. 13094-13100
    • Ortiz-Lombardia, M.1    Pompeo, F.2    Boitel, B.3    Alzari, P.M.4
  • 28
    • 0344395603 scopus 로고    scopus 로고
    • Bypassing a kinase activity with an ATP-competitive drug
    • Papa F.R., Zhang C., Shokat K., and Walter P. Bypassing a kinase activity with an ATP-competitive drug. Science 302 (2003) 1533-1537
    • (2003) Science , vol.302 , pp. 1533-1537
    • Papa, F.R.1    Zhang, C.2    Shokat, K.3    Walter, P.4
  • 29
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D., and Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8 (2007) 519-529
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 31
    • 0029903049 scopus 로고    scopus 로고
    • Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus
    • Shamu C.E., and Walter P. Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J. 15 (1996) 3028-3039
    • (1996) EMBO J. , vol.15 , pp. 3028-3039
    • Shamu, C.E.1    Walter, P.2
  • 32
    • 0030297538 scopus 로고    scopus 로고
    • tRNA ligase is required for regulated mRNA splicing in the unfolded protein response
    • Sidrauski C., Cox J.S., and Walter P. tRNA ligase is required for regulated mRNA splicing in the unfolded protein response. Cell 87 (1996) 405-413
    • (1996) Cell , vol.87 , pp. 405-413
    • Sidrauski, C.1    Cox, J.S.2    Walter, P.3
  • 33
    • 0030954870 scopus 로고    scopus 로고
    • The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response
    • Sidrauski C., and Walter P. The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response. Cell 90 (1997) 1031-1039
    • (1997) Cell , vol.90 , pp. 1031-1039
    • Sidrauski, C.1    Walter, P.2
  • 34
    • 0347383761 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: automated structure solution and density modification
    • Terwilliger T.C. SOLVE and RESOLVE: automated structure solution and density modification. Methods Enzymol. 374 (2003) 22-37
    • (2003) Methods Enzymol. , vol.374 , pp. 22-37
    • Terwilliger, T.C.1
  • 35
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers K.J., Patil C.K., Wodicka L., Lockhart D.J., Weissman J.S., and Walter P. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101 (2000) 249-258
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3    Lockhart, D.J.4    Weissman, J.S.5    Walter, P.6
  • 37
    • 0029892851 scopus 로고    scopus 로고
    • The unfolded protein response pathway in Saccharomyces cerevisiae. Oligomerization and trans-phosphorylation of Ire1p (Ern1p) are required for kinase activation
    • Welihinda A.A., and Kaufman R.J. The unfolded protein response pathway in Saccharomyces cerevisiae. Oligomerization and trans-phosphorylation of Ire1p (Ern1p) are required for kinase activation. J. Biol. Chem. 271 (1996) 18181-18187
    • (1996) J. Biol. Chem. , vol.271 , pp. 18181-18187
    • Welihinda, A.A.1    Kaufman, R.J.2
  • 38
    • 33646538487 scopus 로고    scopus 로고
    • RNA recognition and cleavage by a splicing endonuclease
    • Xue S., Calvin K., and Li H. RNA recognition and cleavage by a splicing endonuclease. Science 312 (2006) 906-910
    • (2006) Science , vol.312 , pp. 906-910
    • Xue, S.1    Calvin, K.2    Li, H.3
  • 39
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida H., Matsui T., Yamamoto A., Okada T., and Mori K. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 107 (2001) 881-891
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 40
    • 0037337317 scopus 로고    scopus 로고
    • Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases
    • Young T.A., Delagoutte B., Endrizzi J.A., Falick A.M., and Alber T. Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases. Nat. Struct. Biol. 10 (2003) 168-174
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 168-174
    • Young, T.A.1    Delagoutte, B.2    Endrizzi, J.A.3    Falick, A.M.4    Alber, T.5
  • 41
    • 33749233991 scopus 로고    scopus 로고
    • The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response
    • Zhou J., Liu C.Y., Back S.H., Clark R.L., Peisach D., Xu Z., and Kaufman R.J. The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. Proc. Natl. Acad. Sci. USA 103 (2006) 14343-14348
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 14343-14348
    • Zhou, J.1    Liu, C.Y.2    Back, S.H.3    Clark, R.L.4    Peisach, D.5    Xu, Z.6    Kaufman, R.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.