메뉴 건너뛰기




Volumn 113, Issue 40, 2016, Pages E5886-E5895

Autonomous translational pausing is required for XBP1u mRNA recruitment to the ER via the SRP pathway

Author keywords

SRP; Translational pausing; Translocon; Unfolded protein response; XBP1 mRNA

Indexed keywords

MESSENGER RNA; TRANSLOCON; X BOX BINDING PROTEIN 1; PROTEIN BINDING; SIGNAL RECOGNITION PARTICLE;

EID: 84989957603     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1604435113     Document Type: Article
Times cited : (50)

References (40)
  • 1
    • 0019822645 scopus 로고
    • Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes
    • Walter P, Blobel G (1981) Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes. J Cell Biol 91(2 Pt 1):557-561.
    • (1981) J Cell Biol , vol.91 , Issue.2 , pp. 557-561
    • Walter, P.1    Blobel, G.2
  • 2
    • 84878941023 scopus 로고    scopus 로고
    • Signal recognition particle: An essential protein-targeting machine
    • Akopian D, Shen K, Zhang X, Shan SO (2013) Signal recognition particle: An essential protein-targeting machine. Annu Rev Biochem 82:693-721.
    • (2013) Annu Rev Biochem , vol.82 , pp. 693-721
    • Akopian, D.1    Shen, K.2    Zhang, X.3    Shan, S.O.4
  • 4
    • 42949161206 scopus 로고    scopus 로고
    • SRP keeps polypeptides translocation-competent by slowing translation to match limiting ER-targeting sites
    • Lakkaraju AK, Mary C, Scherrer A, Johnson AE, Strub K (2008) SRP keeps polypeptides translocation-competent by slowing translation to match limiting ER-targeting sites. Cell 133(3):440-451.
    • (2008) Cell , vol.133 , Issue.3 , pp. 440-451
    • Lakkaraju, A.K.1    Mary, C.2    Scherrer, A.3    Johnson, A.E.4    Strub, K.5
  • 5
    • 1542319100 scopus 로고    scopus 로고
    • Structure of the signal recognition particle interacting with the elongation-arrested ribosome
    • Halic M, et al. (2004) Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Nature 427(6977):808-814.
    • (2004) Nature , vol.427 , Issue.6977 , pp. 808-814
    • Halic, M.1
  • 6
    • 84861361690 scopus 로고    scopus 로고
    • Mechanisms of Sec61/SecY-mediated protein translocation across membranes
    • Park E, Rapoport TA (2012) Mechanisms of Sec61/SecY-mediated protein translocation across membranes. Annu Rev Biophys 41:21-40.
    • (2012) Annu Rev Biophys , vol.41 , pp. 21-40
    • Park, E.1    Rapoport, T.A.2
  • 7
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething MJ, Sambrook J (1992) Protein folding in the cell. Nature 355(6355):33-45.
    • (1992) Nature , vol.355 , Issue.6355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 8
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D, Walter P (2007) Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 8(7):519-529.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , Issue.7 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 9
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter P, Ron D (2011) The unfolded protein response: from stress pathway to homeostatic regulation. Science 334(6059):1081-1086.
    • (2011) Science , vol.334 , Issue.6059 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 10
    • 71949098172 scopus 로고    scopus 로고
    • Signalling pathways in the unfolded protein response: Development from yeast to mammals
    • Mori K (2009) Signalling pathways in the unfolded protein response: Development from yeast to mammals. J Biochem 146(6):743-750.
    • (2009) J Biochem , vol.146 , Issue.6 , pp. 743-750
    • Mori, K.1
  • 11
    • 35348967427 scopus 로고    scopus 로고
    • Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins
    • Kimata Y, et al. (2007) Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins. J Cell Biol 179(1):75-86.
    • (2007) J Cell Biol , vol.179 , Issue.1 , pp. 75-86
    • Kimata, Y.1
  • 12
    • 77958016968 scopus 로고    scopus 로고
    • Mammalian endoplasmic reticulum stress sensor IRE1 signals by dynamic clustering
    • Li H, Korennykh AV, Behrman SL, Walter P (2010) Mammalian endoplasmic reticulum stress sensor IRE1 signals by dynamic clustering. Proc Natl Acad Sci USA 107(37):16113-16118.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.37 , pp. 16113-16118
    • Li, H.1    Korennykh, A.V.2    Behrman, S.L.3    Walter, P.4
  • 13
    • 75649118565 scopus 로고    scopus 로고
    • Stress-sensing mechanisms in the unfolded protein response: Similarities and differences between yeast and mammals
    • Kohno K (2010) Stress-sensing mechanisms in the unfolded protein response: Similarities and differences between yeast and mammals. J Biochem 147(1):27-33.
    • (2010) J Biochem , vol.147 , Issue.1 , pp. 27-33
    • Kohno, K.1
  • 14
    • 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, Mori K (2001) XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 107(7):881-891.
    • (2001) Cell , vol.107 , Issue.7 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 15
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • Calfon M, et al. (2002) IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 415(6867):92-96.
    • (2002) Nature , vol.415 , Issue.6867 , pp. 92-96
    • Calfon, M.1
  • 16
    • 84926106643 scopus 로고    scopus 로고
    • A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB
    • Lu Y, Liang FX, Wang X (2014) A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB. Mol Cell 55(5):758-770.
    • (2014) Mol Cell , vol.55 , Issue.5 , pp. 758-770
    • Lu, Y.1    Liang, F.X.2    Wang, X.3
  • 17
    • 84918823958 scopus 로고    scopus 로고
    • The mammalian tRNA ligase complex mediates splicing of XBP1 mRNA and controls antibody secretion in plasma cells
    • Jurkin J, et al. (2014) The mammalian tRNA ligase complex mediates splicing of XBP1 mRNA and controls antibody secretion in plasma cells. EMBO J 33(24):2922-2936.
    • (2014) EMBO J , vol.33 , Issue.24 , pp. 2922-2936
    • Jurkin, J.1
  • 18
    • 84915814883 scopus 로고    scopus 로고
    • The RtcB RNA ligase is an essential component of the metazoan unfolded protein response
    • Kosmaczewski SG, et al. (2014) The RtcB RNA ligase is an essential component of the metazoan unfolded protein response. EMBO Rep 15(12):1278-1285.
    • (2014) EMBO Rep , vol.15 , Issue.12 , pp. 1278-1285
    • Kosmaczewski, S.G.1
  • 19
    • 79960272681 scopus 로고    scopus 로고
    • Reconstitution and characterization of the unconventional splicing of XBP1u mRNA in vitro
    • Shinya S, et al. (2011) Reconstitution and characterization of the unconventional splicing of XBP1u mRNA in vitro. Nucleic Acids Res 39(12):5245-5254.
    • (2011) Nucleic Acids Res , vol.39 , Issue.12 , pp. 5245-5254
    • Shinya, S.1
  • 20
    • 0037320265 scopus 로고    scopus 로고
    • A time-dependent phase shift in the mammalian unfolded protein response
    • Yoshida H, et al. (2003) A time-dependent phase shift in the mammalian unfolded protein response. Dev Cell 4(2):265-271.
    • (2003) Dev Cell , vol.4 , Issue.2 , pp. 265-271
    • Yoshida, H.1
  • 21
    • 64749103329 scopus 로고    scopus 로고
    • Cotranslational targeting of XBP1 protein to the membrane promotes cytoplasmic splicing of its own mRNA
    • Yanagitani K, et al. (2009) Cotranslational targeting of XBP1 protein to the membrane promotes cytoplasmic splicing of its own mRNA. Mol Cell 34(2):191-200.
    • (2009) Mol Cell , vol.34 , Issue.2 , pp. 191-200
    • Yanagitani, K.1
  • 22
    • 79551629027 scopus 로고    scopus 로고
    • Translational pausing ensures membrane targeting and cytoplasmic splicing of XBP1u mRNA
    • Yanagitani K, Kimata Y, Kadokura H, Kohno K (2011) Translational pausing ensures membrane targeting and cytoplasmic splicing of XBP1u mRNA. Science 331(6017):586-589.
    • (2011) Science , vol.331 , Issue.6017 , pp. 586-589
    • Yanagitani, K.1    Kimata, Y.2    Kadokura, H.3    Kohno, K.4
  • 24
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • Nagai T, et al. (2002) A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat Biotechnol 20(1):87-90.
    • (2002) Nat Biotechnol , vol.20 , Issue.1 , pp. 87-90
    • Nagai, T.1
  • 25
    • 0037189518 scopus 로고    scopus 로고
    • Endoplasmic reticulum-bound ribosomes reside in stable association with the translocon following termination of protein synthesis
    • Potter MD, Nicchitta CV (2002) Endoplasmic reticulum-bound ribosomes reside in stable association with the translocon following termination of protein synthesis. J Biol Chem 277(26):23314-23320.
    • (2002) J Biol Chem , vol.277 , Issue.26 , pp. 23314-23320
    • Potter, M.D.1    Nicchitta, C.V.2
  • 26
    • 0009499348 scopus 로고
    • Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum
    • Walter P, Blobel G (1980) Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum. Proc Natl Acad Sci USA 77(12):7112-7116.
    • (1980) Proc Natl Acad Sci USA , vol.77 , Issue.12 , pp. 7112-7116
    • Walter, P.1    Blobel, G.2
  • 27
    • 0034672006 scopus 로고    scopus 로고
    • In vivo kinetics of protein targeting to the endoplasmic reticulum determined by site-specific phosphorylation
    • Goder V, Crottet P, Spiess M (2000) In vivo kinetics of protein targeting to the endoplasmic reticulum determined by site-specific phosphorylation. EMBO J 19(24):6704-6712.
    • (2000) EMBO J , vol.19 , Issue.24 , pp. 6704-6712
    • Goder, V.1    Crottet, P.2    Spiess, M.3
  • 28
    • 81055155799 scopus 로고    scopus 로고
    • Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes
    • Ingolia NT, Lareau LF, Weissman JS (2011) Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes. Cell 147(4):789-802.
    • (2011) Cell , vol.147 , Issue.4 , pp. 789-802
    • Ingolia, N.T.1    Lareau, L.F.2    Weissman, J.S.3
  • 29
    • 0025762681 scopus 로고
    • Requirements for the membrane insertion of signal-anchor type proteins
    • High S, Flint N, Dobberstein B (1991) Requirements for the membrane insertion of signal-anchor type proteins. J Cell Biol 113(1):25-34.
    • (1991) J Cell Biol , vol.113 , Issue.1 , pp. 25-34
    • High, S.1    Flint, N.2    Dobberstein, B.3
  • 30
    • 0141992130 scopus 로고    scopus 로고
    • Cotranslational protein integration into the ER membrane is mediated by the binding of nascent chains to translocon proteins
    • McCormick PJ, Miao Y, Shao Y, Lin J, Johnson AE (2003) Cotranslational protein integration into the ER membrane is mediated by the binding of nascent chains to translocon proteins. Mol Cell 12(2):329-341.
    • (2003) Mol Cell , vol.12 , Issue.2 , pp. 329-341
    • McCormick, P.J.1    Miao, Y.2    Shao, Y.3    Lin, J.4    Johnson, A.E.5
  • 31
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki Y, Hubbard AL, Fowler S, Lazarow PB (1982) Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J Cell Biol 93(1):97-102.
    • (1982) J Cell Biol , vol.93 , Issue.1 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 32
    • 0029096050 scopus 로고
    • A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane
    • Jungnickel B, Rapoport TA (1995) A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane. Cell 82(2):261-270.
    • (1995) Cell , vol.82 , Issue.2 , pp. 261-270
    • Jungnickel, B.1    Rapoport, T.A.2
  • 33
    • 84895538371 scopus 로고    scopus 로고
    • Minimal, encapsulated proteomic-sample processing applied to copy-number estimation in eukaryotic cells
    • Kulak NA, Pichler G, Paron I, Nagaraj N, Mann M (2014) Minimal, encapsulated proteomic-sample processing applied to copy-number estimation in eukaryotic cells. Nat Methods 11(3):319-324.
    • (2014) Nat Methods , vol.11 , Issue.3 , pp. 319-324
    • Kulak, N.A.1    Pichler, G.2    Paron, I.3    Nagaraj, N.4    Mann, M.5
  • 34
    • 84930649002 scopus 로고    scopus 로고
    • A functional link between the co-translational protein translocation pathway and the UPR
    • Plumb R, Zhang ZR, Appathurai S, Mariappan M (2015) A functional link between the co-translational protein translocation pathway and the UPR. eLife 4:e07426.
    • (2015) eLife , vol.4
    • Plumb, R.1    Zhang, Z.R.2    Appathurai, S.3    Mariappan, M.4
  • 35
    • 84925553022 scopus 로고    scopus 로고
    • Local slowdown of translation by nonoptimal codons promotes nascent-chain recognition by SRP in vivo
    • Pechmann S, Chartron JW, Frydman J (2014) Local slowdown of translation by nonoptimal codons promotes nascent-chain recognition by SRP in vivo. Nat Struct Mol Biol 21(12):1100-1105.
    • (2014) Nat Struct Mol Biol , vol.21 , Issue.12 , pp. 1100-1105
    • Pechmann, S.1    Chartron, J.W.2    Frydman, J.3
  • 36
    • 84909607974 scopus 로고    scopus 로고
    • Principles of ER cotranslational translocation revealed by proximity-specific ribosome profiling
    • Jan CH, Williams CC, Weissman JS (2014) Principles of ER cotranslational translocation revealed by proximity-specific ribosome profiling. Science 346(6210):1257521.
    • (2014) Science , vol.346 , Issue.6210
    • Jan, C.H.1    Williams, C.C.2    Weissman, J.S.3
  • 37
    • 84922219279 scopus 로고    scopus 로고
    • Signal peptide peptidase functions in ERAD to cleave the unfolded protein response regulator XBP1u
    • Chen CY, et al. (2014) Signal peptide peptidase functions in ERAD to cleave the unfolded protein response regulator XBP1u. EMBO J 33(21):2492-2506.
    • (2014) EMBO J , vol.33 , Issue.21 , pp. 2492-2506
    • Chen, C.Y.1
  • 38
    • 84892779367 scopus 로고    scopus 로고
    • Heat shock transcription factor σ32 co-opts the signal recognition particle to regulate protein homeostasis in E. coli
    • Lim B, et al. (2013) Heat shock transcription factor σ32 co-opts the signal recognition particle to regulate protein homeostasis in E. coli. PLoS Biol 11(12):e1001735.
    • (2013) PLoS Biol , vol.11 , Issue.12
    • Lim, B.1
  • 39
    • 33750295885 scopus 로고    scopus 로고
    • Transfection of mammalian cells using linear polyethylenimine is a simple and effective means of producing recombinant adeno-associated virus vectors
    • Reed SE, Staley EM, Mayginnes JP, Pintel DJ, Tullis GE (2006) Transfection of mammalian cells using linear polyethylenimine is a simple and effective means of producing recombinant adeno-associated virus vectors. J Virol Methods 138(1-2):85-98.
    • (2006) J Virol Methods , vol.138 , Issue.1-2 , pp. 85-98
    • Reed, S.E.1    Staley, E.M.2    Mayginnes, J.P.3    Pintel, D.J.4    Tullis, G.E.5
  • 40
    • 51749085388 scopus 로고    scopus 로고
    • HELIQUEST: A web server to screen sequences with specific alpha-helical properties
    • Gautier R, Douguet D, Antonny B, Drin G (2008) HELIQUEST: A web server to screen sequences with specific alpha-helical properties. Bioinformatics 24(18):2101-2102.
    • (2008) Bioinformatics , vol.24 , Issue.18 , pp. 2101-2102
    • Gautier, R.1    Douguet, D.2    Antonny, B.3    Drin, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.