메뉴 건너뛰기




Volumn 33, Issue 13, 2013, Pages 2510-2526

Degradation of Newly Synthesized Polypeptides by Ribosome-Associated RACK1/c-Jun N-Terminal Kinase/Eukaryotic Elongation Factor 1A2 Complex

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR; EUKARYOTIC ELONGATION FACTOR 1A2; MITOGEN ACTIVATED PROTEIN KINASE P38; POLYPEPTIDE; RECEPTOR FOR ACTIVATED C KINASE 1; SERINE; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG;

EID: 84880667395     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.01362-12     Document Type: Article
Times cited : (55)

References (62)
  • 1
    • 66849109240 scopus 로고    scopus 로고
    • The ribosome as a platform for cotranslational processing, folding, and targeting of newly synthesized proteins
    • Kramer G, Boehringer D, Ban N, Bukau B. 2009. The ribosome as a platform for cotranslational processing, folding, and targeting of newly synthesized proteins. Nat. Struct. Mol. Biol. 16:589-597.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 589-597
    • Kramer, G.1    Boehringer, D.2    Ban, N.3    Bukau, B.4
  • 2
    • 79957812064 scopus 로고    scopus 로고
    • Birth, life, and death of nascent polypeptide chains
    • Jha S, Komar AA. 2011. Birth, life, and death of nascent polypeptide chains. Biotechnol. J. 6:623-640.
    • (2011) Biotechnol. J. , vol.6
    • Jha, S.1    Komar, A.A.2
  • 3
    • 77956006893 scopus 로고    scopus 로고
    • The three-dimensional organization of polyribosomes in intact human cells
    • Brandt F, Carlson LA, Hartl FU, Baumeister W, Grunewald K. 2010. The three-dimensional organization of polyribosomes in intact human cells. Mol. Cell 39:560-569.
    • (2010) Mol. Cell , vol.39 , pp. 560-569
    • Brandt, F.1    Carlson, L.A.2    Hartl, F.U.3    Baumeister, W.4    Grunewald, K.5
  • 4
    • 0033572725 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on protein folding and aggregation
    • van den Berg B, Ellis RJ, Dobson CM. 1999. Effects of macromolecular crowding on protein folding and aggregation. EMBO J. 18:6927-6933.
    • (1999) EMBO J. , vol.18 , pp. 6927-6933
    • van den Berg, B.1    Ellis, R.J.2    Dobson, C.M.3
  • 5
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by cotranslational folding in eukaryotes
    • Netzer WJ, Hartl FU. 1997. Recombination of protein domains facilitated by cotranslational folding in eukaryotes. Nature 388:343-349.
    • (1997) Nature , vol.388 , pp. 343-349
    • Netzer, W.J.1    Hartl, F.U.2
  • 6
    • 0033203533 scopus 로고    scopus 로고
    • Cotranslational folding of an alphavirus capsid protein in the cytosol of living cells
    • Nicola AV, Chen W, Helenius A. 1999. Cotranslational folding of an alphavirus capsid protein in the cytosol of living cells. Nat. Cell Biol. 1:341-345.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 341-345
    • Nicola, A.V.1    Chen, W.2    Helenius, A.3
  • 7
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases
    • Sherman MY, Goldberg AL. 2001. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron 29:15-32.
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 8
    • 0027980239 scopus 로고
    • A protein complex required for signal-sequence-specific sorting and translocation
    • Wiedmann B, Sakai H, Davis TA, Wiedmann M. 1994. A protein complex required for signal-sequence-specific sorting and translocation. Nature 370:434-440.
    • (1994) Nature , vol.370 , pp. 434-440
    • Wiedmann, B.1    Sakai, H.2    Davis, T.A.3    Wiedmann, M.4
  • 11
    • 11144342006 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of cotranslationally damaged proteins involves translation elongation factor 1A
    • Chuang SM, Chen L, Lambertson D, Anand M, Kinzy TG, Madura K. 2005. Proteasome-mediated degradation of cotranslationally damaged proteins involves translation elongation factor 1A. Mol. Cell. Biol. 25:403-413.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 403-413
    • Chuang, S.M.1    Chen, L.2    Lambertson, D.3    Anand, M.4    Kinzy, T.G.5    Madura, K.6
  • 12
    • 66849136862 scopus 로고    scopus 로고
    • Nascent peptidedependent translation arrest leads to Not4p-mediated protein degradation by the proteasome
    • Dimitrova LN, Kuroha K, Tatematsu T, Inada T. 2009. Nascent peptidedependent translation arrest leads to Not4p-mediated protein degradation by the proteasome. J. Biol. Chem. 284:10343-10352.
    • (2009) J. Biol Chem. , vol.284 , pp. 10343-10352
    • Dimitrova, L.N.1    Kuroha, K.2    Tatematsu, T.3    Inada, T.4
  • 14
  • 15
    • 0034703437 scopus 로고    scopus 로고
    • Detecting and measuring cotranslational protein degradation in vivo
    • Turner GC, Varshavsky A. 2000. Detecting and measuring cotranslational protein degradation in vivo. Science 289:2117-2120.
    • (2000) Science , vol.289 , pp. 2117-2120
    • Turner, G.C.1    Varshavsky, A.2
  • 16
  • 17
    • 0031825424 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase cascades as regulators of stress responses
    • Karin M. 1998. Mitogen-activated protein kinase cascades as regulators of stress responses. Ann. N. Y. Acad. Sci. 851:139-146.
    • (1998) Ann. N. Y. Acad. Sci. , vol.851 , pp. 139-146
    • Karin, M.1
  • 22
    • 1642447684 scopus 로고    scopus 로고
    • Transcriptional switch by activating transcription factor 2-derived peptide sensitizes melanoma cells to apoptosis and inhibits their tumorigenicity
    • Bhoumik A, Jones N, Ronai Z. 2004. Transcriptional switch by activating transcription factor 2-derived peptide sensitizes melanoma cells to apoptosis and inhibits their tumorigenicity. Proc. Natl. Acad. Sci. U. S. A. 101: 4222-4227.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 4222-4227
    • Bhoumik, A.1    Jones, N.2    Ronai, Z.3
  • 23
    • 55549130760 scopus 로고    scopus 로고
    • Formation of stress granules inhibits apoptosis by suppressing stressresponsive MAPK pathways
    • Arimoto K, Fukuda H, Imajoh-Ohmi S, Saito H, Takekawa M. 2008. Formation of stress granules inhibits apoptosis by suppressing stressresponsive MAPK pathways. Nat. Cell Biol. 10:1324-1332.
    • (2008) Nat. Cell Biol , vol.10 , pp. 1324-1332
    • Arimoto, K.1    Fukuda, H.2    Imajoh-Ohmi, S.3    Saito, H.4    Takekawa, M.5
  • 26
    • 0018700703 scopus 로고
    • Fluorographic detection of radioactivity in polyacrylamide gels with the water-soluble fluor, sodium salicylate
    • Chamberlain JP. 1979. Fluorographic detection of radioactivity in polyacrylamide gels with the water-soluble fluor, sodium salicylate. Anal. Biochem. 98:132-135.
    • (1979) Anal. Biochem , vol.98 , pp. 132-135
    • Chamberlain, J.P.1
  • 27
    • 0035260658 scopus 로고    scopus 로고
    • Mechanism of ribosome recruitment by hepatitis C IRES RNA
    • Kieft JS, Zhou K, Jubin R, Doudna JA. 2001. Mechanism of ribosome recruitment by hepatitis C IRES RNA. RNA 7:194-206.
    • (2001) RNA , vol.7 , pp. 194-206
    • Kieft, J.S.1    Zhou, K.2    Jubin, R.3    Doudna, J.A.4
  • 30
    • 0032101707 scopus 로고    scopus 로고
    • Calcineurin preferentially synergizes with PKC-theta to activate JNK and IL-2 promoter in T lymphocytes
    • Werlen G, Jacinto E, Xia Y, Karin M. 1998. Calcineurin preferentially synergizes with PKC-theta to activate JNK and IL-2 promoter in T lymphocytes. EMBO J. 17:3101-3111.
    • (1998) EMBO J , vol.17 , pp. 3101-3111
    • Werlen, G.1    Jacinto, E.2    Xia, Y.3    Karin, M.4
  • 31
    • 40149094481 scopus 로고    scopus 로고
    • Requirements for PKC-augmented JNK activation by MKK4/7
    • Lopez-Bergami P, Ronai Z. 2008. Requirements for PKC-augmented JNK activation by MKK4/7. Int. J. Biochem. Cell Biol. 40:1055-1064.
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 1055-1064
    • Lopez-Bergami, P.1    Ronai, Z.2
  • 32
    • 0034725037 scopus 로고    scopus 로고
    • Stability of the ATF2 transcription factor is regulated by phosphorylation and dephosphorylation
    • Fuchs SY, Tappin I, Ronai Z. 2000. Stability of the ATF2 transcription factor is regulated by phosphorylation and dephosphorylation. J. Biol. Chem. 275:12560-12564.
    • (2000) J. Biol Chem. , vol.275 , pp. 12560-12564
    • Fuchs, S.Y.1    Tappin, I.2    Ronai, Z.3
  • 33
    • 16844387124 scopus 로고    scopus 로고
    • Role of JNK activation in apoptosis: a double-edged sword
    • Liu J, Lin A. 2005. Role of JNK activation in apoptosis: a double-edged sword. Cell Res. 15:36-42.
    • (2005) Cell Res , vol.15 , pp. 36-42
    • Liu, J.1    Lin, A.2
  • 34
  • 35
    • 22444444478 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the human 40S ribosomal subunit: native and HCV IRES-bound complexes
    • Yu Y, Ji H, Doudna JA, Leary JA. 2005. Mass spectrometric analysis of the human 40S ribosomal subunit: native and HCV IRES-bound complexes. Protein Sci. 14:1438-1446.
    • (2005) Protein Sci , vol.14 , pp. 1438-1446
    • Yu, Y.1    Ji, H.2    Doudna, J.A.3    Leary, J.A.4
  • 36
    • 62849093964 scopus 로고    scopus 로고
    • Direct link between RACK1 function and localization at the ribosome in vivo
    • Coyle SM, Gilbert WV, Doudna JA. 2009. Direct link between RACK1 function and localization at the ribosome in vivo. Mol. Cell. Biol. 29: 1626-1634.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1626-1634
    • Coyle, S.M.1    Gilbert, W.V.2    Doudna, J.A.3
  • 37
    • 0031985120 scopus 로고    scopus 로고
    • Dominantnegative c-Jun NH2-terminal kinase 2 sensitizes renal inner medullary collecting duct cells to hypertonicity-induced lethality independent of organic osmolyte transport
    • Wojtaszek PA, Heasley LE, Siriwardana G, Berl T. 1998. Dominantnegative c-Jun NH2-terminal kinase 2 sensitizes renal inner medullary collecting duct cells to hypertonicity-induced lethality independent of organic osmolyte transport. J. Biol. Chem. 273:800-804.
    • (1998) J. Biol Chem. , vol.273 , pp. 800-804
    • Wojtaszek, P.A.1    Heasley, L.E.2    Siriwardana, G.3    Berl, T.4
  • 38
    • 0028329953 scopus 로고
    • JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
    • Derijard B, Hibi M, Wu IH, Barrett T, Su B, Deng T, Karin M, Davis RJ. 1994. JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell 76:1025-1037.
    • (1994) Cell. , vol.76 , pp. 1025-1037
    • Derijard, B.1    Hibi, M.2    Wu, I.H.3    Barrett, T.4    Su, B.5    Deng, T.6    Karin, M.7    Davis, R.J.8
  • 39
    • 0037124091 scopus 로고    scopus 로고
    • Ultraviolet light inhibits translation through activation of the unfolded protein response kinase PERK in the lumen of the endoplasmic reticulum
    • Wu S, Hu Y, Wang JL, Chatterjee M, Shi Y, Kaufman RJ. 2002. Ultraviolet light inhibits translation through activation of the unfolded protein response kinase PERK in the lumen of the endoplasmic reticulum. J. Biol. Chem. 277:18077-18083.
    • (2002) J. Biol Chem. , vol.277 , pp. 18077-18083
    • Wu, S.1    Hu, Y.2    Wang, J.L.3    Chatterjee, M.4    Shi, Y.5    Kaufman, R.J.6
  • 40
    • 79951510534 scopus 로고    scopus 로고
    • Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1
    • Rabl J, Leibundgut M, Ataide SF, Haag A, Ban N. 2011. Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1. Science 331:730-736.
    • (2011) Science , vol.331 , pp. 730-736
    • Rabl, J.1    Leibundgut, M.2    Ataide, S.F.3    Haag, A.4    Ban, N.5
  • 41
    • 77954377942 scopus 로고    scopus 로고
    • eEF1A: thinking outside the ribosome
    • Mateyak MK, Kinzy TG. 2010. eEF1A: thinking outside the ribosome. J. Biol. Chem. 285:21209-21213.
    • (2010) J. Biol. Chem. , vol.285 , pp. 21209-21213
    • Mateyak, M.K.1    Kinzy, T.G.2
  • 42
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • Jackson RJ, Hellen CU, Pestova TV. 2010. The mechanism of eukaryotic translation initiation and principles of its regulation. Nat. Rev. Mol. Cell. Biol. 11:113-127.
    • (2010) Nat. Rev Mol. Cell. Biol. , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 43
    • 33744993160 scopus 로고    scopus 로고
    • In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3
    • Alkalaeva EZ, Pisarev AV, Frolova LY, Kisselev LL, Pestova TV. 2006. In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3. Cell 125:1125-1136.
    • (2006) Cell , vol.125 , pp. 1125-1136
    • Alkalaeva, E.Z.1    Pisarev, A.V.2    Frolova, L.Y.3    Kisselev, L.L.4    Pestova, T.V.5
  • 44
    • 0030928059 scopus 로고    scopus 로고
    • Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells
    • Eggers DK, Welch WJ, Hansen WJ. 1997. Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells. Mol. Biol. Cell 8:1559-1573.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 1559-1573
    • Eggers, D.K.1    Welch, W.J.2    Hansen, W.J.3
  • 45
    • 0014413815 scopus 로고
    • Messenger RNA-protein complexes and newly synthesized ribosomal subunits: analysis of free particles and components of polyribosomes
    • Perry RP, Kelley DE. 1968. Messenger RNA-protein complexes and newly synthesized ribosomal subunits: analysis of free particles and components of polyribosomes. J. Mol. Biol. 35:37-59.
    • (1968) J. Mol. Biol. , vol.35 , pp. 37-59
    • Perry, R.P.1    Kelley, D.E.2
  • 46
    • 67749117934 scopus 로고    scopus 로고
    • Signal integration by JNK and p38 MAPK pathways in cancer development
    • Wagner EF, Nebreda AR. 2009. Signal integration by JNK and p38 MAPK pathways in cancer development. Nat. Rev. Cancer 9:537-549.
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 537-549
    • Wagner, E.F.1    Nebreda, A.R.2
  • 48
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye Y, Meyer HH, Rapoport TA. 2001. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414: 652-656.
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 49
    • 0036136901 scopus 로고    scopus 로고
    • AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation
    • Rabinovich E, Kerem A, Frohlich KU, Diamant N, Bar-Nun S. 2002. AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol. Cell. Biol. 22:626-634.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 626-634
    • Rabinovich, E.1    Kerem, A.2    Frohlich, K.U.3    Diamant, N.4    Bar-Nun, S.5
  • 50
    • 78649472341 scopus 로고    scopus 로고
    • Receptor for activated C kinase 1 stimulates nascent polypeptidedependent translation arrest
    • Kuroha K, Akamatsu M, Dimitrova L, Ito T, Kato Y, Shirahige K, Inada T. 2010. Receptor for activated C kinase 1 stimulates nascent polypeptidedependent translation arrest. EMBO Rep. 11:956-961.
    • (2010) EMBO Rep , vol.11 , pp. 956-961
    • Kuroha, K.1    Akamatsu, M.2    Dimitrova, L.3    Ito, T.4    Kato, Y.5    Shirahige, K.6    Inada, T.7
  • 51
    • 39749138785 scopus 로고    scopus 로고
    • A structural understanding of the dynamic ribosome machine
    • Steitz TA. 2008. A structural understanding of the dynamic ribosome machine. Nat. Rev. Mol. Cell. Biol. 9:242-253.
    • (2008) Nat. Rev. Mol. Cell. Biol. , vol.9 , pp. 242-253
    • Steitz, T.A.1
  • 52
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl FU, Bracher A, Hayer-Hartl M. 2010. Molecular chaperones in protein folding and proteostasis. Nature 475:324-332.
    • (2010) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 53
    • 0028136693 scopus 로고
    • Protein synthesis elongation factor EF-1α is essential for ubiquitin-dependent degradation of certain N alpha-acetylated proteins and may be substituted for by the bacterial elongation factor EF-Tu
    • Gonen H, Smith CE, Siegel NR, Kahana C, Merrick WC, Chakraburtty K, Schwartz AL, Ciechanover A. 1994. Protein synthesis elongation factor EF-1α is essential for ubiquitin-dependent degradation of certain N alpha-acetylated proteins and may be substituted for by the bacterial elongation factor EF-Tu. Proc. Natl. Acad. Sci. U. S. A. 91:7648-7652.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 7648-7652
    • Gonen, H.1    Smith, C.E.2    Siegel, N.R.3    Kahana, C.4    Merrick, W.C.5    Chakraburtty, K.6    Schwartz, A.L.7    Ciechanover, A.8
  • 54
    • 57649114878 scopus 로고    scopus 로고
    • Implication of human N-α-acetyltransferase 5 in cellular proliferation and carcinogenesis
    • Ametzazurra A, Larrea E, Civeira MP, Prieto J, Aldabe R. 2008. Implication of human N-α-acetyltransferase 5 in cellular proliferation and carcinogenesis. Oncogene 27:7296-7306.
    • (2008) Oncogene , vol.27 , pp. 7296-7306
    • Ametzazurra, A.1    Larrea, E.2    Civeira, M.P.3    Prieto, J.4    Aldabe, R.5
  • 56
    • 54049149934 scopus 로고    scopus 로고
    • Identification of the human N(α)-acetyltransferase complex B (hNatB): a complex important for cell-cycle progression
    • Starheim KK, Arnesen T, Gromyko D, Ryningen A, Varhaug JE, Lille-haug JR. 2008. Identification of the human N(α)-acetyltransferase complex B (hNatB): a complex important for cell-cycle progression. Biochem. J. 415:325-331.
    • (2008) Biochem. J. , vol.415 , pp. 325-331
    • Starheim, K.K.1    Arnesen, T.2    Gromyko, D.3    Ryningen, A.4    Varhaug, J.E.5    Lille-haug, J.R.6
  • 58
    • 0037085362 scopus 로고    scopus 로고
    • Peptide elongation factor eEF1A-2/S1 expression in cultured differentiated myotubes and its protective effect against caspase-3-mediated apoptosis
    • Ruest LB, Marcotte R, Wang E. 2002. Peptide elongation factor eEF1A-2/S1 expression in cultured differentiated myotubes and its protective effect against caspase-3-mediated apoptosis. J. Biol. Chem. 277:5418-5425.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5418-5425
    • Ruest, L.B.1    Marcotte, R.2    Wang, E.3
  • 62
    • 57149098022 scopus 로고    scopus 로고
    • Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies
    • Yam AY, Xia Y, Lin HT, Burlingame A, Gerstein M, Frydman J. 2008. Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies. Nat. Struct. Mol. Biol. 15:1255-1262.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1255-1262
    • Yam, A.Y.1    Xia, Y.2    Lin, H.T.3    Burlingame, A.4    Gerstein, M.5    Frydman, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.