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Volumn 8, Issue 8, 2013, Pages

Aspergillus oryzae AoSO Is a Novel Component of Stress Granules upon Heat Stress in Filamentous Fungi

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MARKER; CYTOPLASM PROTEIN; ENHANCED GREEN FLUORESCENT PROTEIN; FUNGAL PROTEIN; HYBRID PROTEIN; PROTEIN AOPAB1; PROTEIN AOSO; PROTEIN PAB1P; RIBONUCLEOPROTEIN; UNCLASSIFIED DRUG;

EID: 84882670133     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0072209     Document Type: Article
Times cited : (22)

References (74)
  • 1
    • 17144424622 scopus 로고    scopus 로고
    • Translational control in stress and apoptosis
    • Holcik M, Sonenberg N, (2005) Translational control in stress and apoptosis. Nat Rev Mol Cell Biol 6: 318-327.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 318-327
    • Holcik, M.1    Sonenberg, N.2
  • 3
    • 33847417585 scopus 로고    scopus 로고
    • P bodies and the control of mRNA translation and degradation
    • Parker R, Sheth U, (2007) P bodies and the control of mRNA translation and degradation. Mol Cell 25: 635-646.
    • (2007) Mol Cell , vol.25 , pp. 635-646
    • Parker, R.1    Sheth, U.2
  • 4
    • 39949085583 scopus 로고    scopus 로고
    • Stress granules: The tao of RNA triage
    • Anderson P, Kedersha N, (2008) Stress granules: The tao of RNA triage. Trends Biochem Sci 33: 141-150.
    • (2008) Trends Biochem Sci , vol.33 , pp. 141-150
    • Anderson, P.1    Kedersha, N.2
  • 5
    • 72149095755 scopus 로고    scopus 로고
    • Eukaryotic stress granules: The ins and outs of translation
    • Buchan JR, Parker R, (2009) Eukaryotic stress granules: The ins and outs of translation. Mol Cell 36: 932-941.
    • (2009) Mol Cell , vol.36 , pp. 932-941
    • Buchan, J.R.1    Parker, R.2
  • 6
    • 79551530753 scopus 로고    scopus 로고
    • Cytoplasmic mRNP granules at a glance
    • Erickson SL, Lykke-Andersen J, (2011) Cytoplasmic mRNP granules at a glance. J Cell Sci 124: 293-297.
    • (2011) J Cell Sci , vol.124 , pp. 293-297
    • Erickson, S.L.1    Lykke-Andersen, J.2
  • 7
    • 84865658810 scopus 로고    scopus 로고
    • P-bodies and stress granules: Possible roles in the control of translation and mRNA degradation
    • Decker CJ, Parker R, (2012) P-bodies and stress granules: Possible roles in the control of translation and mRNA degradation. Cold Spring Harb Perspect Biol 4: a012286.
    • (2012) Cold Spring Harb Perspect Biol , vol.4
    • Decker, C.J.1    Parker, R.2
  • 8
    • 66249103703 scopus 로고    scopus 로고
    • RNA granules: Post-transcriptional and epigenetic modulators of gene expression
    • Anderson P, Kedersha N, (2009) RNA granules: Post-transcriptional and epigenetic modulators of gene expression. Nat Rev Mol Cell Biol 10: 430-436.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 430-436
    • Anderson, P.1    Kedersha, N.2
  • 9
    • 32544446451 scopus 로고    scopus 로고
    • Coping with stress: EIF2 kinases and translational control
    • Wek RC, Jiang HY, Anthony TG, (2006) Coping with stress: EIF2 kinases and translational control. Biochem Soc Trans 34: 7-11.
    • (2006) Biochem Soc Trans , vol.34 , pp. 7-11
    • Wek, R.C.1    Jiang, H.Y.2    Anthony, T.G.3
  • 10
    • 0033634641 scopus 로고    scopus 로고
    • Perk is essential for translational regulation and cell survival during the unfolded protein response
    • Harding HP, Zhang Y, Bertolotti A, Zeng H, Ron D, (2000) Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol Cell 5: 897-904.
    • (2000) Mol Cell , vol.5 , pp. 897-904
    • Harding, H.P.1    Zhang, Y.2    Bertolotti, A.3    Zeng, H.4    Ron, D.5
  • 11
    • 31544442938 scopus 로고    scopus 로고
    • Radiation-induced changes in gene expression involve recruitment of existing messenger RNAs to and away from polysomes
    • Lu X, de la Pena L, Barker C, Camphausen K, Tofilon PJ, (2006) Radiation-induced changes in gene expression involve recruitment of existing messenger RNAs to and away from polysomes. Cancer Res 66: 1052-1061.
    • (2006) Cancer Res , vol.66 , pp. 1052-1061
    • Lu, X.1    de la Pena, L.2    Barker, C.3    Camphausen, K.4    Tofilon, P.J.5
  • 12
    • 66149137639 scopus 로고    scopus 로고
    • Translational reprogramming following UVB irradiation is mediated by DNA-PKcs and allows selective recruitment to the polysomes of mRNAs encoding DNA repair enzymes
    • Powley IR, Kondrashov A, Young LA, Dobbyn HC, Hill K, et al. (2009) Translational reprogramming following UVB irradiation is mediated by DNA-PKcs and allows selective recruitment to the polysomes of mRNAs encoding DNA repair enzymes. Genes Dev 23: 1207-1220.
    • (2009) Genes Dev , vol.23 , pp. 1207-1220
    • Powley, I.R.1    Kondrashov, A.2    Young, L.A.3    Dobbyn, H.C.4    Hill, K.5
  • 13
    • 0037101945 scopus 로고    scopus 로고
    • Stressful initiations
    • Anderson P, Kedersha N, (2002) Stressful initiations. J Cell Sci 115: 3227-3234.
    • (2002) J Cell Sci , vol.115 , pp. 3227-3234
    • Anderson, P.1    Kedersha, N.2
  • 14
    • 79251554956 scopus 로고    scopus 로고
    • Stress-specific composition, assembly and kinetics of stress granules in Saccharomyces cerevisiae
    • Buchan JR, Yoon JH, Parker R, (2011) Stress-specific composition, assembly and kinetics of stress granules in Saccharomyces cerevisiae. J Cell Sci 124: 228-239.
    • (2011) J Cell Sci , vol.124 , pp. 228-239
    • Buchan, J.R.1    Yoon, J.H.2    Parker, R.3
  • 15
    • 55549130760 scopus 로고    scopus 로고
    • Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways
    • Arimoto K, Fukuda H, Imajoh-Ohmi S, Saito H, Takekawa M, (2008) Formation of stress granules inhibits apoptosis by suppressing stress-responsive 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
  • 16
    • 84864308260 scopus 로고    scopus 로고
    • Transient sequestration of TORC1 into stress granules during heat stress
    • Takahara T, Maeda T, (2012) Transient sequestration of TORC1 into stress granules during heat stress. Mol Cell 47: 242-252.
    • (2012) Mol Cell , vol.47 , pp. 242-252
    • Takahara, T.1    Maeda, T.2
  • 17
    • 0034761729 scopus 로고    scopus 로고
    • Poly(A)-binding proteins regulate both mRNA deadenylation and decapping in yeast cytoplasmic extracts
    • Wilusz CJ, Gao M, Jones CL, Wilusz J, Peltz SW, (2001) Poly(A)-binding proteins regulate both mRNA deadenylation and decapping in yeast cytoplasmic extracts. RNA 7: 1416-1424.
    • (2001) RNA , vol.7 , pp. 1416-1424
    • Wilusz, C.J.1    Gao, M.2    Jones, C.L.3    Wilusz, J.4    Peltz, S.W.5
  • 18
    • 84863869059 scopus 로고    scopus 로고
    • RNA degradation in Saccharomyces cerevisae
    • Parker R, (2012) RNA degradation in Saccharomyces cerevisae. Genetics 191: 671-702.
    • (2012) Genetics , vol.191 , pp. 671-702
    • Parker, R.1
  • 19
    • 0742288008 scopus 로고    scopus 로고
    • The enzymes and control of eukaryotic mRNA turnover
    • Parker R, Song H, (2004) The enzymes and control of eukaryotic mRNA turnover. Nature Struct Mol Biol 11: 121-127.
    • (2004) Nature Struct Mol Biol , vol.11 , pp. 121-127
    • Parker, R.1    Song, H.2
  • 21
    • 0033055772 scopus 로고    scopus 로고
    • The cis acting sequences responsible for the differential decay of the unstable MFA2 and stable PGK1 transcripts in yeast include the context of the translational start codon
    • LaGrandeur T, Parker R, (1999) The cis acting sequences responsible for the differential decay of the unstable MFA2 and stable PGK1 transcripts in yeast include the context of the translational start codon. RNA 5: 420-433.
    • (1999) RNA , vol.5 , pp. 420-433
    • LaGrandeur, T.1    Parker, R.2
  • 22
    • 0030854119 scopus 로고    scopus 로고
    • Regulated poly(A) tail shortening in somatic cells mediated by cap-proximal translational repressor proteins and ribosome association
    • Muckenthaler M, Gunkel N, Stripecke R, Hentze MW, (1997) Regulated poly(A) tail shortening in somatic cells mediated by cap-proximal translational repressor proteins and ribosome association. RNA 3: 983-995.
    • (1997) RNA , vol.3 , pp. 983-995
    • Muckenthaler, M.1    Gunkel, N.2    Stripecke, R.3    Hentze, M.W.4
  • 23
    • 0028961870 scopus 로고
    • Turnover mechanisms of the stable yeast PGK1 mRNA
    • Muhlrad D, Decker CJ, Parker R, (1995) Turnover mechanisms of the stable yeast PGK1 mRNA. Mol Cell Biol 15: 2145-2156.
    • (1995) Mol Cell Biol , vol.15 , pp. 2145-2156
    • Muhlrad, D.1    Decker, C.J.2    Parker, R.3
  • 24
    • 0032778953 scopus 로고    scopus 로고
    • Mutations in translation initiation factors lead to increased rates of deadenylation and decapping of mRNAs in Saccharomyces cerevisiae
    • Schwartz DC, Parker R, (1999) Mutations in translation initiation factors lead to increased rates of deadenylation and decapping of mRNAs in Saccharomyces cerevisiae. Mol Cell Biol 19: 5247-5256.
    • (1999) Mol Cell Biol , vol.19 , pp. 5247-5256
    • Schwartz, D.C.1    Parker, R.2
  • 25
    • 25144482816 scopus 로고    scopus 로고
    • General translational repression by activators of mRNA decapping
    • Coller J, Parker R, (2005) General translational repression by activators of mRNA decapping. Cell 122: 875-886.
    • (2005) Cell , vol.122 , pp. 875-886
    • Coller, J.1    Parker, R.2
  • 26
    • 77956540817 scopus 로고    scopus 로고
    • Decapping activators in Saccharomyces cerevisiae act by multiple mechanisms
    • Nissan T, Rajyaguru P, She M, Song H, Parker R, (2010) Decapping activators in Saccharomyces cerevisiae act by multiple mechanisms. Mol Cell 39: 773-783.
    • (2010) Mol Cell , vol.39 , pp. 773-783
    • Nissan, T.1    Rajyaguru, P.2    She, M.3    Song, H.4    Parker, R.5
  • 27
    • 56849103665 scopus 로고    scopus 로고
    • The control of mRNA decapping and P-body formation
    • Franks TM, Lykke-Andersen J, (2008) The control of mRNA decapping and P-body formation. Mo Cell 32: 605-615.
    • (2008) Mo Cell , vol.32 , pp. 605-615
    • Franks, T.M.1    Lykke-Andersen, J.2
  • 28
    • 0037968357 scopus 로고    scopus 로고
    • Decapping and decay of messenger RNA occur in cytoplasmic processing bodies
    • Sheth U, Parker R, (2003) Decapping and decay of messenger RNA occur in cytoplasmic processing bodies. Science 300: 805-808.
    • (2003) Science , vol.300 , pp. 805-808
    • Sheth, U.1    Parker, R.2
  • 29
    • 27144515901 scopus 로고    scopus 로고
    • Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies
    • Brengues M, Teixeira D, Parker R, (2005) Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies. Science 310: 486-489.
    • (2005) Science , vol.310 , pp. 486-489
    • Brengues, M.1    Teixeira, D.2    Parker, R.3
  • 30
    • 84870976054 scopus 로고    scopus 로고
    • Multiple modes for gatekeeping at fungal cell-to-cell channels
    • Jedd G, Pieuchot L, (2012) Multiple modes for gatekeeping at fungal cell-to-cell channels. Mol Microbiol 86: 1291-1294.
    • (2012) Mol Microbiol , vol.86 , pp. 1291-1294
    • Jedd, G.1    Pieuchot, L.2
  • 31
    • 0027237229 scopus 로고
    • Cell-to-cell transport via motile tubules in growing hyphae of a fungus
    • Shepherd VA, Orlovich DA, Ashford AE, (1993) Cell-to-cell transport via motile tubules in growing hyphae of a fungus. J Cell Sci 105: 1173-1178.
    • (1993) J Cell Sci , vol.105 , pp. 1173-1178
    • Shepherd, V.A.1    Orlovich, D.A.2    Ashford, A.E.3
  • 32
    • 0028082863 scopus 로고
    • Occlusions of septal pores in filamentous fungi
    • Markham P, (1994) Occlusions of septal pores in filamentous fungi. Mycol Res 98: 1089-1106.
    • (1994) Mycol Res , vol.98 , pp. 1089-1106
    • Markham, P.1
  • 33
    • 0021738979 scopus 로고
    • Septal sealing in the basidiomycete Coriolus versicolor
    • Aylmore RC, Wakley GE, Todd NK, (1984) Septal sealing in the basidiomycete Coriolus versicolor. J Gen Microbiol 130: 2975-2982.
    • (1984) J Gen Microbiol , vol.130 , pp. 2975-2982
    • Aylmore, R.C.1    Wakley, G.E.2    Todd, N.K.3
  • 34
    • 67650159436 scopus 로고    scopus 로고
    • Cytoplasmic continuity revisited: Closure of septa of the filamentous fungus Schizophyllum commune in response to environmental conditions
    • van Peer AF, Muller WH, Boekhout T, Lugones LG, Wosten HA, (2009) Cytoplasmic continuity revisited: Closure of septa of the filamentous fungus Schizophyllum commune in response to environmental conditions. PloS One 4: e5977.
    • (2009) PloS One , vol.4
    • van Peer, A.F.1    Muller, W.H.2    Boekhout, T.3    Lugones, L.G.4    Wosten, H.A.5
  • 35
    • 33846460807 scopus 로고    scopus 로고
    • SO, a protein involved in hyphal fusion in Neurospora crassa, localizes to septal plugs
    • Fleißner A, Glass NL, (2007) SO, a protein involved in hyphal fusion in Neurospora crassa, localizes to septal plugs. Eukaryot Cell 6: 84-94.
    • (2007) Eukaryot Cell , vol.6 , pp. 84-94
    • Fleißner, A.1    Glass, N.L.2
  • 36
    • 73349140226 scopus 로고    scopus 로고
    • Oscillatory recruitment of signaling proteins to cell tips promotes coordinated behavior during cell fusion
    • Fleißner A, Leeder AC, Roca MG, Read ND, Glass NL, (2009) Oscillatory recruitment of signaling proteins to cell tips promotes coordinated behavior during cell fusion. Proc Natl Acad Sci U S A 106: 19387-19392.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 19387-19392
    • Fleißner, A.1    Leeder, A.C.2    Roca, M.G.3    Read, N.D.4    Glass, N.L.5
  • 37
    • 18944401011 scopus 로고    scopus 로고
    • The so locus is required for vegetative cell fusion and postfertilization events in Neurospora crassa
    • Fleißner A, Sarkar S, Jacobson DJ, Roca MG, Read ND, et al. (2005) The so locus is required for vegetative cell fusion and postfertilization events in Neurospora crassa. Eukaryot Cell 4: 920-930.
    • (2005) Eukaryot Cell , vol.4 , pp. 920-930
    • Fleißner, A.1    Sarkar, S.2    Jacobson, D.J.3    Roca, M.G.4    Read, N.D.5
  • 38
    • 34249716323 scopus 로고    scopus 로고
    • The WW domain protein PRO40 is required for fungal fertility and associates with woronin bodies
    • Engh I, Wurtz C, Witzel-Schlomp K, Zhang HY, Hoff B, et al. (2007) The WW domain protein PRO40 is required for fungal fertility and associates with woronin bodies. Eukaryot Cell 6: 831-843.
    • (2007) Eukaryot Cell , vol.6 , pp. 831-843
    • Engh, I.1    Wurtz, C.2    Witzel-Schlomp, K.3    Zhang, H.Y.4    Hoff, B.5
  • 39
    • 72949109953 scopus 로고    scopus 로고
    • AoSO protein accumulates at the septal pore in response to various stresses in the filamentous fungus Aspergillus oryzae
    • Maruyama J, Escaño CS, Kitamoto K, (2010) AoSO protein accumulates at the septal pore in response to various stresses in the filamentous fungus Aspergillus oryzae. Biochem Biophys Res Commun 391: 868-873.
    • (2010) Biochem Biophys Res Commun , vol.391 , pp. 868-873
    • Maruyama, J.1    Escaño, C.S.2    Kitamoto, K.3
  • 40
    • 33747835577 scopus 로고    scopus 로고
    • Development of a versatile expression plasmid construction system for Aspergillus oryzae and its application to visualization of mitochondria
    • Mabashi Y, Kikuma T, Maruyama J, Arioka M, Kitamoto K, (2006) Development of a versatile expression plasmid construction system for Aspergillus oryzae and its application to visualization of mitochondria. Biosci Biotechnol Biochem 70: 1882-1889.
    • (2006) Biosci Biotechnol Biochem , vol.70 , pp. 1882-1889
    • Mabashi, Y.1    Kikuma, T.2    Maruyama, J.3    Arioka, M.4    Kitamoto, K.5
  • 41
    • 29244442741 scopus 로고    scopus 로고
    • Genome sequencing and analysis of Aspergillus oryzae
    • Machida M, Asai K, Sano M, Tanaka T, Kumagai T, et al. (2005) Genome sequencing and analysis of Aspergillus oryzae. Nature 438: 1157-1161.
    • (2005) Nature , vol.438 , pp. 1157-1161
    • Machida, M.1    Asai, K.2    Sano, M.3    Tanaka, T.4    Kumagai, T.5
  • 42
    • 61949336473 scopus 로고    scopus 로고
    • Disruption of the Aopex11-1 gene involved in peroxisome proliferation leads to impaired woronin body formation in Aspergillus oryzae
    • Escaño CS, Juvvadi PR, Jin FJ, Takahashi T, Koyama Y, et al. (2009) Disruption of the Aopex11-1 gene involved in peroxisome proliferation leads to impaired woronin body formation in Aspergillus oryzae. Eukaryot Cell 8: 296-305.
    • (2009) Eukaryot Cell , vol.8 , pp. 296-305
    • Escaño, C.S.1    Juvvadi, P.R.2    Jin, F.J.3    Takahashi, T.4    Koyama, Y.5
  • 43
    • 0036366095 scopus 로고    scopus 로고
    • Molecular biology of the koji molds
    • Kitamoto K, (2002) Molecular biology of the koji molds. Adv Appl Microbiol 51: 129-153.
    • (2002) Adv Appl Microbiol , vol.51 , pp. 129-153
    • Kitamoto, K.1
  • 44
    • 80052925932 scopus 로고    scopus 로고
    • Targeted gene disruption in koji mold Aspergillus oryzae
    • Maruyama J, Kitamoto K, (2011) Targeted gene disruption in koji mold Aspergillus oryzae. Methods Mol Biol 765: 447-456.
    • (2011) Methods Mol Biol , vol.765 , pp. 447-456
    • Maruyama, J.1    Kitamoto, K.2
  • 45
    • 85009547782 scopus 로고    scopus 로고
    • Transformation system for Aspergillus oryzae with double auxotrophic mutations, niaD and sC
    • Yamada O, Lee BR, Gomi K, (1997) Transformation system for Aspergillus oryzae with double auxotrophic mutations, niaD and sC. Biosci Biotechnol Biochem 61: 1367-1369.
    • (1997) Biosci Biotechnol Biochem , vol.61 , pp. 1367-1369
    • Yamada, O.1    Lee, B.R.2    Gomi, K.3
  • 46
    • 50249161913 scopus 로고    scopus 로고
    • Multiple gene disruptions by marker recycling with highly efficient gene-targeting background (ΔligD) in Aspergillus oryzae
    • Maruyama J, Kitamoto K, (2008) Multiple gene disruptions by marker recycling with highly efficient gene-targeting background (ΔligD) in Aspergillus oryzae. Biotechnol Lett 30: 1811-1817.
    • (2008) Biotechnol Lett , vol.30 , pp. 1811-1817
    • Maruyama, J.1    Kitamoto, K.2
  • 47
    • 0032532439 scopus 로고    scopus 로고
    • mRNA stabilization by poly(A) binding protein is independent of poly(A) and requires translation
    • Coller JM, Gray NK, Wickens MP, (1998) mRNA stabilization by poly(A) binding protein is independent of poly(A) and requires translation. Genes Dev 12: 3226-3235.
    • (1998) Genes Dev , vol.12 , pp. 3226-3235
    • Coller, J.M.1    Gray, N.K.2    Wickens, M.P.3
  • 48
    • 77958607457 scopus 로고    scopus 로고
    • Tethering of poly(A)-binding protein interferes with non-translated mRNA decay from the 5' end in yeast
    • Tsuboi T, Inada T, (2010) Tethering of poly(A)-binding protein interferes with non-translated mRNA decay from the 5' end in yeast. J Biol Chem 285: 33589-33601.
    • (2010) J Biol Chem , vol.285 , pp. 33589-33601
    • Tsuboi, T.1    Inada, T.2
  • 49
    • 56149086182 scopus 로고    scopus 로고
    • P bodies promote stress granule assembly in Saccharomyces cerevisiae
    • Buchan JR, Muhlrad D, Parker R, (2008) P bodies promote stress granule assembly in Saccharomyces cerevisiae. J Cell Biol 183: 441-455.
    • (2008) J Cell Biol , vol.183 , pp. 441-455
    • Buchan, J.R.1    Muhlrad, D.2    Parker, R.3
  • 50
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: Mechanisms and biological targets
    • Sonenberg N, Hinnebusch AG, (2009) Regulation of translation initiation in eukaryotes: Mechanisms and biological targets. Cell 136: 731-745.
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 51
    • 22344455246 scopus 로고    scopus 로고
    • Stress granules and processing bodies are dynamically linked sites of mRNP remodeling
    • Kedersha N, Stoecklin G, Ayodele M, Yacono P, Lykke-Andersen J, et al. (2005) Stress granules and processing bodies are dynamically linked sites of mRNP remodeling. J Cell Biol 169: 871-884.
    • (2005) J Cell Biol , vol.169 , pp. 871-884
    • Kedersha, N.1    Stoecklin, G.2    Ayodele, M.3    Yacono, P.4    Lykke-Andersen, J.5
  • 52
    • 34347387606 scopus 로고    scopus 로고
    • Accumulation of polyadenylated mRNA, Pab1p, eIF4E, and eIF4G with P-bodies in Saccharomyces cerevisiae
    • Brengues M, Parker R, (2007) Accumulation of polyadenylated mRNA, Pab1p, eIF4E, and eIF4G with P-bodies in Saccharomyces cerevisiae. Mol Biol Cell 18: 2592-2602.
    • (2007) Mol Biol Cell , vol.18 , pp. 2592-2602
    • Brengues, M.1    Parker, R.2
  • 53
    • 68949172267 scopus 로고    scopus 로고
    • Robust heat shock induces eIF2alpha-phosphorylation-independent assembly of stress granules containing eIF3 and 40S ribosomal subunits in budding yeast, Saccharomyces cerevisiae
    • Grousl T, Ivanov P, Frydlova I, Vasicova P, Janda F, et al. (2009) Robust heat shock induces eIF2alpha-phosphorylation-independent assembly of stress granules containing eIF3 and 40S ribosomal subunits in budding yeast, Saccharomyces cerevisiae. J Cell Sci 122: 2078-2088.
    • (2009) J Cell Sci , vol.122 , pp. 2078-2088
    • Grousl, T.1    Ivanov, P.2    Frydlova, I.3    Vasicova, P.4    Janda, F.5
  • 54
    • 35348989809 scopus 로고    scopus 로고
    • Stress-dependent relocalization of translationally primed mRNPs to cytoplasmic granules that are kinetically and spatially distinct from P-bodies
    • Hoyle NP, Castelli LM, Campbell SG, Holmes LE, Ashe MP, (2007) Stress-dependent relocalization of translationally primed mRNPs to cytoplasmic granules that are kinetically and spatially distinct from P-bodies. J Cell Biol 179: 65-74.
    • (2007) J Cell Biol , vol.179 , pp. 65-74
    • Hoyle, N.P.1    Castelli, L.M.2    Campbell, S.G.3    Holmes, L.E.4    Ashe, M.P.5
  • 55
    • 16844365216 scopus 로고    scopus 로고
    • The translational regulator CPEB1 provides a link between dcp1 bodies and stress granules
    • Wilczynska A, Aigueperse C, Kress M, Dautry F, Weil D, (2005) The translational regulator CPEB1 provides a link between dcp1 bodies and stress granules. J Cell Sci 118: 981-992.
    • (2005) J Cell Sci , vol.118 , pp. 981-992
    • Wilczynska, A.1    Aigueperse, C.2    Kress, M.3    Dautry, F.4    Weil, D.5
  • 56
    • 30044439885 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe
    • She M, Decker CJ, Chen N, Tumati S, Parker R, et al. (2006) Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe. Nat Struct Mol Biol 13: 63-70.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 63-70
    • She, M.1    Decker, C.J.2    Chen, N.3    Tumati, S.4    Parker, R.5
  • 57
    • 0037121926 scopus 로고    scopus 로고
    • Human Dcp2: A catalytically active mRNA decapping enzyme located in specific cytoplasmic structures
    • van Dijk E, Cougot N, Meyer S, Babajko S, Wahle E, et al. (2002) Human Dcp2: A catalytically active mRNA decapping enzyme located in specific cytoplasmic structures. EMBO J21: 6915-6924.
    • (2002) EMBO , vol.J21 , pp. 6915-6924
    • van Dijk, E.1    Cougot, N.2    Meyer, S.3    Babajko, S.4    Wahle, E.5
  • 58
    • 15444379718 scopus 로고    scopus 로고
    • Processing bodies require RNA for assembly and contain nontranslating mRNAs
    • Teixeira D, Sheth U, Valencia-Sanchez MA, Brengues M, Parker R, (2005) Processing bodies require RNA for assembly and contain nontranslating mRNAs. RNA 11: 371-382.
    • (2005) RNA , vol.11 , pp. 371-382
    • Teixeira, D.1    Sheth, U.2    Valencia-Sanchez, M.A.3    Brengues, M.4    Parker, R.5
  • 59
    • 78650499705 scopus 로고    scopus 로고
    • Cellular stress induces cytoplasmic RNA granules in fission yeast
    • Nilsson D, Sunnerhagen P, (2011) Cellular stress induces cytoplasmic RNA granules in fission yeast. RNA 17: 120-133.
    • (2011) RNA , vol.17 , pp. 120-133
    • Nilsson, D.1    Sunnerhagen, P.2
  • 60
    • 0034638837 scopus 로고    scopus 로고
    • Dynamic shuttling of TIA-1 accompanies the recruitment of mRNA to mammalian stress granules
    • Kedersha N, Cho MR, Li W, Yacono PW, Chen S, et al. (2000) Dynamic shuttling of TIA-1 accompanies the recruitment of mRNA to mammalian stress granules. J Cell Biol 151: 1257-1268.
    • (2000) J Cell Biol , vol.151 , pp. 1257-1268
    • Kedersha, N.1    Cho, M.R.2    Li, W.3    Yacono, P.W.4    Chen, S.5
  • 61
    • 0033611157 scopus 로고    scopus 로고
    • RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules
    • Kedersha NL, Gupta M, Li W, Miller I, Anderson P, (1999) RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules. J Cell Biol 147: 1431-1442.
    • (1999) J Cell Biol , vol.147 , pp. 1431-1442
    • Kedersha, N.L.1    Gupta, M.2    Li, W.3    Miller, I.4    Anderson, P.5
  • 62
    • 9444279617 scopus 로고    scopus 로고
    • Stress granule assembly is mediated by prion-like aggregation of TIA-1
    • Gilks N, Kedersha N, Ayodele M, Shen L, Stoecklin G, et al. (2004) Stress granule assembly is mediated by prion-like aggregation of TIA-1. Mol Biol Cell 15: 5383-5398.
    • (2004) Mol Biol Cell , vol.15 , pp. 5383-5398
    • Gilks, N.1    Kedersha, N.2    Ayodele, M.3    Shen, L.4    Stoecklin, G.5
  • 63
    • 0034710897 scopus 로고    scopus 로고
    • A census of glutamine/asparagine-rich regions: Implications for their conserved function and the prediction of novel prions
    • Michelitsch MD, Weissman JS, (2000) A census of glutamine/asparagine-rich regions: Implications for their conserved function and the prediction of novel prions. Proc Natl Acad Sci U S A 97: 11910-11915.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 11910-11915
    • Michelitsch, M.D.1    Weissman, J.S.2
  • 64
    • 0036444135 scopus 로고    scopus 로고
    • Evidence for general stabilization of mRNAs in response to UV light
    • Bollig F, Winzen R, Kracht M, Ghebremedhin B, Ritter B, et al. (2002) Evidence for general stabilization of mRNAs in response to UV light. FEBS 269: 5830-5839.
    • (2002) FEBS , vol.269 , pp. 5830-5839
    • Bollig, F.1    Winzen, R.2    Kracht, M.3    Ghebremedhin, B.4    Ritter, B.5
  • 65
    • 0033574789 scopus 로고    scopus 로고
    • Control of mRNA decay by heat shock-ubiquitin-proteasome pathway
    • Laroia G, Cuesta R, Brewer G, Schneider RJ, (1999) Control of mRNA decay by heat shock-ubiquitin-proteasome pathway. Science 284: 499-502.
    • (1999) Science , vol.284 , pp. 499-502
    • Laroia, G.1    Cuesta, R.2    Brewer, G.3    Schneider, R.J.4
  • 66
    • 79955623483 scopus 로고    scopus 로고
    • RhoA activation participates in rearrangement of processing bodies and release of nucleated AU-rich mRNAs
    • Takahashi S, Sakurai K, Ebihara A, Kajiho H, Saito K, et al. (2011) RhoA activation participates in rearrangement of processing bodies and release of nucleated AU-rich mRNAs. Nucleic Acids Res 39: 3446-3457.
    • (2011) Nucleic Acids Res , vol.39 , pp. 3446-3457
    • Takahashi, S.1    Sakurai, K.2    Ebihara, A.3    Kajiho, H.4    Saito, K.5
  • 67
    • 13844322292 scopus 로고    scopus 로고
    • Polarisome meets spitzenkorper: Microscopy, genetics, and genomics converge
    • Harris SD, Read ND, Roberson RW, Shaw B, Seiler S, et al. (2005) Polarisome meets spitzenkorper: Microscopy, genetics, and genomics converge. Eukaryot Cell 4: 225-229.
    • (2005) Eukaryot Cell , vol.4 , pp. 225-229
    • Harris, S.D.1    Read, N.D.2    Roberson, R.W.3    Shaw, B.4    Seiler, S.5
  • 68
    • 33947644066 scopus 로고    scopus 로고
    • Hyphal growth: A tale of motors, lipids, and the spitzenkörper
    • Steinberg G, (2007) Hyphal growth: A tale of motors, lipids, and the spitzenkörper. Eukaryot Cell 6: 351-360.
    • (2007) Eukaryot Cell , vol.6 , pp. 351-360
    • Steinberg, G.1
  • 69
    • 0019390955 scopus 로고
    • Ultrastructural analysis of hyphal tip cell growth in fungi: Spitzenkörper, cytoskeleton and endomembranes after freeze-substitution
    • Howard RJ, (1981) Ultrastructural analysis of hyphal tip cell growth in fungi: Spitzenkörper, cytoskeleton and endomembranes after freeze-substitution. J Cell Sci 48: 89-103.
    • (1981) J Cell Sci , vol.48 , pp. 89-103
    • Howard, R.J.1
  • 70
    • 84866869780 scopus 로고    scopus 로고
    • Intrinsically disordered proteins aggregate at fungal cell-to-cell channels and regulate intercellular connectivity
    • Lai J, Koh CH, Tjota M, Pieuchot L, Raman V, et al. (2012) Intrinsically disordered proteins aggregate at fungal cell-to-cell channels and regulate intercellular connectivity. Proc Natl Acad Sci U S A 109: 15781-15786.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 15781-15786
    • Lai, J.1    Koh, C.H.2    Tjota, M.3    Pieuchot, L.4    Raman, V.5
  • 71
    • 35948951960 scopus 로고    scopus 로고
    • Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae
    • Decker CJ, Teixeira D, Parker R, (2007) Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae. J Cell Biol 179: 437-449.
    • (2007) J Cell Biol , vol.179 , pp. 437-449
    • Decker, C.J.1    Teixeira, D.2    Parker, R.3
  • 72
    • 50249131374 scopus 로고    scopus 로고
    • A role for Q/N-rich aggregation-prone regions in P-body localization
    • Reijns MA, Alexander RD, Spiller MP, Beggs JD, (2008) A role for Q/N-rich aggregation-prone regions in P-body localization. J Cell Sci121: 2463-2472.
    • (2008) J Cell Sci , vol.121 , pp. 2463-2472
    • Reijns, M.A.1    Alexander, R.D.2    Spiller, M.P.3    Beggs, J.D.4
  • 73
    • 77955099645 scopus 로고    scopus 로고
    • Localization to, and effects of Pbp1, Pbp4, Lsm12, Dhh1, and Pab1 on stress granules in Saccharomyces cerevisiae
    • Swisher KD, Parker R, (2010) Localization to, and effects of Pbp1, Pbp4, Lsm12, Dhh1, and Pab1 on stress granules in Saccharomyces cerevisiae. PloS One 5: e10006.
    • (2010) PloS One , vol.5
    • Swisher, K.D.1    Parker, R.2
  • 74
    • 84882646874 scopus 로고    scopus 로고
    • Processing body and stress granule assembly occur by independent and differentially regulated pathways in saccharomyces cerevisiae
    • in press
    • Shah KH, Zhang B, Ramachandran V, Herman PK (2012) Processing body and stress granule assembly occur by independent and differentially regulated pathways in saccharomyces cerevisiae. Genetics 112: in press.
    • (2012) Genetics , vol.112
    • Shah, K.H.1    Zhang, B.2    Ramachandran, V.3    Herman, P.K.4


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