메뉴 건너뛰기




Volumn 420, Issue 4, 2012, Pages 768-774

Stress granules contribute to α-globin homeostasis in differentiating erythroid cells

Author keywords

Globin; Erythroid cell; G3BP; HRI eIF2 ; Stress granule

Indexed keywords

ALPHA GLOBIN; ARSENIC TRIOXIDE; CD11B ANTIGEN; CD71 ANTIGEN; FIBRINOGEN RECEPTOR; G3BP PROTEIN; HEME REGULATED KINASE INHIBITOR; INITIATION FACTOR 2ALPHA; INITIATION FACTOR 4E; MESSENGER RNA; PHOSPHOTRANSFERASE INHIBITOR; PROTEIN; UNCLASSIFIED DRUG;

EID: 84859866797     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.03.070     Document Type: Article
Times cited : (16)

References (18)
  • 1
    • 33947584856 scopus 로고    scopus 로고
    • Regulation of protein synthesis by the heme-regulated eIF2α kinase: relevance to anemias
    • Chen J.J. Regulation of protein synthesis by the heme-regulated eIF2α kinase: relevance to anemias. Blood 2007, 109:2693-2699.
    • (2007) Blood , vol.109 , pp. 2693-2699
    • Chen, J.J.1
  • 2
    • 0141504266 scopus 로고    scopus 로고
    • Iron deficiency and erythropoiesis: new diagnostic approaches
    • Brugnara C. Iron deficiency and erythropoiesis: new diagnostic approaches. Clin. Chem. 2003, 49:1573-1578.
    • (2003) Clin. Chem. , vol.49 , pp. 1573-1578
    • Brugnara, C.1
  • 3
    • 20144378698 scopus 로고    scopus 로고
    • Heme-regulated inhibitor kinase-mediated phosphorylation of eukaryotic translation initiation factor 2 inhibits translation, induces stress granule formation, and mediates survival upon arsenite exposure
    • McEwen E., Kedersha N., Song B., et al. Heme-regulated inhibitor kinase-mediated phosphorylation of eukaryotic translation initiation factor 2 inhibits translation, induces stress granule formation, and mediates survival upon arsenite exposure. J. Biol. Chem. 2005, 280:16925-16933.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16925-16933
    • McEwen, E.1    Kedersha, N.2    Song, B.3
  • 4
    • 39949085583 scopus 로고    scopus 로고
    • Stress granules: the Tao of RNA triage
    • Anderson P., Kedersha N. Stress granules: the Tao of RNA triage. Trends Biochem. Sci. 2008, 33:141-150.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 141-150
    • Anderson, P.1    Kedersha, N.2
  • 5
    • 0037451173 scopus 로고    scopus 로고
    • The RasGAP-associated endoribonuclease G3BP assembles stress granules
    • Tourriere H., Chebli K., Zekri L., et al. The RasGAP-associated endoribonuclease G3BP assembles stress granules. J. Cell Biol. 2003, 160:823-831.
    • (2003) J. Cell Biol. , vol.160 , pp. 823-831
    • Tourriere, H.1    Chebli, K.2    Zekri, L.3
  • 6
    • 13144276292 scopus 로고    scopus 로고
    • Rasputin, more promiscuous than ever: a review of G3BP
    • Irvine K., Stirling R., Hume D., et al. Rasputin, more promiscuous than ever: a review of G3BP. Int. J. Dev. Biol. 2004, 48:1065-1077.
    • (2004) Int. J. Dev. Biol. , vol.48 , pp. 1065-1077
    • Irvine, K.1    Stirling, R.2    Hume, D.3
  • 7
    • 0033048950 scopus 로고    scopus 로고
    • Upregulation of the RAS-GTPase activating protein (GAP)-binding protein (G3BP) in proliferating RPE cells
    • Kociok N., Esser P., Unfried K., et al. Upregulation of the RAS-GTPase activating protein (GAP)-binding protein (G3BP) in proliferating RPE cells. J. Cell. Biochem. 1999, 74:194-201.
    • (1999) J. Cell. Biochem. , vol.74 , pp. 194-201
    • Kociok, N.1    Esser, P.2    Unfried, K.3
  • 8
    • 25444523445 scopus 로고    scopus 로고
    • Control of fetal growth and neonatal survival by the RasGAP-associated endoribonuclease G3BP
    • Zekri L., Chebli K., Tourriere H., et al. Control of fetal growth and neonatal survival by the RasGAP-associated endoribonuclease G3BP. Mol. Cell. Biol. 2005, 25:8703-8716.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8703-8716
    • Zekri, L.1    Chebli, K.2    Tourriere, H.3
  • 9
    • 38349088899 scopus 로고    scopus 로고
    • Identification of RPS14 as a 5q-syndrome gene by RNA interference screen
    • Ebert B.L., Pretz J., Bosco J., et al. Identification of RPS14 as a 5q-syndrome gene by RNA interference screen. Nature 2008, 451:335-339.
    • (2008) Nature , vol.451 , pp. 335-339
    • Ebert, B.L.1    Pretz, J.2    Bosco, J.3
  • 10
    • 20444402200 scopus 로고    scopus 로고
    • An RNA interference model of RPS19 deficiency in diamond-blackfan anemia recapitulates defective hematopoiesis and rescue by dexamethasone: identification of dexamethasone-responsive genes by microarray
    • Ebert B.L., Lee M.M., Pretz J.L., et al. An RNA interference model of RPS19 deficiency in diamond-blackfan anemia recapitulates defective hematopoiesis and rescue by dexamethasone: identification of dexamethasone-responsive genes by microarray. Blood 2005, 105:4620-4626.
    • (2005) Blood , vol.105 , pp. 4620-4626
    • Ebert, B.L.1    Lee, M.M.2    Pretz, J.L.3
  • 11
    • 53349165578 scopus 로고    scopus 로고
    • A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly
    • Ohn T., Kedersha N., Hickman T., et al. A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly. Nat. Cell Biol. 2008, 10:1224-1231.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1224-1231
    • Ohn, T.1    Kedersha, N.2    Hickman, T.3
  • 12
    • 9444279617 scopus 로고    scopus 로고
    • Stress granule assembly is mediated by prion-like aggregation of TIA-1
    • Gilks N., Kedersha N., Ayodele M., et al. Stress granule assembly is mediated by prion-like aggregation of TIA-1. Mol. Biol. Cell 2004, 15:5383-5398.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5383-5398
    • Gilks, N.1    Kedersha, N.2    Ayodele, M.3
  • 13
    • 22344455246 scopus 로고    scopus 로고
    • Stress granules and processing bodies are dynamically linked sites of mRNP remodeling
    • Kedersha N., Stoecklin G., Ayodele M., et al. Stress granules and processing bodies are dynamically linked sites of mRNP remodeling. J. Cell Biol. 2005, 169:871-884.
    • (2005) J. Cell Biol. , vol.169 , pp. 871-884
    • Kedersha, N.1    Stoecklin, G.2    Ayodele, M.3
  • 14
    • 41749089797 scopus 로고    scopus 로고
    • Reprogramming mRNA translation during stress
    • Yamasaki S., Anderson P. Reprogramming mRNA translation during stress. Curr. Opin. Cell Biol. 2008, 20:222-226.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 222-226
    • Yamasaki, S.1    Anderson, P.2
  • 15
    • 0028148498 scopus 로고
    • Erythroid cell-specific determinants of alpha-globin mRNA stability
    • Weiss I.M., Liebhaber S.A. Erythroid cell-specific determinants of alpha-globin mRNA stability. Mol. Cell. Biol. 1994, 14:8123-8132.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 8123-8132
    • Weiss, I.M.1    Liebhaber, S.A.2
  • 16
    • 0033031221 scopus 로고    scopus 로고
    • Assembly of the alpha-globin mRNA stability complex reflects binary interaction between the pyrimidine-rich 3' untranslated region determinant and poly(C) binding protein alphaCP
    • Chkheidze A.N., Lyakhov D.L., Makeyev A.V., et al. Assembly of the alpha-globin mRNA stability complex reflects binary interaction between the pyrimidine-rich 3' untranslated region determinant and poly(C) binding protein alphaCP. Mol. Cell. Biol. 1999, 19:4572-4581.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4572-4581
    • Chkheidze, A.N.1    Lyakhov, D.L.2    Makeyev, A.V.3
  • 17
    • 33846996020 scopus 로고    scopus 로고
    • An erythroid-enriched endoribonuclease (ErEN) involved in alpha-globin mRNA turnover
    • Liu H., Kiledjian M. An erythroid-enriched endoribonuclease (ErEN) involved in alpha-globin mRNA turnover. Protein Pept. Lett. 2007, 14:131-136.
    • (2007) Protein Pept. Lett. , vol.14 , pp. 131-136
    • Liu, H.1    Kiledjian, M.2
  • 18
    • 49549097347 scopus 로고    scopus 로고
    • Erythropoietin receptor-mediated Egr-1 activation: structural requirements and functional implications
    • Schulze C., Buchse T., Mikkat S., et al. Erythropoietin receptor-mediated Egr-1 activation: structural requirements and functional implications. Cell. Signal. 2008, 20:1848-1854.
    • (2008) Cell. Signal. , vol.20 , pp. 1848-1854
    • Schulze, C.1    Buchse, T.2    Mikkat, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.