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Volumn 1725, Issue 2, 2005, Pages 174-181

Interdomain interactions regulate the activation of the heme-regulated eIF2α kinase

Author keywords

Carbon monoxide; Heme; Heme binding domain; Heme regulated eIF2 kinase; Interdomain interaction; Nitric oxide

Indexed keywords

AMINO ACID; CARBON MONOXIDE; HEME; HEMIN; MUTANT PROTEIN; NITRIC OXIDE; PROTEIN KINASE R;

EID: 24344444080     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2005.07.011     Document Type: Article
Times cited : (16)

References (24)
  • 1
    • 0033213918 scopus 로고    scopus 로고
    • Translation initiation: Adept at adapting
    • T.E. Dever Translation initiation: adept at adapting Trends Biochem. Sci. 24 1999 398 403
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 398-403
    • Dever, T.E.1
  • 2
    • 0028935374 scopus 로고
    • Regulation of protein synthesis by heme-regulated eIF-2 alpha kinase
    • J.J. Chen, and I.M. London Regulation of protein synthesis by heme-regulated eIF-2 alpha kinase Trends Biochem. Sci. 20 1995 105 108
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 105-108
    • Chen, J.J.1    London, I.M.2
  • 3
    • 0030997120 scopus 로고    scopus 로고
    • Hsp90 is obligatory for the heme-regulated eIF-2alpha kinase to acquire and maintain an activable conformation
    • S. Uma, S.D. Hartson, J.J. Chen, and R.L. Matts Hsp90 is obligatory for the heme-regulated eIF-2alpha kinase to acquire and maintain an activable conformation J. Biol. Chem. 272 1997 11648 11656
    • (1997) J. Biol. Chem. , vol.272 , pp. 11648-11656
    • Uma, S.1    Hartson, S.D.2    Chen, J.J.3    Matts, R.L.4
  • 4
    • 0032766645 scopus 로고    scopus 로고
    • Dual role for Hsc70 in the biogenesis and regulation of the heme-regulated kinase of the α subunit of eukaryotic translation initiation factor 2
    • S. Uma, V. Thulasiraman, and R.L. Matts Dual role for Hsc70 in the biogenesis and regulation of the heme-regulated kinase of the α subunit of eukaryotic translation initiation factor 2 Mol. Cell. Biol. 19 1999 5861 5871
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5861-5871
    • Uma, S.1    Thulasiraman, V.2    Matts, R.L.3
  • 6
    • 0037188421 scopus 로고    scopus 로고
    • Evidence that protein phosphatase 5 functions to negatively modulate the maturation of the Hsp90-dependent heme-regulated eIF2alpha kinase
    • J. Shao, S.D. Hartson, and R.L. Matts Evidence that protein phosphatase 5 functions to negatively modulate the maturation of the Hsp90-dependent heme-regulated eIF2alpha kinase Biochemistry 41 2002 6770 6779
    • (2002) Biochemistry , vol.41 , pp. 6770-6779
    • Shao, J.1    Hartson, S.D.2    Matts, R.L.3
  • 7
    • 0035166679 scopus 로고    scopus 로고
    • Translation initiation control by heme-regulated eukaryotic initiation factor 2alpha kinase in erythroid cells under cytoplasmic stresses
    • L. Lu, A.P. Han, and J.J. Chen Translation initiation control by heme-regulated eukaryotic initiation factor 2alpha kinase in erythroid cells under cytoplasmic stresses Mol. Cell. Biol. 21 2001 7971 7980
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7971-7980
    • Lu, L.1    Han, A.P.2    Chen, J.J.3
  • 8
    • 0035949630 scopus 로고    scopus 로고
    • Multiple autophosphorylation is essential for the formation of the active and stable homodimer of heme-regulated eIF2alpha kinase
    • B.N. Bauer, M. Rafie-Kolpin, L. Lu, A. Han, and J.J. Chen Multiple autophosphorylation is essential for the formation of the active and stable homodimer of heme-regulated eIF2alpha kinase Biochemistry 40 2001 11543 11551
    • (2001) Biochemistry , vol.40 , pp. 11543-11551
    • Bauer, B.N.1    Rafie-Kolpin, M.2    Lu, L.3    Han, A.4    Chen, J.J.5
  • 9
    • 0019405290 scopus 로고
    • Relationship between phosphorylation and activity of heme-regulated eukaryotic initiation factor 2 alpha kinase
    • R. Fagard, and I.M. London Relationship between phosphorylation and activity of heme-regulated eukaryotic initiation factor 2 alpha kinase Proc. Natl. Acad. Sci. U. S. A. 78 1981 866 870
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , pp. 866-870
    • Fagard, R.1    London, I.M.2
  • 10
    • 0026725775 scopus 로고
    • Regulation of heme-controlled eukaryotic polypeptide chain initiation factor 2 alpha-subunit kinase of reticulocyte lysates
    • R. Mendez, A. Moreno, and C. de Haro Regulation of heme-controlled eukaryotic polypeptide chain initiation factor 2 alpha-subunit kinase of reticulocyte lysates J. Biol. Chem. 267 1992 11500 11507
    • (1992) J. Biol. Chem. , vol.267 , pp. 11500-11507
    • Mendez, R.1    Moreno, A.2    De Haro, C.3
  • 11
    • 0034681436 scopus 로고    scopus 로고
    • Two heme-binding domains of heme-regulated eukaryotic initiation factor-2alpha kinase. N terminus and kinase insertion
    • M. Rafie-Kolpin, P.J. Chefalo, Z. Hussain, J. Hahn, S. Uma, R.L. Matts, and J.J. Chen Two heme-binding domains of heme-regulated eukaryotic initiation factor-2alpha kinase. N terminus and kinase insertion J. Biol. Chem. 275 2000 5171 5178
    • (2000) J. Biol. Chem. , vol.275 , pp. 5171-5178
    • Rafie-Kolpin, M.1    Chefalo, P.J.2    Hussain, Z.3    Hahn, J.4    Uma, S.5    Matts, R.L.6    Chen, J.J.7
  • 12
    • 0033957156 scopus 로고    scopus 로고
    • The N-terminal region of the heme-regulated eIF2alpha kinase is an autonomous heme binding domain
    • S. Uma, R.L. Matts, Y. Guo, S. White, and J.J. Chen The N-terminal region of the heme-regulated eIF2alpha kinase is an autonomous heme binding domain Eur. J. Biochem. 267 2000 498 506
    • (2000) Eur. J. Biochem. , vol.267 , pp. 498-506
    • Uma, S.1    Matts, R.L.2    Guo, Y.3    White, S.4    Chen, J.J.5
  • 14
    • 0035805526 scopus 로고    scopus 로고
    • The heme-regulated eukaryotic initiation factor 2alpha kinase. a potential regulatory target for control of protein synthesis by diffusible gases
    • S. Uma, B.G. Yun, and R.L. Matts The heme-regulated eukaryotic initiation factor 2alpha kinase. A potential regulatory target for control of protein synthesis by diffusible gases J. Biol. Chem. 276 2001 14875 14883
    • (2001) J. Biol. Chem. , vol.276 , pp. 14875-14883
    • Uma, S.1    Yun, B.G.2    Matts, R.L.3
  • 16
    • 0030021905 scopus 로고    scopus 로고
    • Binding of nitric oxide and carbon monoxide to soluble guanylate cyclase as observed with resonance Raman spectroscopy
    • G. Deinum, J.R. Stone, G.T. Babcock, and M.A. Marletta Binding of nitric oxide and carbon monoxide to soluble guanylate cyclase as observed with resonance Raman spectroscopy Biochemistry 35 1996 1540 1547
    • (1996) Biochemistry , vol.35 , pp. 1540-1547
    • Deinum, G.1    Stone, J.R.2    Babcock, G.T.3    Marletta, M.A.4
  • 17
    • 1342282967 scopus 로고    scopus 로고
    • Identification of crucial histidines for heme binding in the N-terminal domain of the heme-regulated eIF2alpha kinase
    • T. Inuzuka, B.G. Yun, H. Ishikawa, S. Takahashi, H. Hori, R.L. Matts, K. Ishimori, and I. Morishima Identification of crucial histidines for heme binding in the N-terminal domain of the heme-regulated eIF2alpha kinase J. Biol. Chem. 279 2004 6778 6782
    • (2004) J. Biol. Chem. , vol.279 , pp. 6778-6782
    • Inuzuka, T.1    Yun, B.G.2    Ishikawa, H.3    Takahashi, S.4    Hori, H.5    Matts, R.L.6    Ishimori, K.7    Morishima, I.8
  • 18
    • 1942469554 scopus 로고    scopus 로고
    • Activation of heme-regulated eukaryotic initiation factor 2alpha kinase by nitric oxide is induced by the formation of a five-coordinate NO-heme complex: Optical absorption, electron spin resonance, and resonance Raman spectral studies
    • J. Igarashi, A. Sato, T. Kitagawa, T. Yoshimura, S. Yamauchi, I. Sagami, and T. Shimizu Activation of heme-regulated eukaryotic initiation factor 2alpha kinase by nitric oxide is induced by the formation of a five-coordinate NO-heme complex: optical absorption, electron spin resonance, and resonance Raman spectral studies J. Biol. Chem. 279 2004 15752 15762
    • (2004) J. Biol. Chem. , vol.279 , pp. 15752-15762
    • Igarashi, J.1    Sato, A.2    Kitagawa, T.3    Yoshimura, T.4    Yamauchi, S.5    Sagami, I.6    Shimizu, T.7
  • 19
    • 0038728800 scopus 로고    scopus 로고
    • Autophosphorylation of threonine 485 in the activation loop is essential for attaining eIF2alpha kinase activity of HRI
    • M. Rafie-Kolpin, A.P. Han, and J.J. Chen Autophosphorylation of threonine 485 in the activation loop is essential for attaining eIF2alpha kinase activity of HRI Biochemistry 42 2003 6536 6544
    • (2003) Biochemistry , vol.42 , pp. 6536-6544
    • Rafie-Kolpin, M.1    Han, A.P.2    Chen, J.J.3
  • 20
    • 0026699920 scopus 로고
    • Effects of hemin and porphyrin compounds on intersubunit disulfide formation of heme-regulated eIF-2 alpha kinase and the regulation of protein synthesis in reticulocyte lysates
    • J.M. Yang, I.M. London, and J.J. Chen Effects of hemin and porphyrin compounds on intersubunit disulfide formation of heme-regulated eIF-2 alpha kinase and the regulation of protein synthesis in reticulocyte lysates J. Biol. Chem. 267 1992 20519 20524
    • (1992) J. Biol. Chem. , vol.267 , pp. 20519-20524
    • Yang, J.M.1    London, I.M.2    Chen, J.J.3
  • 21
    • 0024333869 scopus 로고
    • Disulfide bond formation in the regulation of eIF-2 alpha kinase by heme
    • J.J. Chen, J.M. Yang, R. Petryshyn, N. Kosower, and I.M. London Disulfide bond formation in the regulation of eIF-2 alpha kinase by heme J. Biol. Chem. 264 1989 9559 9564
    • (1989) J. Biol. Chem. , vol.264 , pp. 9559-9564
    • Chen, J.J.1    Yang, J.M.2    Petryshyn, R.3    Kosower, N.4    London, I.M.5
  • 23
    • 3042656869 scopus 로고    scopus 로고
    • Novobiocin induces a distinct conformation of Hsp90 and alters Hsp90-cochaperone-client interactions
    • B.G. Yun, W. Huang, N. Leach, S.D. Hartson, and R.L. Matts Novobiocin induces a distinct conformation of Hsp90 and alters Hsp90-cochaperone-client interactions Biochemistry 43 2004 8217 8229
    • (2004) Biochemistry , vol.43 , pp. 8217-8229
    • Yun, B.G.1    Huang, W.2    Leach, N.3    Hartson, S.D.4    Matts, R.L.5
  • 24
    • 0029785485 scopus 로고    scopus 로고
    • Histidyl-tRNA synthetase-related sequences in GCN2 protein kinase regulate in vitro phosphorylation of eIF-2
    • S. Zhu, A.Y. Sobolev, and R.C. Wek Histidyl-tRNA synthetase-related sequences in GCN2 protein kinase regulate in vitro phosphorylation of eIF-2 J. Biol. Chem. 271 1996 24989 24994
    • (1996) J. Biol. Chem. , vol.271 , pp. 24989-24994
    • Zhu, S.1    Sobolev, A.Y.2    Wek, R.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.