ライフサイエンスコーパス: eIF-2

1 orylation of eukaryotic initiation factor-2 (eIF-2).

2 eukaryotic translation initiation factor 2 (eIF-2).

3 a subunit of eukaryotic initiation factor-2 (eIF-2).

4 unction of the translation initiation factor eIF-2.

5 unction of the translation initiation factor eIF-2.

6 ates phosphorylation of the alpha subunit of eIF-2.

7 s similarly phosphorylated exogenously added eIF-2.

8 lpha subunit of eukaryotic initiation factor eIF-2.

9 (GCD11) predicted to alter ligand binding by eIF-2.

10 Five eukaryotic initiation factors (eIF 2, 3, 4A, 4B and 4F) with established functions have

11 However, we found high phosphorylated eIF-2 alpha (eIF-2 alpha[P]) levels in nonstressed pancr

12 necessary, it was not sufficient to promote eIF-2 alpha dephosphorylation in cells.

13 ne phosphatase (PP1), which dephosphorylates eIF-2 alpha during cellular stresses.

14 Phosphorylation of eIF-2 alpha is a classical mechanism for the downregulat

15 its the phosphorylation of the plant encoded eIF-2 alpha kinase (pPKR) as well as plant and human eIF

16 protein synthesis in the presence of active eIF-2 alpha kinases in vitro.

17 Among the four eIF-2 alpha kinases present in mammals, PERK is most hig

18 esis was inhibited by cotransfection with an eIF-2 alpha mutant S51D, a mutant that mimics phosphoryl

19 ression of a nonphosphorylatable S51A mutant eIF-2 alpha partially protected cells from TNF alpha-ind

20 ion of GADD34 in assembling an ER-associated eIF-2 alpha phosphatase that regulates protein translati

21 P1 being a component of the GADD34-assembled eIF-2 alpha phosphatase.

22 GADD34 expression also reversed eIF-2 alpha phosphorylation induced by okadaic acid but

23 n of human GADD34 in cultured cells reversed eIF-2 alpha phosphorylation induced by thapsigargin and

24 ed an absence of GADD34 induction, prolonged eIF-2 alpha phosphorylation, delayed protein synthesis r

25 s-induced apoptosis that is mediated through eIF-2 alpha phosphorylation.

26 pha kinase (pPKR) as well as plant and human eIF-2 alpha phosphorylation.

27 ing in vitro, while sequences containing the eIF-2 alpha similarity region were essential for efficie

28 ion of eukaryotic initiation factor 2 alpha (eIF-2 alpha) is typically associated with stress respons

29 eukaryotic translation initiation factor 2 (eIF-2 alpha), the primary physiological substrate of the

30 eukaryotic translation initiation factor 2, (eIF-2 alpha).

31 unit of translation initiation factor eIF-2 (eIF-2 alpha).

32 d apoptosis, and expression of a S51D mutant eIF-2 alpha, a mutant that mimics phosphorylated eIF-2 a

33 nt S51D, a mutant that mimics phosphorylated eIF-2 alpha, indicating that p67 cannot bypass translati

34 2 alpha, a mutant that mimics phosphorylated eIF-2 alpha, was sufficient to induce apoptosis.

35 gative feedback regulatory loop in which the eIF-2 alpha-controlled inhibition of protein translation

36 sponse targets like BiP are sensitive to the eIF-2 alpha-mediated block in translation.

37 which is paradoxically translated during the eIF-2 alpha-mediated translational block, is required fo

38 the serum-starved cells cannot phosphorylate eIF-2 alpha-subunit as these cells contain p67.

39 iated 67 kDa glycoprotein (p67) protects the eIF-2 alpha-subunit from inhibitory phosphorylation by e

40 This eIF-2 alpha-subunit phosphorylation was not observed whe

41 nhibition mediated by phosphorylation of the eIF-2 alpha-subunit.

42 cose stimulated a rapid dephosphorylation of eIF-2 alpha.

43 f p67 reduced phosphorylation of coexpressed eIF-2 alpha.

44 ting that it may be responsible for the high eIF-2 alpha[P] levels found therein.

45 r, we found high phosphorylated eIF-2 alpha (eIF-2 alpha[P]) levels in nonstressed pancreata of mice.

46 orylated the eukaryotic initiation factor-2 (eIF-2) alpha-subunit.

47 ctors eIF-4A, eIF-4B, eIF-4F, eIF-iso4F, and eIF-2 and the poly(A)-binding protein in the seed, durin

48 complex structure of the eukaryotic factor (eIF-2) and its association with other proteins underlie

49 eukaryotic translation initiation factor 2 (eIF-2) and total shutoff of protein synthesis is observe

50 ty of mammalian cells (also known as DAI, P1-eIF-2, and p68 kinase).

51 to stimulate the hydrolysis of GTP bound to eIF-2 as part of the 43S preinitiation complex.

52 eukaryotic translation initiation factor 2 (eIF-2)-associated 67 kDa glycoprotein (p67) protects the

53 In vitro, eIF-2 binds the initiator methionyl-tRNA in a GTP-depend

54 from phosphorylation of the alpha subunit of eIF-2 by the double-stranded RNA-activated protein kinas

55 gene, which encodes the gamma subunit of the eIF-2 complex and contains a mutation in the G2 motif, o

56 es indeed provide EF-Tu-like function to the eIF-2 complex, and further suggest that the level of Met

57 subunit of eIF-2 revealed that these mutant eIF-2 complexes have a higher intrinsic rate of GTP hydr

58 Eukaryotic translation initiation factor 2 (eIF-2) comprises three non-identical subunits alpha, bet

59 e studies indicate that the gamma-subunit of eIF-2 does indeed provide EF-Tu-like function to the eIF

60 pha subunit of translation initiation factor eIF-2 (eIF-2 alpha).

61 pha subunit of translation initiation factor eIF-2 (eIF-2alpha).

62 tiation factor 2 (IF-2) and eukaryotic IF-2 (eIF-2)/eIF-2B, i.e., the initiation factors involved in

63 EF-Tu, dramatically reduced the affinity of eIF-2 for Met-tRNAi(Met) without affecting the k(off) va

64 For eIF-2[gamma-K250R], the increased off-rate also seen for

65 e 40 S initiation complex (40S.mRNA.MettRNAf.eIF-2.GTP) to promote the hydrolysis of bound GTP with t

66 Phosphorylation of the substrate eIF-2 inhibited the GEF activity of the five-subunit eIF

67 subunit of the translation initiation factor eIF-2, inhibiting its function.

68 on, while modulating the release of GDP from eIF-2 is a key mechanism for regulating translation in e

69 Modulation of GTP hydrolysis by eIF-2 is important during the scanning phase of initiati

70 n kinase (PKR) but that the alpha subunit of eIF-2 is not phosphorylated and that protein synthesis i

71 a subunit of eukaryotic initiation factor-2 (eIF-2) is a well characterized mechanism regulating prot

72 1) The eIF-2 kinase activity was the same in the cells grown in

73 However, the eIF-2 kinase in the cells grown in complete medium and a

74 he effect of overexpression of this cellular eIF-2 kinase inhibitor in an in vivo system using transi

75 a-subunit from inhibitory phosphorylation by eIF-2 kinases, and this promotes protein synthesis in th

76 Archaea appear to posses a fully functional eIF-2 molecule, but they lack the associated GTP recycli

77 tor; and (iii) the alpha subunit in purified eIF-2 phosphorylated in vitro is specifically dephosphor

78 Cycloheximide sharply reduced eIF-2 phosphorylation in response to ER stressors for ab

79 d form of GRP78 and increased sensitivity of eIF-2 phosphorylation in response to ER stressors.

80 ch inhibits translational initiation through eIF-2 phosphorylation without affecting the ER, also pro

81 sylation of GRP78 in parallel with increased eIF-2 phosphorylation.

82 -ribosylation of GRP78 within 90 min without eIF-2 phosphorylation.

83 reitol) resulted in GRP78 deribosylation and eIF-2 phosphorylation.

84 xamining the biochemical activities of yeast eIF-2 purified from wild-type strains and strains harbor

85 t encode mutant forms of the beta subunit of eIF-2 revealed that these mutant eIF-2 complexes have a

86 activating the C. elegans eIF-4G homolog and eIF-2 subunits results in developmental arrest accompani

87 ation of protein synthesis initiation factor eIF-2, suggesting full-length PKR can bind to and be reg

88 Reduced sensitivity of eIF-2 to phosphorylation appeared to derive from the acc

89 GTP hydrolysis that leads to dissociation of eIF-2 x GDP from the initiator-tRNA in the 43S preinitia