ライフサイエンスコーパス: GRF2

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1 ctivated both Ha-Ras and R-Ras in cells, Ras-GRF2 activated only Ha-Ras.

2 ing post-translationally modified, since Ras-GRF2 activated unprocessed R-Ras as effectively as unpro

3 cks transcriptional activation of Jun by Ras-GRF2 and activates ERK1 via a Ras-GRF2 independent pathw

4 using the guanine nucleotide exchange factor GRF2 and two interacting proteins, Ras and calmodulin, a

5 ction is correlated with a decrease in GRF1, GRF2, and GRF3 transcripts.

6 eotide-releasing factor 1 (Ras-GRF1) and Ras-GRF2 are highly similar calcium-stimulated exchange fact

7 The GRF2-binding factor appears to facilitate the binding of

8 n-chip immunoprecipitation assay to identify GRF2-binding partners from complex protein mixtures.

9 h the guanine nucleotide exchange factor Ras-GRF2 by yeast two-hybrid assay, and this interaction is

10 We conclude that GRF1 and GRF2 can form homo- and hetero-oligomers via their DH do

11 ese studies revealed a critical role for the GRF2 CDC25 domain in the induction of TBS-LTP by GRF pro

12 p140 Ras-GRF1 and p130 Ras-GRF2 constitute a family of calcium/calmodulin-regulated

13 Ras-GRF1 and Ras-GRF2 constitute a family of calmodulin-regulated guanine

14 Ras-GRF1 (GRF1) and Ras-GRF2 (GRF2) constitute a family of similar calcium sensors tha

15 of Ras-GRF knock-out mice, we show that Ras-GRF2 contributes predominantly to the induction of NMDAR

16 evealed that both p140 Ras-GRF1 and p130 Ras-GRF2 couple NMDA glutamate receptors (NMDARs) to the act

17 nalysis of chimeras between Ras-GRF1 and Ras-GRF2 demonstrated that a 30-amino acid segment embedded

18 library was isolated which consisted of the GRF2 DH domain and its adjacent ilimaquinone domain.

19 TP and/or LTD in the CA1 hippocampus of Grf1/Grf2 double knock-out mice.

20 alcium/calmodulin regulated Ras-GRF1 and Ras-GRF2 exchange factors, which form AMPA-induced complexes

21 Moreover, Ras-GRF2 failed to activate fully processed R-Ras in vitro.

22 Ras-GRF1 (GRF1) and Ras-GRF2 (GRF2) constitute a family of similar calcium senso

23 fic exchange factors Ras-GRF1 (GRF1) and Ras-GRF2 (GRF2), which are expressed in brain and a restrict

24 RS1), positioned immediately upstream of the GRF2-HSE1 region and only weakly occupied in chromatin,

25 n extract, and forced expression of GRF1 and GRF2 in cultured mammalian cells formed homo- and hetero

26 Jun by Ras-GRF2 and activates ERK1 via a Ras-GRF2 independent pathway.

27 Human Ras-GRF2 is expressed in a variety of tissues and, similar t

28 d reduced excitability in the absence of Ras-GRF2, likely because of lack of inhibition of the I(A) p

29 e direct association between dematin and Ras-GRF2 may provide an alternate mechanism for regulating t

30 tional domain organization, Ras-GRF1 and Ras-GRF2 mediate opposing forms of synaptic plasticity by co

31 Ras-GRF2 mediates signaling from (R)-[(S)-1-(4-bromo-phenyl)

32 the hippocampus, GRF1 promotes LTD, whereas GRF2 promotes theta-burst stimulation-induced LTP (TBS-L

33 ns, WT and various chimeras between GRF1 and GRF2 proteins were tested for their abilities to reconst

34 stable protein-DNA interactions in vivo, the GRF2/REB1 site and the TATA box, despite reducing transc

35 However, deletion of URS1, like mutation of GRF2, shifts the translational setting of an upstream nu

36 The inability of Ras-GRF2 to activate R-Ras was the consequence of the GTPase

37 In addition to detecting GRF2, we also identified calmodulin, demonstrating that

38 Oligomers between GRF1 and GRF2 were detected in a rat brain extract, and forced ex

39 Cells overexpressing FLAG-GRF2 were lysed and then incubated with the anti-FLAG ch

40 y, since R-Ras became more responsive to Ras-GRF2 when it was farnesylated instead of geranylgeranyla

41 ilarly, Ha-Ras became less responsive to Ras-GRF2 when it was geranylgeranylated instead of farnesyla

42 change factors Ras-GRF1 (GRF1) and Ras-GRF2 (GRF2), which are expressed in brain and a restricted num

43 The interaction of GRF2 with calmodulin and Ras was demonstrated, and the l

44 eveloped, and the interaction of immobilized GRF2 with the two analytes was verified by fluorescence

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