ライフサイエンスコーパス: RasGAP

1 RasGAP (Ras GTPase-activating protein) is a negative reg

2 RasGAP and Shc were also found to associate with GRB2 in

3 RasGAP residues 890-902 (block 3A) were observed to be h

4 RasGAP used its N-terminal Src homology 2 domain to bind

5 RasGAP, that responds to activation of PDGFR-beta but no

6 RasGAP, which associates with PDGFRbeta but not PDGFRalp

7 Neurofibromin, the product of NF1, acts as a RasGAP and suppresses growth; inactivating mutations in

8 melanoma exomes identified RASA2, encoding a RasGAP, as a tumor-suppressor gene mutated in 5% of mela

9 ated and co-immunoprecipitates with Bcr-Abl, RasGAP, and CrkL, a Src homology 2 (SH2) and SH3 domain-

10 ors of the EGFR pathway, including c-Cbl and RasGAP, and more than that of MAPK phosphatase.

11 The opposing actions of CSW and RasGAP modulate the strength of the Torso signal, contri

12 tigated the interaction between p62(dok) and RasGAP and the consequences of p62(dok) tyrosine phospho

13 n mast cells via recruitment of p62(dok) and RasGAP.

14 Furthermore, PLC gamma and RasGAP negatively modulate PDGF-dependent PI3K activatio

15 binds directly to the SH2 domain of Nck and RasGAP and indirectly to NIK bound to the SH3 domain of

16 ast, receptors that associated with PI3K and RasGAP or PI3K and PLC gamma displayed a greatly reduced

17 light the dynamic balance between RasGEF and RasGAP in these T-ALLs and put forth a new model in whic

18 activation of the PLCgamma, PI3K, SHP2, and RasGAP pathways still retain partial ability to induce 6

19 1 (TIA-1), TIA1-related protein (TIAR), and RasGAP-SH3 domain binding protein 1 (G3BP1) are required

20 ropose that the physical interaction between RasGAP and FLN-C facilitates an interaction between G3BP

21 These results highlight the role played by RasGAP in FGFR signaling and how graded stress intensiti

22 ited (i) the cleavage of RasGTP to RasGDP by RasGAP; (ii) the binding to RasGTP of Raf-1, phosphatidy

23 are activated by RasGEFs and inactivated by RasGAPs, which stimulate the hydrolysis of RasGTP to ina

24 romin that is present in all known canonical RasGAPs.

25 of cells to form stress granules by cleaving RasGAP-SH3-binding protein (G3BP).

26 Under mild stress conditions, RasGAP is cleaved by caspase-3 at position 455.

27 Consequently, RasGAP undergoes a conformational change that results in

28 forth a new model in which IL-2/7/9 decrease RasGAP activity.

29 stress intensities, by generating different RasGAP fragments, can positively or negatively impact th

30 misregulation by using cells with disrupted RasGAP activity.

31 ntly to a complex between NIK/Nck, p62(dok), RasGAP, and an unidentified 145-kDa tyrosine-phosphoryla

32 Pase-activating proteins (RasGAPs) with dual RasGAP/RapGAP specificity, is epigenetically silenced in

33 In contrast to mice lacking either RasGAP alone in T cells, double-deficient mice developed

34 3K as well as one additional protein, either RasGAP, SHP-2, or PLC gamma.

35 pin RNA interference to knock out endogenous RasGAP expression.

36 Rasal and Ras in the membrane essential for RasGAP activation, but direct and Ca-dependent interacti

37 development, supporting an effector role for RasGAP.

38 be provoked by the release of cdk7 mRNA from RasGAP SH3 domain-binding protein, G3BP, and its subsequ

39 und that huntingtin is associated with Grb2, RasGAP, and tyrosine-phosphorylated EGF receptor.

40 first time to our knowledge, the entire HRas-RasGAP protein complex in a QM/MM simulation context.

41 e involved in GTP hydrolysis within the HRas.RasGAP system is analyzed using a tailored approach base

42 entical to p62(dok-1), a recently identified RasGAP binding protein from CML cells, and analysis of t

43 s 1099-1129 have no structural equivalent in RasGAP and are seen to form an extension at one end of t

44 overexpression of Dok-1 that was mutated in RasGAP-binding domain.

45 signaling or regulatory proteins, including RasGAP, AP-2, p53BP-2 (p53-binding protein-2), interleuk

46 at tyrosine-phosphorylated p62(dok) inhibits RasGAP activity.

47 ted in infected cells despite lacking intact RasGAP SH3-domain binding protein 1 (G3BP) and eukaryoti

48 and lipids, which simultaneously induces its RasGAP activity through a yet unknown mechanism.

49 activation of phosphatidylinositol 3-kinase, RasGAP, SHP-2, phospholipase C-gamma, and Src are not ne

50 Hence, full-length RasGAP favors Akt activity by shielding it from deactiva

51 eins but observed the stress granule markers RasGAP SH3-binding protein and phosphorylated eukaryotic

52 not at the cell surface to inhibit multiple RasGAPs, resulting in sustained Ras activation.

53 se-activating protein (SynGAP) is a neuronal RasGAP (Ras GTPase-activating protein) that is selective

54 firming that exon 23a inclusion inhibits Nf1 RasGAP activity in vivo as it does in cultured cells.

55 stem cell-derived neurons indicated that Nf1 RasGAP activity is modulated by the highly regulated alt

56 for the Ras small G proteins, yet it has no RasGAP activity and binds to the Rho family small G prot

57 IQGAP1, a novel RasGAP-related protein that interacts with the cytoskele

58 d cells via recruitment and/or activation of RasGAP, and that preventing this negative feedback mecha

59 tyrosine phosphorylation on the activity of RasGAP.

60 DF-1alpha/CXCL12 enhanced the association of RasGAP with Pyk2.

61 We found that binding of RasGAP to the wild-type betaPDGFR was decreased; the act

62 the phosphotyrosine required for binding of RasGAP.

63 the rapid recruitment to the cytoskeleton of RasGAP (p120RasGAP), its associated protein of 190 kilod

64 is achieved through the dephosphorylation of RasGAP binding sites at the level of the plasma membrane

65 We find that the Drosophila homolog of RasGAP associates with pY918 and is a negative effector

66 nvestigated in Xenopus oocytes the impact of RasGAP and its fragments on FGF1-mediated signaling duri

67 st that SC1 works through dual inhibition of RasGAP and ERK1.

68 Knockdown of RasGAP or FLN-C, or severing their interaction, resulted

69 Knockdown of RasGAP resulted in a similar enhancement of CrkI transfo

70 On the other hand, overexpression of RasGAP induced a Cdk7- and FLN-C-dependent growth.

71 Overexpression of RasGAP or a mutant lacking the GTPase-activating domain

72 To identify partners of RasGAP we used it as the bait in a yeast two-hybrid scre

73 on fibronectin diminished the recruitment of RasGAP to the betaPDGFR, we focused on SHP-2 since it de

74 most highly conserved amino acid residues of RasGAP were changed by mutation.

75 indicate a previously unappreciated role of RasGAP in antagonizing indirect activation of PDGFRbeta,

76 To determine the role of RasGAP in receptor-mediated activation of Akt, we used s

77 de between the active anticancer sequence of RasGAP and DLC1.

78 Previous structural studies of RasGAP have failed to clearly localize sites of Ras inte

79 e phosphorylation-dependent translocation of RasGAP to the plasma membrane, to its substrate (GTP-Ras

80 anoma driver and highlight the importance of RasGAPs in cancer.

81 hese studies highlight the expanding role of RasGAPs and reveal an alternative mechanism of activatin

82 studies indicate that SH3 domains of Grb2 or RasGAP are required for their binding to huntingtin.

83 p120 RasGAP (GTPase-activating protein), which contains an SH

84 The caspase-3/p120 RasGAP module is a stress sensor switch.

85 rc homology 3 domain of p200 RhoGAP and p120 RasGAP, respectively.

86 RASA1 (also known as p120 RasGAP) is a Ras GTPase-activating protein that function

87 ations of the RASA1 gene, which encodes p120 RasGAP (RASA1), a negative regulator of the Ras small GT

88 is very similar to the GAP domains from p120 RasGAP, neurofibromin, and SynGAP.

89 nd the SH2 domains of the Ras inhibitor p120 RasGAP.

90 se model to investigate the role of the p120 RasGAP (RASA1) in T cells.

91 00 RhoGAP that disrupt interaction with p120 RasGAP abolish its Ras activation and cell transforming

92 kDa protein that stably associates with p120 RasGAP and regulates actin dynamics through members of t

93 p200 RhoGAP co-localizes with p120 RasGAP in cells and forms a complex with p120 RasGAP, an

94 hesize that the association of FAK with p120 RasGAP may facilitate Ras activity.

95 asGAP in cells and forms a complex with p120 RasGAP, and this interaction is mediated by the C-termin

96 PXXP motifs, and the ability to bind to p120(RasGAP).

97 RAFTK is associated with p190 RhoGAP (p190), RasGAP and ErbB-2, and plays an essential role in mediat

98 ceptor-associated proteins such as PLCgamma, RasGAP, Shc, and SHP-2 and for maximal activation of Erk

99 exinA2 co-expressed by GCs, and the PlexinA2-RasGAP activity is necessary to suppress spinogenesis.

100 protein is a Ras GTPase-activating protein (RasGAP) [2].

101 NF1 encodes a Ras GTPase-activating protein (RasGAP) and its loss drives cancer by activating Ras.

102 tudies of the Ras GTPase activating protein (RasGAP) and the elongation factor-Tu (EF-Tu) with a 1 W

103 ecruitment of Ras GTPase-activating protein (RasGAP) by Dok-1, and inhibited activation of the mitoge

104 to a putative Ras GTPase-activating protein (RasGAP) from the fission yeast Schizosaccharomyces pombe

105 t loss of the Ras GTPase-activating protein (RasGAP) gene DAB2IP induces metastatic prostate cancer i

106 reported that Ras GTPase-activating protein (RasGAP) is involved in a pathway that regulates total ce

107 s not bind to Ras GTPase-activating protein (RasGAP) upon phosphorylation.

108 e, encoding a Ras GTPase activating protein (RasGAP), and elucidate the mechanism producing crisis ep

109 ates with the Ras GTPase-activating protein (RasGAP), but only when p62(dok) is tyrosine phosphorylat

110 ts, including Ras GTPase-activating protein (RasGAP), cyclin-dependent kinase 9 (Cdk9), fibronectin,

111 gment of p120 Ras GTPase-activating protein (RasGAP), sensitizes tumor cells to apoptosis induced by

112 de is the Nf1 Ras GTPase activating protein (RasGAP), which attenuates Ras/ERK signaling by convertin

113 A 62-kDa Ras GTPase-activating protein (RasGAP)-associated protein is tyrosine-phosphorylated un

114 catalyzed by Ras GTPase-activating protein (RasGAP).

115 omains of the Ras GTPase-activating protein (RasGAP).

116 unctions as a Ras-GTPase activating protein (RasGAP).

117 ween Ras and its GTPase-activating proteins (RasGAP and NF1) has provided important insights into the

118 nknown which Ras GTPase-activating proteins (RasGAPs) inactivate Ras in T cells.

119 Ras GTPase-activating proteins (RasGAPs) inhibit signal transduction initiated through t

120 subfamily of Ras GTPase-activating proteins (RasGAPs) with dual RasGAP/RapGAP specificity, is epigene

121 amma), the GTPase-activating protein of Ras (RasGAP), and the tyrosine phosphatase SHP-2.

122 e Cdc42-Cdc42GAP complex, as well as the Ras-RasGAP complex, it has been proposed that an arginine re

123 raction similar to that displayed in the Ras-RasGAP complex, we created an energy-minimized model of

124 action of Rasal with membranes induces Rasal RasGAP activity by spatial and conformational regulation

125 binds to SHIP and both Dok1 and Dok2 recruit RasGAP, which mediates the inhibition of the Ras/MAPK pa

126 rom associating with the negative regulator, RasGAP (the GTPase-activating protein of Ras).

127 dentity with almost the entire S. pombe sar1 RasGAP homolog.

128 that SynGAP, an excitatory synapse-specific RasGAP, regulates AMPAR trafficking, silent synapse numb

129 It has been proposed that RasGAP may also function as an effector of Ras activity.

130 In this paper, we report that RasGAP (GTPase-activating protein of Ras) prevented indi

131 This suggests that RasGAP and PKA may mediate common pathways that regulate

132 PDGFR, which in turn decreases the time that RasGAP interacts with the receptor.

133 g (CRIB) motif-containing molecules, and the RasGAP domain containing IQGAP1 and IQGAP2.

134 e p21-binding domains of PAK1, PAK2, and the RasGAP-related domain of IQGAP1, which all cause signifi

135 d p21(cdc42/rac)-activated kinase 1, and the RasGAP-related domain of IQGAP1, which all inhibit the i

136 nase PAK, the tyrosine kinase ACK-2, and the RasGAP-related protein IQGAP.

137 A cDNA for p62(dok), reported to be the RasGAP-associated 62-kDa protein, was recently cloned fr

138 Using chimeric FcgammaRIIB containing the RasGAP-binding domain of p62dok, we demonstrate that p62

139 This gene encodes the RasGAP Neurofibromin (NF1).

140 GAP (trans-glutamine); this differs from the RasGAP mechanism, where the cis-glutamine is also import

141 ion, it appears that the role of p190 in the RasGAP signaling complex is to promote additional protei

142 g GAP/GEF proteins at the PSD, including the RasGAP Syngap1, the ArfGAP Agap2, and the RhoGEF Kalirin

143 However, which members of the RasGAP family act as negative regulators of T cell respo

144 proteins in vivo by genetic deletion of the RasGAP protein Nf1 and examined mice doubly deficient in

145 haracterized the Drosophila homologue of the RasGAP-binding protein G3BP encoded by rasputin (rin).

146 to increased tyrosine phosphorylation of the RasGAP-binding protein p62dok, with a concomitant increa

147 the expression of a noncleavable form of the RasGAP-SH3 domain binding protein in PV-infected cells e

148 d the interaction between RhoA and p190, the RasGAP binding phosphoprotein which has been implicated

149 erved ubiquitination pathways regulating the RasGAP proteins Ira2 (in yeast) and neurofibromin (in hu

150 stingly, a mutant receptor that restores the RasGAP-binding site promotes induction of an independent

151 Here, we report that the RasGAP gene, RASAL2, functions as a tumor and metastasis

152 s is part of the cell's compass and that the RasGAP-mediated regulation of Ras activity affects direc

153 In contrast to the RasGAP mechanism, an accumulation of a state in which ph

154 ides in p190 that bind simultaneously to the RasGAP SH2 domains upon p190 phosphorylation.

155 n ring, and patches become enlarged when the RasGAP NF1 is mutated, showing that Ras plays an instruc

156 udy, we investigated potential roles for the RasGAPs RASA1 and neurofibromin 1 (NF1) in T cells throu

157 This RasGAP-derived peptide, by targeting the deleted in live

158 We evaluated intracellular signaling through RasGAP-associated protein p62Dok-1 (downstream of tyrosi

159 of Dok-related proteins exists that bind to RasGAP and may mediate the effects of p210(bcr-abl) in C

160 ith a concomitant increase in its binding to RasGAP.

161 We used RasGAP SH3-binding protein (G3BP) overexpression to indu

162 osine residues that are involved in in vitro RasGAP binding and have found that tyrosine-phosphorylat

163 dependently of its ability to associate with RasGAP and Nck.

164 tor-phosphorylated IRS5/DOK4 associates with RasGAP, Crk, Src, and Fyn, but not phosphatidylinositol

165 , preventing PDGFRbeta from associating with RasGAP allowed it to signal enduringly and drive pathoge

166 yrosine phosphorylation and association with RasGAP are observed, suggesting that SHIP may mediate Fc

167 yrosine phosphorylation and association with RasGAP, adaptor protein p46Nck, and Crk-L in Jurkat T ce

168 promote additional protein interactions with RasGAP via its SH3 domain.