ライフサイエンスコーパス: Ran GTPase

1 in (a guanine nucleotide-exchange factor for Ran-GTPase).

2 h supporting binding of exportin-6 (XPO6) to RAN GTPase.

3 guanine nucleotide exchange factor (GEF) for Ran GTPase.

4 s the mechanism of substrate displacement by Ran GTPase.

5 hat it was a CRM-1-dependent event driven by Ran GTPase.

6 RanGAP1 is the activating protein for the Ran GTPase.

7 y-dependent process, but may not involve the RAN GTPase.

8 o the guanine nucleotide exchange factor for Ran GTPase.

9 nsitive to the nucleotide-bound state of the Ran GTPase.

10 nd by a dominant-negative mutant form of the Ran GTPase.

11 lly interact with both the NES motif and the Ran GTPase.

12 o leptomycin B and nucleotide-bound state of Ran-GTPase.

13 tinal cyclophilin-related protein that binds Ran-GTPase.

14 ng five subfamilies: Ras, Rho, Arf, Rab, and Ran-GTPases.

15 e show that this process is regulated by the Ran GTPase, a conserved mediator of chromatin signal, an

16 d but clearly involves L binding to cellular Ran GTPase, a critical factor of active NCT.

17 Without Ran GTPase, a critical regulator of transport directiona

18 us (EMCV) binds and inhibits the activity of Ran-GTPase, a key regulator of nucleocytoplasmic transpo

19 The Ran GTPase activating protein (RanGAP) is important to R

20 GTP.RBH complex stimulated GTP hydrolysis by Ran GTPase activating protein 1 both in vitro and in per

21 dissociation by RanBP1 and GTP hydrolysis by Ran GTPase activating protein 1.

22 The cytoplasmic Ran GTPase activating protein RanGAP is critical to esta

23 at resides on chromatin, and the cytoplasmic Ran GTPase activating protein RanGAP.

24 for distortion, encodes a truncated RanGAP (Ran GTPase activating protein), a key nuclear transport

25 r import were used together with cytoplasmic Ran GTPase-activating factors to demonstrate that import

26 DP, established by the spatial separation of Ran GTPase-activating protein (RanGAP) and the Ran guani

27 However, injection of Ran GTPase-activating protein (RanGAP) into RCC1-deplete

28 -purification strategy, we have identified a Ran GTPase-activating protein (RanGAP2) as an Rx-interac

29 (gsp1), and essential Ran regulatory factors Ran GTPase-activating protein (rna1), Ran guanine nucleo

30 , we show that reduction and inactivation of Ran GTPase-activating protein 1 (RanGAP1) commonly occur

31 Cdc25C (Chk1, Chk2, and H2AX), as well as on Ran GTPase-activating protein 1 conjugated to small ubiq

32 sentrin-2 could covalently modify RanGAP1, a Ran GTPase-activating protein critically involved in nuc

33 GDP enabled by the specific locations of the Ran GTPase-activating protein RanGAP and the nucleotide

34 sequestering of its accessory proteins, the Ran GTPase-activating protein RanGAP and the nucleotide

35 We have found that the mammalian Ran GTPase-activating protein RanGAP1 is highly concentr

36 Covalent modification of the Ran GTPase-activating protein RanGAP1 with the ubiquitin

37 s been characterized as a coactivator of the Ran GTPase-activating protein RanGAP1.

38 if at all, to a major SUMO-1 substrate, the Ran GTPase-activating protein RanGAP1.

39 is not stimulated to hydrolyze bound GTP by Ran GTPase-activating protein, RanGAP1.

40 n vitro, this interaction can accelerate the Ran GTPase-activating protein-mediated hydrolysis of GTP

41 ulator of the Ran GTP/GDP cycle is the 70-kD Ran-GTPase-activating protein RanGAP1.

42 not identical to Fug1/RanGAP1, the mammalian Ran-GTPase-activating protein.

43 plasm where it is disassembled by RanBP1 and Ran GTPase--activating protein.

44 1 as well as the L. pneumophila T4SS and the Ran GTPase activator LegG1 promote LCV-LD interactions.

45 This trafficking was dependent on the high Ran GTPase activity resulting from oncogenic transformat

46 ng nuclear localization signals requires the Ran GTPase and a complex of proteins assembled at the nu

47 the nuclear/cytoplasmic concentration of the Ran GTPase and inhibits the nuclear localization of Ubc9

48 ns, ultimately affecting the localization of Ran GTPase and subsequent cellular toxicity in C9orf72 i

49 ast in part, through reduced function of the Ran GTPase and SUMOylation pathways.

50 been defined by their ability to bind to the Ran GTPase and the presence of a common region of approx

51 Importin-11 interacts with the Ran GTPase, and constitutively shuttles between the nucl

52 ntrosome independent, operates downstream of Ran GTPase, and depends upon BRCA1/BARD1 E3 ubiquitin li

53 plore the relationship between progerin, the Ran GTPase, and oxidative stress.

54 Red/green opsin, Ran-GTPase, and the 19 S regulatory complex of the prote

55 uclear protein import pathway, including the Ran-GTPase, and the dimeric import receptor, importin-al

56 Whereas studies in human oocytes identified Ran GTPase as a crucial regulator of the MI spindle func

57 Our previous work identified the Ran GTPase as an essential component in this process.

58 Ribosome export is dependent on the Ran-GTPase as mutations in Ran or its regulators caused

59 Maintaining the Ran GTPase at a proper concentration in the nucleus is i

60 to the nucleus of 10-20% of the cytoplasmic Ran GTPase-binding protein (RanBP1) indicating that RanB

61 We identified a region in the human Ran GTPase-binding protein RanBP1 that shares similariti

62 shows that plants contain Rab, Rho, Arf, and Ran GTPases, but no Ras GTPases.

63 We posit that the control of Ran GTPase by Ranbp2 emerges as a novel therapeutic targ

64 the C9-isoforms with both Importin beta1 and Ran-GTPase, components of the nuclear pore complex.

65 The Ran GTPase controls multiple cellular processes includin

66 rt through the NPC can be uncoupled from the Ran GTPase cycle and can occur without GTP hydrolysis.

67 karyopherin-alpha, karyopherin-beta1 and the Ran GTPase cycle are required for INM targeting, undersc

68 we suggest that Yrb2p may play a role in the Ran GTPase cycle distinct from nuclear transport.

69 Here, we report the first evidence that the Ran GTPase cycle is required for nuclear pore complex (N

70 TPase Ran, and it has been proposed that the Ran GTPase cycle mediates translocation.

71 otein-1 (RanBP1), a known coregulator of the Ran GTPase cycle.

72 import is dependent on the integrity of the Ran GTPase cycle.

73 control of the Ras-related nuclear protein (Ran) GTPase cycle depends on the regulated activity of r

74 ty is dependent on Crm1, the RanGAP1 NES and Ran GTPase cycling.

75 The Ran GTPase drives nucleocytoplasmic transport, stabilize

76 Overexpression of Ran or RanGEF (Ran GTPase exchange factor) in the male germline fully s

77 Ran GTPase has been shown to be involved in host innate

78 al. (2014) describe how microtubules and the RAN GTPase/importin-beta system collaborate to control t

79 letion of which mislocalizes RanGAP1 and the Ran GTPase in cells.

80 s been identified as an important target for Ran GTPase in spindle formation in fission yeast.

81 L segment that makes subsequent contact with Ran GTPase in the nucleus, and Ran can displace 2A from

82 ttles between the cytoplasm and nucleus in a Ran GTPase-independent manner.

83 We also found that the Ran GTPase is not required for GR export.

84 The Ran GTPase is required for nuclear assembly, nuclear tra

85 Ran GTPase is required for nucleocytoplasmic transport o

86 n guanine-nucleotide exchange factor for the Ran GTPase, is an approximately 45-kD nuclear protein th

87 ease-associated Nup alterations, deficits in Ran GTPase localization, defects in TDP-43-associated mR

88 In a proteomics screen, we identified RAN GTPase, MST1 and 2 kinases, and alpha- and gamma-tub

89 d microtubule formation system that uses the Ran-GTPase nuclear transport machinery, but no targets o

90 Similarly, the Ran GTPase pathway is also involved in the nuclear trans

91 Analysis of the Ran-GTPase pathway in Xenopus extracts allows the examin

92 The Ran GTPase plays a central role in nucleocytoplasmic tra

93 The Ran GTPase plays a critical role in this process, becaus

94 Ran GTPase plays essential roles in multiple cellular pr

95 ith an expression vector for OPN to identify RAN GTPase (RAN) as the most overexpressed gene, in addi

96 ween docking and translocation mediated by a Ran GTPase-Ran binding protein complex.

97 se (DDR) and the cell cycle depends on their Ran GTPase-regulated nuclear-cytoplasmic transport (NCT)

98 nbp2(-/-) share proteostatic deregulation of Ran GTPase, serotransferrin, and gamma-tubulin and suppr

99 uclear pore complex and interaction with the Ran-GTPase support also its role in nucleocytoplasmic tr

100 ific changes in the nuclear pore complex and Ran GTPase system in lower eukaryotes.

101 lation of RanBP3, an accessory factor in the Ran GTPase system.

102 in order to unravel the complexities of the Ran GTPase system.

103 ic compartmentalization of components of the Ran GTPase system.

104 protein and RNA in eukaryotes depends on the Ran-GTPase system to regulate cargo-receptor interaction

105 rm1, a nuclear export receptor that binds to Ran GTPase, thereby inducing nuclear localization of NF-

106 s that interact with the GTP-charged form of Ran GTPase through a conserved Ran-binding domain (RBD).

107 se, Nek6, and also binds specifically to the Ran GTPase through both its catalytic and its RCC1-like

108 oplasmic trafficking, a process regulated by Ran GTPase through its nucleotide cycle.

109 , we show that importin beta cooperates with Ran GTPase to promote ubiquitination and proteasomal deg

110 Ran GTPase uses cellular energy in the direct form of GT

111 e mechanisms of Ran function, mutants of the Ran GTPase were characterized, several of which are capa

112 The recently solved structures of the Ran GTPase with a Ran-binding domain and with karyopheri

113 We illustrate this here for Ran GTPases, within which two highly conserved histidine