ライフサイエンスコーパス: SCF complex

1 e F-box protein may regulate activity of the SCF complex.

2 odes CULLIN1, an invariable component of the SCF complex.

3 iting binding between beta-TrCP and the core SCF complex.

4 is indirect via binding to Skp1 in the host SCF complex.

5 FBXW7 and disables its recruitment into the SCF complex.

6 tain optimal composition and function of the SCF complex.

7 n of Grr1 that should not associate with the SCF complex.

8 WD-1, the substrate-recruiting subunit of an SCF complex.

9 uclear localization and assimilation into an SCF complex.

10 sm may involve regulation of assembly of the SCF complex.

11 conjugating enzyme of the Skp1/cullin/F-box (SCF) complex.

12 by the Cdc4 E3 ligase of the Skp1/Cul1/Rbx1 (SCF) complex.

13 e best-characterized families of E3s are the SCF complexes.

14 to-ubiquitination in the context of Cdc53 or SCF complexes.

15 ) appeared to be internalized along with Kit-SCF complexes.

16 3 ligase activity, but not activity of other SCF complexes.

17 profoundly alters the cellular landscape of SCF complexes.

18 orate to regulate the cellular repertoire of SCF complexes.

19 al evidence showing the polymorphic roles of SCF complexes.

20 nhibitors to modulate function of individual SCF complexes.

21 controlling the localization of the cognate SCF complexes.

22 e aspects of flower development as a part of SCF complexes.

23 e to the selection of substrates by metazoan SCF complexes.

24 s suggests an extensive set of combinatorial SCF complexes.

25 iquitin ligases, Skp1/Cullin1/F-box protein (SCF) complexes.

26 An activated SCF complex, a heterotetramer (Skp1, Cul-1, beta-TrCP [F

27 vity or its capacity to interact with the E3-SCF complex abrogate its abd1 suppressor function.

28 e substrate specificity to Skp Cullin F box (SCF) complexes, acting as E3 ligases that target phospho

29 r TRIM9-mediated regulation of the beta-TrCP SCF complex activity but also identifies TRIM9 as a brai

30 This SCF complex also recognizes a conserved destruction moti

31 ain ubiquitin protein ligases, including the SCF complex and APC, have been suggested to govern termi

32 ts interaction with active components of the SCF complex and that HOS stability is regulated by a bou

33 ata shows that Arabidopsis has exploited the SCF complex and the ubiquitin/26S proteasome pathway as

34 ods that preserve the in vivo assemblages of SCF complexes and apply quantitative mass spectrometry t

35 e subunits and substrates of CUL1-associated SCF complexes and CUL2 ubiquitin ligases are well establ

36 Hrt1 assembles into recombinant SCF complexes and individually binds Cdc4, Cdc53 and Cdc

37 CULLIN1 (CUL1) is a core component of SCF complexes and is involved in multiple signaling path

38 ition of p18-Cyclin E by the Skp1-Cul1-Fbw7 (SCF) complex and its interaction with the Fbw7 protein i

39 box protein PhMAX2A of the Skp-Cullin-F-box (SCF) complex and/or a repressor of SL signaling, PhD53A.

40 st that CAND1 regulates the formation of the SCF complex, and its dissociation from CUL1 is coupled w

41 E interacted with the CULLIN1 subunit of the SCF complex, and this interaction required the F-box dom

42 e that the cellular responses mediated by an SCF complex are directly regulated by environmental cond

43 Because the constituents of the SCF complex are members of protein families, SCFCdc4 is

44 SCF complexes are a conserved family of ubiquitin ligase

45 To illuminate how SCF complexes are regulated, we sought proteins that int

46 SCF complexes are the largest and best studied family of

47 SCF complexes are the largest family of E3 ubiquitin-pro

48 Skp1, Cullin, F-box (SCF) complexes are one influential E3 class that use F-b

49 ral intermediates, including a ternary CAND1-SCF complex, as well as conformational and compositional

50 y and a component of the Skp1.Cullin1.F-box (SCF) complex, as a new p53-interacting protein.

51 ZTL with the three known core components of SCF complexes (ASK1, AtCUL1 and AtRBX1) demonstrates tha

52 nterferes with Skp1 binding, thus preventing SCF complex assembly.

53 anism for maintaining activities of specific SCF complexes based on availability of a particular subs

54 umor suppressor and Skp1-Cul1-F-box protein (SCF) complexes belong to families of structurally relate

55 the incorporation of F box proteins into the SCF complex, causing their destabilization.

56 lants, the multi-subunit Skp1-Cullin1-F-box (SCF) complexes compose the largest group of E3 ligases w

57 an E3 ubiquitin ligase, a Skp1-cullin-F-box (SCF) complex composed of SKR-1 and the F-box protein SEL

58 SCF complexes consist of three invariable components, Sk

59 Ectopic expression of SCF complex containing beta-TrCP1 is sufficient to induc

60 In Saccharomyces cerevisiae, an SCF complex contains a common set of components, namely,

61 SCF complexes couple protein kinase signaling pathways t

62 th these results, cells that overexpress the SCF complex display an inhibited TGF-beta-dependent tran

63 ggesting that a hierarchical organization of SCF complexes exists defined by distinct Skp/F-box prote

64 mal degradation by FBXL20 and the associated SCF complex expression provides a novel checkpoint for p

65 ught to artificially target a protein to the SCF complex for ubiquitination and degradation.

66 recognition component of SKP1/Cullin/F-box (SCF) complexes for targeted protein polyubiquitination.

67 These differences in substrate recognition, SCF complex formation, and tissue distribution suggest t

68 ved in cul1-6 plants are caused by defective SCF complex formation.

69 family of ubiquitin ligase complexes, called SCF complexes, found throughout eukaryotes, is involved

70 SCF complexes have a variable F-box protein subunit that

71 In yeasts, three SCF complexes have been demonstrated to associate with t

72 In plants, SCF complexes have been found to regulate auxin response

73 ) demonstrates that ZTL can assemble into an SCF complex in vivo.

74 The RBX1 protein is a component of SCF complexes in Arabidopsis.

75 RING-H2 finger protein RBX1 is a subunit of SCF complexes in fungi and animals.

76 e obtained cryo-EM structures of CAND1-bound SCF complexes in multiple states and correlated mutation

77 SN inhibits the ubiquitin ligase activity of SCF complexes in vitro.

78 results, also provide evidence for distinct SCF complexes in vivo and support the idea that their F-

79 CSN plays a central role in the assembly of SCF complexes in vivo, regulation of Jab1/CSN5 by MIF is

80 st to substrates of the SKP1-Cullin 1-F box (SCF) complexes, in vitro ubiquitination of E2F1 by CUL1-

81 ), an accessory protein that associates with SCF-complex, in plant transformation.

82 rf)-p53 response is impaired, whereas a Skp2-SCF complex inhibitor can trigger cellular senescence in

83 apable of binding Skp1p and entering into an SCF complex interfered with proteolysis of SCF targets a

84 nents Skp1, Cul1, and Rbx1 serve in multiple SCF complexes involving different substrate-specific F-b

85 Another component of SCF complexes is provided by members of the Roc1/Rbx1/Hr

86 However, how the repertoire of SCF complexes is sustained remains unclear.

87 , we show that Skp2, a component of the Skp2 SCF complex, is an important regulator for HSC quiescenc

88 Only in fully assembled SCF complexes, it is believed, can substrates bound to F

89 s suggest that the cullin specificity of the SCF complex may reflect its ability to associate with Rb

90 mal F-box proteins, suggesting that distinct SCF complexes may direct proteolysis of factors mediatin

91 h Skp1, Cullin-1, and Rbx1, could compose an SCF complex mediating the degradation of nonself S-RNase

92 ntrast to IGF-1 induced activation, the Skp2 SCF complex, not TRAF6, is a critical E3 ligase for ErbB

93 ), the substrate recognition component of an SCF (complex of SKP1, CUL1 and F-box protein)-type E3 ub

94 rticular, SKP1, cullin/CDC53, F-box protein (SCF) complexes play important roles in selecting substra

95 Each SCF complex recognizes different substrates according to

96 In contrast, the SCF complex recruits substrates through a substrate adap

97 These results suggest that SCF complexes regulate several aspects of floral develop

98 s but ATR, in coordination with the cyclin F-SCF complex, represses premature stem cell quiescence ex

99 These findings define a new SCF complex required for caspase activation during sperm

100 eractor F-box (PHIF1) as constituents of the SCF complex responsible for PHR1 degradation.We found th

101 egradation of some host factors by using the SCF complex resulting in the enrichment of c-Jun.

102 ility of mutant CUL1 to assemble into stable SCF complexes resulting in reduced degradation of the SC

103 Knocking down cyclin F or inhibiting the SCF complex results in E2F1 accumulation and in MuSCs ex

104 -TrCP-containing Skp-Cullin 1-F-box protein (SCF) complex (SCF(beta-TrCP)) E3 ubiquitin ligase in a p

105 biochemical dissection of a novel mammalian SCF complex, SCFbeta-TRCP, that specifically recognizes

106 co-precipitated components of the canonical SCF complex (Skp1, Cullin1, and Rbx1), yet FBXO2 bound v

107 Both SCF complexes targeted the cyclin-dependent kinase inhib

108 Polyubiquitination of proteins by Cdc34/SCF complexes targets them for degradation by the 26S pr

109 of Skp2, the rate-limiting component of the SCF complex that degrades p27(kip1), was reduced.

110 Both are components of the SCF complex that ubiquitinates proteins during the G1-S

111 teract with SKP1 and cullin proteins to form SCF complexes that selectively recruit regulatory protei

112 sually forms part of an Skp1, cullin, F-box (SCF) complex that targets specific protein substrates fo

113 integrated into functional Skp-Cullin-F-box (SCF) complexes that confer E3 ubiquitin ligase activity.

114 kp1 and Cul1 are invariant components of all SCF complexes, the 69 different human F-box proteins are

115 ligases is defined by the recently described SCF complexes, the archetype of which was first describe

116 bound to SKR-1 and inhibited assembly of the SCF complex, thereby protecting nearby synapses.

117 In the SCF complex, this module is composed of Skp1, which bind

118 n the substrate in an optimal way within the SCF complex to enable efficient ubiquitin transfer.

119 ts that Slimb and Roc1a function in the same SCF complex to target Ci but that a different RING-H2 pr

120 er, these factors enable rapid remodeling of SCF complexes to promote biased assembly of SR modules b

121 eins, EBF1 and -2, that work coordinately in SCF complexes to repress ethylene action.

122 o assess the contribution of CUL1-containing SCF complexes to signaling within the plant oscillator,

123 he ability of the Skp1-Cullin-F-box protein (SCF) complex to ubiquitylate p27, such a mutation has no

124 dentify regulators/components of hCUL1-based SCF complexes, to determine whether the hCUL2-hCUL5 prot

125 LRC5 N-terminus while its F-box directs host SCF complex ubiquitination of NLRC5 in the leucine-rich

126 C/C with another multiprotein E3 ligase, the SCF complex, uncovers remarkable structural similarities

127 o report that M-T5 can bind Akt and the host SCF complex (via Skp1) simultaneously in MYXV-infected c

128 Grr1p, another F box component of SCF complexes, was also ubiquitinated.

129 determine whether COI1 also functions in an SCF complex, we have characterized Arabidopsis proteins

130 omponents and substrates of a putative human SCF complex, we isolated hSKP1 in a two-hybrid screen wi

131 uring G(2) and M phase is dependent upon the SCF complex, whereas the APC/C is responsible for Cig2 d

132 -beta negatively regulates components of the SCF complex, which degrades the p27Kip1 during the G1 to

133 he anaphase-promoting complex (APC/C) or the SCF complex, which mediate the major cell cycle regulate

134 al structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF complex, which shows that Cul1 is an elongated prote

135 ass of ubiquitin ligases (E3 enzymes) called SCF complexes, which regulate the abundance of proteins

136 showed that mH2A1 is a new substrate of Skp2 SCF complex whose degradation by Skp2 promotes CDK8 gene

137 F-box proteins also act in non-SCF complexes whose functions are not well understood.

138 quitin ligases is formed by the multisubunit SCF complex, whose core complex (Rbx1/Cul1-Cdc53/Skp1) b

139 Being a part of SCF complex with Skp1 and Cullin1, HOS specifically inte

140 BF1 or -2, suggesting that the corresponding SCF complexes work together in EIN3 breakdown.