ライフサイエンスコーパス: hnRNP-H

1 hnRNP H and F are alternative splicing factors for numer

2 hnRNP H does not appear to mediate splicing control or s

3 hnRNP H family proteins bind to the enhancer as well; th

4 hnRNP H is required for interaction of U1 snRNP with the

5 nce was also specifically bound by hnRNP A1, hnRNP H, ASF/SF2 and SRp40, but not by 9G8.

6 to this element were identified as hnRNP A1, hnRNP H, hnRNP F, and SF2/ASF by site-specific cross-lin

7 Antibodies against hnRNP H immunoprecipitated cross-linked p55 and induced

8 that the sequence GGGA is recognized by all hnRNP H family proteins.

9 ds only hnRNP H/H' to a binding site for all hnRNP H family members.

10 expression level, suggesting that Chtop and hnRNP H regulate intron 2 retention of Chtop mRNA antago

11 g of each factor demonstrated that SRSF1 and hnRNP H antagonistically modulate splicing by binding ex

12 nt on the antagonistic activities of 9G8 and hnRNPs H and F.

13 s from in vitro splicing reactions with anti-hnRNP H antibody indicated that hnRNP H remains bound to

14 sis of purified p58 protein identified it as hnRNP H.

15 ction and identified by mass spectrometry as hnRNP H.

16 The c-src DCS has been shown to assemble hnRNP H, not hnRNP F, from HeLa cell extracts, and we sh

17 physical and functional interactions between hnRNP H, CUG-BP1 and MBNL1 dictate IR splicing in normal

18 el G-rich elements tested were found to bind hnRNP H/H' protein and the processing of selected signal

19 Sequences capable of binding hnRNP H protein with varying affinities may play a role

20 RNA interference was used to knock down both hnRNP H and hnRNP F.

21 endent suppressor complex consisting of both hnRNP H and CUG-BP1, which is required to maximally inhi

22 n that affects the spatial location of bound hnRNP H with respect to the exon 6D splicing determinant

23 otifs, some resembling known motifs bound by hnRNPs H and A1.

24 tracts revealed large assemblages containing hnRNP H, H', and F but deficient in CstF-64 in memory B-

25 polyadenylation, since viral RNAs containing hnRNP H-specific mutations were spliced and polyadenylat

26 n normal myoblasts, overexpression of either hnRNP H or CUG-BP1 results in the formation of an RNA-de

27 These results establish hnRNP H and hnRNP F as being repressors of exon inclusio

28 C repeat RNA in vitro is the splicing factor hnRNP H, and that this interaction is linked to G-Q form

29 e previously identified an auxiliary factor, hnRNP H/H', which stimulates 3'-end processing through a

30 nce that interacts with the splicing factors hnRNP H and SC35.

31 protein mutation suggests the potential for hnRNP H to antagonize polyadenylation.

32 Much less is known, however, about how hnRNP H and hnRNP F silence exons.

33 However, hnRNP H binding to the SRE acts as an enhancer of exon 6

34 mutant DMPK-derived RNA and have identified hnRNP H as an abundant candidate.

35 In this study, we identify hnRNP H and hnRNP F proteins as being novel silencers of

36 deling ribonucleoprotein complexes including hnRNP H, H2, H3, F, A2/B1, K, L, DDX5, DDX17, and DHX9.

37 dampen the inhibitory activity of increased hnRNP H levels on IR splicing in normal myoblasts.

38 elevated in DM1 myoblasts and that increased hnRNP H levels in normal myoblasts results in the inhibi

39 ns, which correlates with elevated insoluble hnRNP H/G-Q aggregates.

40 eptide sequencing reveal that this factor is hnRNP H, a member of the heterogeneous nuclear ribonucle

41 rate dysregulated splicing of multiple known hnRNP H-target transcripts in C9 patient brains, which c

42 taining this sequence to a substrate lacking hnRNP H binding activity is sufficient to promote bindin

43 ric complex containing the proteins hnRNP M, hnRNP H, hnRNP C, Matrin3, NF110/NFAR-2, NF45, and DDX5,

44 However, the ability of hnRNP H mutations to suppress the read-through caused by

45 Binding of hnRNP H correlates with the ESS activity.

46 The specific binding of hnRNP H requires not only a CUG repeat expansion but als

47 onjunction with si-RNA mediated depletion of hnRNP H contributes to partial rescue of the IR splicing

48 e splicing reactions or partial depletion of hnRNP H from nuclear extract activates exon 7 splicing i

49 The identification of hnRNP H as a factor capable of binding and possibly modu

50 Partial immunodepletion of hnRNP H from the nuclear extract partially inactivated t

51 Immunoprecipitation of hnRNP H cross-linked to the N1 enhancer RNA, as well as

52 The involvement of hnRNP H in the activity of an ESS may represent a protot

53 blasts demonstrates that increased levels of hnRNP H, H2, H3, F, and DDX5 independently dysregulate s

54 s of the enhancer complex in the presence of hnRNP H-specific antibodies, confirmed that hnRNP H is a

55 emingly contrasting functional properties of hnRNP H appear to be caused by a change in the RNA secon

56 that may also explain the dual properties of hnRNP H in splicing regulation.

57 The possible roles of hnRNP H in NRS function are discussed.

58 icate C9 expansion-mediated sequestration of hnRNP H as a significant contributor to neurodegeneratio

59 Suppression of hnRNP H expression by RNAi rescued nuclear retention of

60 Furthermore, expression of hnRNPs H, F, 2H9, A1, and A2 and SR proteins SF2 and SRp

61 g virus, we altered the expression levels of hnRNPs H, F, 2H9, GRSF1, A1, A2, and A3 and SR proteins

62 Overexpression of hnRNPs H and F blocked 9G8-mediated splicing both in viv

63 of the DCS from a substrate that binds only hnRNP H/H' to a binding site for all hnRNP H family memb

64 y heterogeneous nuclear ribonuclear protein (hnRNP)H/F.

65 a splicing-suppressing RNA-binding protein, hnRNP H.

66 enhances the binding of two other proteins, hnRNP H and KSRP, to the DCS RNA.

67 RS binds serine/arginine-rich (SR) proteins, hnRNP H and the U1/U11 snRNPs, and appears to inhibit sp

68 n of antibodies that specifically recognizes hnRNP H to the splicing reactions or partial depletion o

69 n be restored by the addition of recombinant hnRNP H, indicating that hnRNP H is an important factor

70 reversed by addition of purified recombinant hnRNP H.

71 lity shift assays indicated that recombinant hnRNP H specifically interacts with the p55 binding site

72 steady-state levels of the splice regulator, hnRNP H, are elevated in DM1 myoblasts and that increase

73 Heterogeneous nuclear ribonucleoprotein (hnRNP) H and F are members of a closely related subfamil

74 ich heterogeneous nuclear ribonucleoprotein (hnRNP) H and F regulate proteolipid protein (PLP)/DM20 a

75 the heterogeneous nuclear ribonucleoprotein (hnRNP) H protein family to determine their RNA binding s

76 the heterogeneous nuclear ribonucleoprotein (hnRNP) H protein family, H, H', F, and 2H9, are involved

77 Heterogeneous nuclear ribonucleoprotein (hnRNP) H, polypyrimidine tract binding protein (PTB), an

78 he heterogeneous nuclear ribonucleoproteins (hnRNPs) H and F bind to and compete for the same element

79 nylation signals identified potential G-rich hnRNP H/H' binding sites at similar downstream locations

80 the context of the wild-type viral sequence, hnRNP H acts as a repressor of exon 6D inclusion indepen

81 hnRNP H-specific antibodies, confirmed that hnRNP H is a protein component of the splicing enhancer

82 s with the p55 binding site, confirming that hnRNP H is p55.

83 ly, in vitro binding assays demonstrate that hnRNP H can interact with the related protein hnRNP F, s

84 onstitution assays we have demonstrated that hnRNP H/H' can stimulate processing of two additional mo

85 These results indicate that hnRNP H participates in exclusion of exon 7 in nonmuscle

86 ns with anti-hnRNP H antibody indicated that hnRNP H remains bound to the src pre-mRNA after the asse

87 tion of recombinant hnRNP H, indicating that hnRNP H is an important factor for N1 splicing.

88 In addition, we show that hnRNP H accelerates intron 2 splicing of Chtop mRNA in a

89 We show that hnRNP H and hnRNP F proteins are present in a complex wi

90 depletion-- reconstitution studies show that hnRNP H is essential for enhancer activity.

91 Finally, we show that hnRNP H/F are transcription-dependent shuttling proteins

92 from the HIV-1 tat gene and have shown that hnRNP H family members are required for efficient splici

93 Collectively, the results suggest that hnRNP H and F are GYR domain-dependent shuttling protein

94 Our data indicate that hnRNPs H, H', F, 2H9, and GRSF-1 bind the consensus moti

95 the related protein hnRNP F, suggesting that hnRNPs H and F may exist as a heterodimer in a single en

96 The hnRNP H protein family members activated splicing of the

97 ith RNA-seq revealed that exons carrying the hnRNP H-binding GGGGG motif are predisposed to be skippe

98 to the point mutation region may convert the hnRNP H-U1 snRNP complex into a splicing enhancer.

99 ee RNA-binding motifs and is a member of the hnRNP H family of RNA-binding proteins.

100 (GST) pulldown assays demonstrated that the hnRNP H NLS interacts with the import receptor transport

101 ermined to be a common property of all three hnRNP H/H' binding sites.

102 bind to degenerative binding motifs, whereas hnRNP H strictly requires an uninterrupted stretch of po

103 NRS did not affect polyadenylation, whereas hnRNP H strongly inhibited polyadenylation.

104 We propose a model in which hnRNP H and SR proteins compete for binding to the NRS.

105 pansion, and more frequently colocalize with hnRNP H.

106 By selectively coordinating with hnRNP H/F and U proteins, AKAP95 appears to mainly promo

107 tissue-specific splicing by interacting with hnRNP H protein subfamily.

108 MBNL1 show RNA-independent interaction with hnRNP H and dampen the inhibitory activity of increased