ライフサイエンスコーパス: hnRNP

1 l splicing activators (SRSF) and repressors (HNRNP).

2 ed heterogeneous nuclear ribonucleoproteins (hnRNPs).

3 heterogeneous nuclear ribonuclear proteins (hnRNPs).

4 analysis identified the RNA binding protein, HNRNPD.

5 i-system congenital defects and are found in hnRNPs.

6 ary changes impact nearly all members of the hnRNP A and D families of RNA binding proteins.

7 ng, heterogeneous nuclear ribonucleoprotein (hnRNP) A/B proteins.

8 nc13 regulates gene expression by binding to hnRNPD, a member of a family of ubiquitously expressed h

9 A screen identified hnRNP A1 (A1) and RPS25 as IRES-binding trans-acting fac

10 We used RNA sequencing (RNA-seq) to confirm hnRNP A1 and A2/B1 motif-dependent roles genome-wide, pr

11 o 40) of p17 that is critical for binding to hnRNP A1 and for nucleocytoplasmic shuttling of p17.

12 voring recruitment of the splicing repressor hnRNP A1 and interfering with that of U2AF65 at the 3' s

13 This study provides novel insights into how hnRNP A1 and lamin A/C modulate nucleocytoplasmic shuttl

14 Here we report that hnRNP A1 and lamin A/C serve as carrier and mediator pro

15 this study provide mechanistic insights into hnRNP A1 and lamin A/C-modulated nucleocytoplasmic shutt

16 sults reveal general rules of specificity of hnRNP A1 and provide a quantitative framework for unders

17 al gray matter of the spinal cord where anti-hnRNP A1 antibodies localized.

18 Anti-hnRNP A1 antibodies were found to surround neuronal cell

19 Additionally, anti-hnRNP A1 antibodies were found within neuronal cell bodi

20 s (EAE), we show here that injection of anti-hnRNP A1 antibodies, in contrast to control antibodies,

21 y shown to undergo neurodegeneration in anti-hnRNP A1 antibody injected EAE mice.

22 neous nuclear ribonucleoprotein (hnRNP) L or hnRNP A1 are Akt substrates during Treg induction and ha

23 ng and in vitro evolution identify consensus hnRNP A1 binding motifs; however, such data do not revea

24 n addition, we show by NMR that both RRMs of hnRNP A1 can bind simultaneously to a single bipartite m

25 to the hnRNP A1-binding site or knockdown of hnRNP A1 expression promoted 233^416 splicing and reduce

26 We determined the affinity of hnRNP A1 for all possible sequence variants (n = 16,384)

27 organization of the two RRMs is essential to hnRNP A1 function.

28 t comprise the NES can modulate both p17 and hnRNP A1 interaction and nucleocytoplasmic shuttling of

29 y attenuates viral replication by abrogating hnRNP A1 interactions.

30 We showed that hnRNP A1 is methylated by PRMT5 on two residues, R218 an

31 ndicated that direct interaction of p17 with hnRNP A1 maps within the amino terminus (amino acids [aa

32 Neurons displayed increased levels of hnRNP A1 nucleocytoplasmic mislocalization and stress gr

33 Knockdown of hnRNP A1 or lamin A/C led to inhibition of nucleocytopla

34 HnRNP A1 regulates many alternative splicing events by t

35 differentiation, and knockdown of hnRNP L or hnRNP A1 results in the lower induction of Treg cells.

36 rentially spliced gene isoforms in LIN28 and hnRNP A1 small interfering RNA (siRNA)-treated cells.

37 loops represent an important class of known hnRNP A1 targets, yet little is known about the structur

38 s methylation facilitates the interaction of hnRNP A1 with IRES RNA to promote IRES-dependent transla

39 This interaction of hnRNP A1 with LANA mRNA could be exploited for controlli

40 dentified heterogenous ribonucleoprotein A1 (hnRNP A1) as a G-quadruplex-unwinding helicase, which un

41 heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) as a possible mechanism of neurodegeneration i

42 Heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) is a multipurpose RNA-binding protein (RBP) in

43 heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1), a protein with multiple roles in mRNA metabol

44 icing of HPV18 E6E7 pre-mRNAs via binding to hnRNP A1, a well-characterized, abundantly and ubiquitou

45 ugh interaction with a host splicing factor, hnRNP A1, and regulates E6 and E7 expression of the earl

46 Notably, hnRNP A1, hnRNP A2, and hnRNP B1 bound to many dispersed

47 Drosophila hnRNP A1, Hrp38, is required for germ line stem cell mai

48 The heterogeneous nuclear ribonucleoprotein, hnRNP A1, is an IRES transacting factor (ITAF) that regu

49 s suggest that autoimmunity to RBPs, such as hnRNP A1, play a role in neurodegeneration in EAE with i

50 LANA and identified a cellular RNA helicase, hnRNP A1, regulating the translation of LANA mRNA.

51 MS patients make antibodies to hnRNP A1, which have been shown to lead to neuronal dysf

52 Introduction of point mutations into the hnRNP A1-binding site or knockdown of hnRNP A1 expressio

53 nformational change to assemble a functional hnRNP A1-RNA complex.

54 Mechanisms and putative hnRNP A1-RNA interactions have been inferred primarily f

55 esented here provide the first insights into hnRNP A1-RNA interactions.

56 ittle is known about the structural basis of hnRNP A1-RNA recognition.

57 esembles sequence elements of several native hnRNP A1-RNA stem loop targets.

58 The formation of p17-hnRNP A1-transportin 1 carrier-cargo complex is required

59 our results reveal that the formation of p17-hnRNP A1-transportin 1 carrier-cargo complex is required

60 of either RRM impairs splicing repression by hnRNP A1.

61 ing site for the pre-mRNA processing protein hnRNP A1.

62 and the Gly-rich region of the C terminus of hnRNP A1.

63 Most importantly, the expression of hnRNP A1/A2 and PTB/nPTB is significantly altered in pat

64 ding proteins, such as hnRNP L, PTB/nPTB and hnRNP A1/A2.

65 The heterogeneous nuclear ribonucleoprotein (hnRNP) A1 protein is a multifunctional RNA binding prote

66 hat heterogeneous nuclear ribonucleoprotein (hnRNP) A1 serves as a carrier protein to modulate nucleo

67 ed heterogeneous nuclear ribonucleoproteins (hnRNPs) A1 and A2/B1, which are required for transcript

68 The role of hnRNP-A1 in telomere protection also involves DNA-depend

69 Here we report that hnRNP-A1 is phosphorylated by DNA-PKcs during the G2 and

70 Consequently, in cells lacking hnRNP-A1 or DNA-PKcs-dependent hnRNP-A1 phosphorylation,

71 our results indicate that DNA-PKcs-dependent hnRNP-A1 phosphorylation is critical for capping of the

72 he G2 and M phases and that DNA-PK-dependent hnRNP-A1 phosphorylation promotes the RPA-to-POT1 switch

73 cells lacking hnRNP-A1 or DNA-PKcs-dependent hnRNP-A1 phosphorylation, impairment of the RPA-to-POT1

74 ecent evidence has further demonstrated that hnRNP-A1 plays a crucial role in maintaining newly repli

75 d heterogenous nuclear ribonucleoprotein A1 (hnRNP-A1) as a pharmacodynamic biomarker of type I PRMT

76 heterogeneous nuclear ribonucleoprotein A1 (hnRNP-A1) has been implicated in telomere protection and

77 methylation of specific arginine residues on hnRNP-A1.

78 cold inducible RNA-binding protein (CIRP or hnRNP A18) as a telomerase-interacting factor.

79 As a result, hnRNP A2 is displaced, and BC RNAs are impaired in their

80 native name for TOG protein) that binds both hnRNP A2 molecules and RNA.

81 uence called the A2 response element (A2RE), hnRNP A2 proteins that bind specifically (with high affi

82 heterogeneous nuclear ribonucleoprotein A2 (hnRNP A2) for access to BC RNAs.

83 heterogeneous nuclear ribonucleoprotein A2 (hnRNP A2) for DTE access and significantly diminish BC R

84 re modulated by a bivalent adaptor molecule (hnRNP A2).

85 Notably, hnRNP A1, hnRNP A2, and hnRNP B1 bound to many dispersed sites acr

86 G motifs enriched within approximately 2,500 hnRNP A2/B1 binding sites and an unexpected role for hnR

87 ALS-associated hnRNP A2/B1 D290V mutant patient fibroblasts and motor n

88 -dependent rescue does, however, require fly hnRNP A2/B1 homologues Hrb87F and Hrb98DE.

89 /B1 binding sites and an unexpected role for hnRNP A2/B1 in alternative polyadenylation.

90 ed survival in long-term culture and exhibit hnRNP A2/B1 localization to cytoplasmic granules as well

91 HnRNP A2/B1 loss results in alternative splicing (AS), i

92 s, likely due to increased nuclear-insoluble hnRNP A2/B1.

93 degeneration, regulated by normal and mutant hnRNP A2/B1.

94 tor heterogeneous nuclear ribonucleoprotein (hnRNP) A2 form the basis for activity-dependent dendriti

95 Heterogeneous nuclear ribonucleoprotein (hnRNP) A2/B1 binds this element and promotes readthrough

96 ied heterogeneous nuclear ribonucleoprotein (hnRNP)-A2/B1 and hnRNP-R as interactors binding directly

97 We conclude that hnRNP and NF90 are important host factors for HCV replic

98 hnRNP and SR proteins also regulate the expression of ot

99 ripts than previously appreciated, including HNRNPD and HNRNPDL, which are involved in multivalent pr

100 n of the interplay between hnRNP K (or other hnRNPs) and Nrf2-mediated antioxidant signaling is warra

101 by heterogeneous nuclear ribonucleoproteins (hnRNPs) and their viral target sequences, which typicall

102 HNRNPs are a large group of ubiquitous proteins that ass

103 Heterogeneous nuclear ribonucleoproteins (hnRNPs) are a group of functionally versatile proteins t

104 nd heterogeneous nuclear ribonucleoproteins (hnRNPs) are families of sequence-specific, posttranscrip

105 formation of tyrosine-dependent multivalent hnRNP assemblies that, in turn, function to globally reg

106 Notably, hnRNP A1, hnRNP A2, and hnRNP B1 bound to many dispersed sites across viral mRNA

107 re, we determined the location and extent of hnRNP binding to HIV-1 mRNAs and their impact on splicin

108 in heterogeneous nuclear ribonucleoproteins (hnRNPs) binding to A3B.

109 We found that HNRNPD binds chromatin, although this binding occurred i

110 ogether, this work reveals new activities of hnRNP C and CELF2, provides insight into a previously un

111 We analyze RNA-Seq data to show that hnRNP C is a potential regulator of SMN6B expression and

112 Specifically, we show that loss of hnRNP C reduces the transcription of CELF2 mRNA, while l

113 Here we demonstrate that the RBPs CELF2 and hnRNP C regulate the expression of each other, such that

114 of CELF2 results in decreased efficiency of hnRNP C translation.

115 e heterogeneous nuclear ribonucleoprotein C (hnRNP C) family.

116 ex containing the proteins hnRNP M, hnRNP H, hnRNP C, Matrin3, NF110/NFAR-2, NF45, and DDX5, all appr

117 Knockdown of RALY and hnRNP-C increased levels of viral RNA splicing, protein

118 at viral-mediated ubiquitination of RALY and hnRNP-C relieves a restriction on viral RNA processing a

119 irus resulted in an increased interaction of hnRNP-C with viral RNA and attenuation of viral RNA proc

120 ocused on two RNA-binding proteins, RALY and hnRNP-C, which we confirm are ubiquitinated without degr

121 Our results suggested that hnRNP C1 controls HPV16 late gene expression.

122 Overexpression of RALYL or hnRNP C1 induced HPV16 late gene expression from HPV16 s

123 Binding of hnRNP C1 to the HPV16 early, untranslated region activat

124 on in metabolic control and a model by which hnRNPs can impact health and disease states.

125 red to as polyC-binding proteins (PCBPs) and hnRNPEs) comprise a subset of KH-domain proteins with hi

126 rescues the defective DNA damage response of HNRNPD-depleted cells.

127 HNRNPD depletion resulted in an increased amount of RNA:

128 oly(C) binding proteins, PCBPs (alphaCPs and hnRNP E proteins), are encoded by a highly conserved and

129 Genes that are translationally silenced by hnRNP E1 and expressed by its dissociation are highly im

130 n cellular models by the high abundance of p-hnRNP E1 and low levels of hnRNP E1.

131 Levels of p-hnRNP E1 are highly upregulated in metastatic cancer cel

132 We have identified an hnRNP E1 consensus-binding motif and genomically resolve

133 lect transcripts via the RNA-binding protein hnRNP E1 during EMT.

134 ed to a significantly reduced level of total hnRNP E1 in metastatic cells.

135 TGFbeta stimulation or silencing of hnRNP E1 increases ILEI translation and induces an EMT p

136 ting cells and reduced metastasis within the hnRNP E1 knock-down cell populations in vivo.

137 Herein, we demonstrate that hnRNP E1 knockdown significantly shifts normal mammary e

138 his post-translational modification (PTM) of hnRNP E1 promotes its dissociation from a 3' untranslate

139 a signature high level of Akt2, p-Akt2 and p-hnRNP E1 protein expression, coupled to a significantly

140 TGFbeta treatment or knockdown of hnRNP E1 relieves silencing of the inhibin betaA transcr

141 e for inducing EMT by aberrant expression of hnRNP E1 silenced targets.

142 heterogeneous nuclear ribonucleoprotein E1 (hnRNP E1) at serine-43 (p-hnRNP E1).

143 onucleoprotein E1 (hnRNP E1) at serine-43 (p-hnRNP E1).

144 kinetics of the consensus-binding motif and hnRNP E1, its various K-homology (KH) domains and p-hnRN

145 is translationally regulated by TGFbeta via hnRNP E1.

146 1, its various K-homology (KH) domains and p-hnRNP E1.

147 gh abundance of p-hnRNP E1 and low levels of hnRNP E1.

148 translational silencing at the mRNA level by hnRNP E1.

149 sgenic (Tg) mice specifically overexpressing hnRNP F in their RPTCs.

150 HnRNP F inhibited Bmf transcription via hnRNP F-responsi

151 In vitro, hnRNP F overexpression stimulated Sirtuin-1 and Foxo3alp

152 Our results demonstrate that hnRNP F protects kidneys against oxidative stress and ne

153 Transfection of p44/42 MAPK or hnRNP F small interfering RNA (siRNA) prevented insulin

154 hnRNP F stimulated Sirtuin-1 transcription via hnRNP F-r

155 of Sirtuin-1 small interfering RNA prevented hnRNP F stimulation of Foxo3alpha and downregulation of

156 in Akita mice and Akita mice overexpressing hnRNP F suppressed Bmf expression and RPTC apoptosis.

157 Our results demonstrate that hnRNP F suppression of Bmf transcription is an important

158 g heterogeneous nuclear ribonucleoprotein F (hnRNP F) in their RPTCs and immortalized rat renal proxi

159 f heterogeneous nuclear ribonucleoprotein F (hnRNP F) renoprotective action in a type 2 diabetes (T2D

160 more RPTC apoptosis and lower expression of hnRNP F, SIRTUIN-1, and FOXO3alpha than nondiabetic kidn

161 HnRNP F inhibited Bmf transcription via hnRNP F-responsive element in the Bmf promoter.

162 RNP F stimulated Sirtuin-1 transcription via hnRNP F-responsive element in the Sirtuin-1 promoter.

163 ion was down-regulated with up-regulation of hnRNP F.

164 Interestingly, AS targets of the QKI-6-hnRNP F/H pathway in OLs are differentially affected in

165 RALY is a member of the hnRNP family that binds poly-U-rich elements within seve

166 RNPA1, hnRNPA3 and hnRNPU-all members of the hnRNP family.

167 he heterogeneous nuclear ribonucleoproteins (hnRNPs) family cause ALS.

168 he heterogeneous nuclear ribonucleoproteins (hnRNP) form a large family of RNA-binding proteins that

169 The heterogeneous nuclear ribonucleoprotein (HNRNP) genes code for a set of RNA-binding proteins that

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

171 rked increase in basal level of synaptosomal hnRNP H and mitochondrial proteins that decreased in res

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

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

174 Thus, we identified a potential role for hnRNP H in basal and dynamic mitochondrial function that

175 iscovered a role for the RNA binding protein hnRNP H in methamphetamine reward and reinforcement.

176 lysis identified a corresponding decrease in hnRNP H protein in 114 kb congenic mice.

177 urprisingly, there was a twofold increase in hnRNP H protein in the striatal synaptosome of H1(+/-) m

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

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

180 to the mechanisms linking increased synaptic hnRNP H with decreased methamphetamine-induced dopamine

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

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

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

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

185 pansion, and more frequently colocalize with hnRNP H.

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

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

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

189 letion and mutation of a prominent viral RNA hnRNP H1 binding site decreased the use of splice accept

190 Conversely, hnRNP H1 bound to a few discrete purine-rich sequences,

191 uences, a finding that was mirrored in vitro hnRNP H1 depletion and mutation of a prominent viral RNA

192 led an unexpected splicing enhancer role for hnRNP H1 through binding to its target element.IMPORTANC

193 the heterogeneous nuclear ribonucleoprotein hnRNP H2.

194 is heterogenous nuclear ribonuclear protein (hnRNP) has multiple functions in RNA processing includin

195 Laccase2 gene product but rather by multiple hnRNP (heterogeneous nuclear ribonucleoprotein) and SR (

196 Although hnRNP I and AUF1 can interact with many RNA species and

197 While Linc-RoR is required for hnRNP I to bind to c-Myc mRNA, interaction of Linc-RoR w

198 ith heterogeneous nuclear ribonucleoprotein (hnRNP) I and AU-rich element RNA-binding protein 1 (AUF1

199 Here, we outline a role for hnRNPs in gene regulatory circuits controlling sterol ho

200 of heterogeneous nuclear ribonucleoproteins (hnRNPs) in the control of alternative splicing at cis-ac

201 We found that HNRNPD interacts with the heterogeneous nuclear ribonucl

202 cerevisiae Likewise, recruitment of Npl3 (an hnRNP involved in mRNA export via formation of export-co

203 further exploration of the interplay between hnRNP K (or other hnRNPs) and Nrf2-mediated antioxidant

204 pment of hematological disorders and suggest hnRNP K acts as a tumor suppressor.

205 required for the cytoplasmic localization of hnRNP K and for its role in regulating the expression of

206 duced negative superhelicity, where relative hnRNP K and nucleolin expression shifts the equilibrium

207 o a thermodynamically stable complex between hnRNP K and the unfolded i-motif.

208 Reduced hnRNP K expression attenuated p21 activation, downregula

209 xpressing TDP-43Q331K mutation, we show that hnRNP K expression is impaired in urea soluble extracts

210 infection, which may alter accessibility of hnRNP K for host transcripts thereby leading to a progra

211 Finally, we find an increase in hnRNP K in nuclear speckles upon IAV infection, which ma

212 Together, these data implicate hnRNP K in the development of hematological disorders an

213 effects of mutant TDP-43-mediated changes to hnRNP K metabolism by RNA binding immunoprecipitation an

214 The K17-hnRNP K partnership is regulated by the ser/thr kinase R

215 We provide evidence that morphine increases hnRNP K protein expression via MOR activation in rat pri

216 hnRNP K protein was bound to antioxidant NFE2L2 transcri

217 hnRNP K regulates cellular programs, and changes in its

218 We demonstrated that hnRNP K regulates dendritic spine density and long-term

219 For maximal hnRNP K transcription activation, two additional cytosin

220 species and destabilizes the interaction of hnRNP K with the Mid-region i-motif.

221 h heterogeneous nuclear ribonucleoprotein K (hnRNP K) in the nucleus and acts as a transcription fact

222 r heterogeneous nuclear ribonucleoprotein K (hnRNP K) was found to bind selectively to the i-motif sp

223 d heterogeneous nuclear ribonucleoprotein K (hnRNP K).

224 IAV-induced splicing events are regulated by hnRNP K, a host protein required for efficient splicing

225 These findings functionally integrate K17, hnRNP K, and gene expression along with RSK and CXCR3 si

226 ng to known splicing factors including DDX5, hnRNP K, and PRPF6.

227 t K17 interacts with the RNA-binding protein hnRNP K, which has also been implicated in cancer.

228 within the 4CT element and is recognized by hnRNP K, which leads to a low level of transcription act

229 the heterogeneous nuclear ribonucleoprotein hnRNP K.

230 transcription-repressive complex containing hnRNP-K/L proteins and show that knockdown of these fact

231 d the ability to phosphorylate RPA32 S4/8 in HNRNPD knockout cells upon DNA damage, suggesting that R

232 CRISPR/Cas9-mediated HNRNPD knockout impaired in vitro DNA resection and sens

233 (polypyrimidine tract-binding protein 1) and HNRNP L (heterogeneous nuclear ribonucleoprotein L) prot

234 574-3p, acting as a decoy, binds cytoplasmic hnRNP L and prevents its binding to the CARE and stimula

235 Here, we identify hnRNP L as a factor that protects mRNAs with NMD-inducin

236 CRISPR/Cas9 deletion of hnRNP L binding sites near the BCL2 stop codon reduces e

237 The RNA processing factor hnRNP L is required for T cell development and function.

238 ing T cell differentiation, and knockdown of hnRNP L or hnRNP A1 results in the lower induction of Tr

239 gether, our data indicate that protection by hnRNP L overrides the presence of multiple 3'UTR introns

240 lasmic accumulation of Tyr359-phosphorylated hnRNP L sequesters miR-574-3p, overcoming its decoy acti

241 ells, in agreement with the critical role of hnRNP L throughout T cell biology.

242 eported that competition between miR-297 and hnRNP L to bind a 3UTR-localized CA-rich element (CARE)

243 demonstrating that the RNA-binding protein, hnRNP L, protects a subset of RNAs from degradation by N

244 by additional RNA-binding proteins, such as hnRNP L, PTB/nPTB and hnRNP A1/A2.

245 tiple RNA recognition motif (RRM) domains of hnRNP L, synergizes with miR-297, reduces VEGFA mRNA tra

246 Importantly, based on the binding profile of hnRNP L, we validate numerous instances of hnRNP L-depen

247 f hnRNP L, we validate numerous instances of hnRNP L-dependent alternative splicing of genes critical

248 n via interaction with the ribonucleoprotein hnRNP L-like (hnRNP LL) has prompted a more detailed stu

249 between miR-574-3p, a CA-rich microRNA, and hnRNP L.

250 d by its 3'UTR length and ability to recruit hnRNP L.

251 ly, heterogeneous nuclear ribonucleoprotein (hnRNP) L or hnRNP A1 are Akt substrates during Treg indu

252 , the lnc13 disease-associated variant binds hnRNPD less efficiently than its wild-type counterpart,

253 ibrium perspective, that small molecules and hnRNP LL can modulate bcl-2 transcription through intera

254 iments using the individual RRM domains from hnRNP LL confirm the role of this transcription factor i

255 otif (RRM1) of putative transcription factor hnRNP LL containing nucleobase amino acids at specific p

256 basis for the recognition of the i-motif by hnRNP LL is determined, and we demonstrate that the prot

257 ognition algorithm, we found that IMC-48 and hnRNP LL share 80% similarity in stabilizing i-motifs wi

258 RRM1 domain of putative transcription factor hnRNP LL was cotransformed with plasmid pTECH-Pyl-OP in

259 The RNA recognition motifs (RRMs) of hnRNP LL were expressed individually, and both RRM1 and

260 ion with the ribonucleoprotein hnRNP L-like (hnRNP LL) has prompted a more detailed study of the natu

261 We show that splicing repression mediated by hnRNP M is stimulated by Rbfox.

262 ron-bound Rbfox is associated with LASR, and hnRNP M motifs are enriched adjacent to Rbfox crosslinki

263 a multimeric complex containing the proteins hnRNP M, hnRNP H, hnRNP C, Matrin3, NF110/NFAR-2, NF45,

264 tors and repressors, such as SR proteins and hnRNPs, modulate spliceosome assembly and regulate alter

265 he discovery that ubiquilin-2 interacts with hnRNP proteins and that mutation in either protein disru

266 enrichment of numerous splicing factors like hnRNP proteins before ZGA was surprising, because matern

267 We observed that SR and hnRNP proteins tend to act coordinately with each other,

268 vestigate the protein connectivity of SR and hnRNP proteins to the core spliceosome using probabilist

269 eded to assemble an EDC with the eviction of hnRNP proteins, the late recruitment of SR proteins, and

270 NA processing, including selective groups of hnRNP proteins, through its N-terminal region, and direc

271 by the conserved RNA binding protein Syncrip/hnRNP Q.

272 rotein 43 (Gap-43) mRNA as a novel target of hnRNP-Q1 and have demonstrated that hnRNP-Q1 represses G

273 of Gap-43 mRNA that directly interacts with hnRNP-Q1 as a means to inhibit Gap-43 mRNA translation.

274 hnRNP-Q1 is an mRNA-binding protein that regulates mRNA

275 hnRNP-Q1 is highly expressed in brain tissue, suggesting

276 Our results reveal that hnRNP-Q1 knockdown increased nascent axon length, total

277 arget of hnRNP-Q1 and have demonstrated that hnRNP-Q1 represses Gap-43 mRNA translation and consequen

278 Therefore hnRNP-Q1-mediated repression of Gap-43 mRNA translation

279 ied heterogeneous nuclear ribonucleoproteins hnRNP R and hnRNP U as KPNA7-interacting proteins.

280 nuclear ribonucleoprotein (hnRNP)-A2/B1 and hnRNP-R as interactors binding directly to the ASCL1 mRN

281 that tissue-selective loss of the conserved hnRNP RALY enriches for metabolic pathways.

282 However, upon damage, HNRNPD re-localized to gammaH2Ax foci and its silencing

283 of heterogeneous nuclear ribonucleoproteins (hnRNPs) regulates the posttranscriptional fate of RNA du

284 omain, the domain most frequently mutated in hnRNP-related proteins that cause ALS.

285 control of IDR-mediated interactions between hnRNPs represents an important and recurring mechanism u

286 Indeed, HNRNPD silencing reduced: the ssDNA fraction upon campto

287 o phase-separated forms of full-length human hnRNPs (TDP-43, FUS, hnRNPA2) and their low-complexity d

288 n-dependent interplay between a miRNA and an hnRNP that regulates their functions in a bidirectional

289 tablished a strong link between mutations of hnRNP U and human epilepsies and intellectual disability

290 Mutations of human Slo2 channel and hnRNP U are strongly linked to epileptic disorders and i

291 neous nuclear ribonucleoproteins hnRNP R and hnRNP U as KPNA7-interacting proteins.

292 Loss of hnRNP U expression in cardiomyocytes also leads to aberr

293 onclusive evidence for the essential role of hnRNP U in heart development and function and in the reg

294 However, it is unclear how mutations of hnRNP U may cause such disorders.

295 underlying neurological disorders caused by hnRNP U mutations.

296 T Heterogeneous nuclear ribonucleoprotein U (hnRNP U) belongs to a family of RNA-binding proteins tha

297 e heterogeneous nuclear ribonucleoprotein U (hnRNP U) in the heart develop lethal dilated cardiomyopa

298 n heterogeneous nuclear ribonucleoprotein U (hnRNP U), plays an important role in regulating the expr

299 tions of HRPU-2, a worm homolog of mammalian hnRNP U, result in dysfunction of a Slo2 potassium chann

300 heterogenous nuclear ribonuclear protein U (hnRNP-U), is phosphorylated on serine 59 by the DNA-depe

301 nts on 19 RBPs involved in splicing (such as hnRNPs, U2AF2, ELAVL1, TDP-43 and FUS) and processing of