Heterogeneous nuclear ribonucleoprotein U

Definition:

DNA- and RNA-binding protein involved in several cellular processes such as nuclear chromatin organization, telomere-length regulation, transcription, mRNA alternative splicing and stability, Xist-mediated transcriptional silencing and mitotic cell progression. Plays a role in the regulation of interphase large-scale gene-rich chromatin organization through chromatin-associated RNAs (caRNAs) in a transcription-dependent manner, and thereby maintains genomic stability. Required for the localization of the long non-coding Xist RNA on the inactive chromosome X (Xi) and the subsequent initiation and maintenance of X-linked transcriptional gene silencing during X-inactivation (By similarity). Plays a role as a RNA polymerase II (Pol II) holoenzyme transcription regulator. Promotes transcription initiation by direct association with the core-TFIIH basal transcription factor complex for the assembly of a functional pre-initiation complex with Pol II in a actin-dependent manner. Blocks Pol II transcription elongation activity by inhibiting the C-terminal domain (CTD) phosphorylation of Pol II and dissociates from Pol II pre-initiation complex prior to productive transcription elongation. Positively regulates CBX5-induced transcriptional gene silencing and retention of CBX5 in the nucleus. Negatively regulates glucocorticoid-mediated transcriptional activation. Key regulator of transcription initiation and elongation in embryonic stem cells upon leukemia inhibitory factor (LIF) signaling (By similarity). Involved in the long non-coding RNA H19-mediated Pol II transcriptional repression. Participates in the circadian regulation of the core clock component BMAL1 transcription (By similarity). Plays a role in the regulation of telomere length. Plays a role as a global pre-mRNA alternative splicing modulator by regulating U2 small nuclear ribonucleoprotein (snRNP) biogenesis. Plays a role in mRNA stability. Component of the CRD-mediated complex that promotes MYC mRNA stabilization. Enhances the expression of specific genes, such as tumor necrosis factor TNFA, by regulating mRNA stability, possibly through binding to the 3'-untranslated region (UTR). Plays a role in mitotic cell cycle regulation. Involved in the formation of stable mitotic spindle microtubules (MTs) attachment to kinetochore, spindle organization and chromosome congression. Phosphorylation at Ser-59 by PLK1 is required for chromosome alignement and segregation and progression through mitosis. Contributes also to the targeting of AURKA to mitotic spindle MTs. Binds to double- and single-stranded DNA and RNA, poly(A), poly(C) and poly(G) oligoribonucleotides. Binds to chromatin-associated RNAs (caRNAs). Associates with chromatin to scaffold/matrix attachment region (S/MAR) elements in a chromatin-associated RNAs (caRNAs)-dependent manner. Binds to the Xist RNA. Binds the long non-coding H19 RNA. Binds to SMN1/2 pre-mRNAs at G/U-rich regions. Binds to small nuclear RNAs (snRNAs). Binds to the 3'-UTR of TNFA mRNA. Binds (via RNA-binding RGG-box region) to the long non-coding Xist RNA; this binding is direct and bridges the Xist RNA and the inactive chromosome X (Xi) (By similarity). Also negatively regulates embryonic stem cell differentiation upon LIF signaling (By similarity). Required for embryonic development (By similarity). Binds to brown fat long non-coding RNA 1 (Blnc1); facilitates the recruitment of Blnc1 by ZBTB7B required to drive brown and beige fat development and thermogenesis (By similarity).; (Microbial infection) Negatively regulates immunodeficiency virus type 1 (HIV-1) replication by preventing the accumulation of viral mRNA transcripts in the cytoplasm.

References:

[1]. Susana T Valente, et al. Inhibition of HIV-1 gene expression by a fragment of hnRNP U. Mol Cell. 2006 Aug;23(4):597-605. [Content Brief]

[2]. Lars Jønson, et al. Molecular composition of IMP1 ribonucleoprotein granules. Mol Cell Proteomics. 2007 May;6(5):798-811. [Content Brief]

[3]. Masato Yugami, et al. hnRNP-U enhances the expression of specific genes by stabilizing mRNA. FEBS Lett. 2007 Jan 9;581(1):1-7. [Content Brief]

[4]. Doreen Weidensdorfer, et al. Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs. RNA. 2009 Jan;15(1):104-15. [Content Brief]

[5]. M Kiledjian, et al. Primary structure and binding activity of the hnRNP U protein: binding RNA through RGG box. EMBO J. 1992 Jul;11(7):2655-64. [Content Brief]

[6]. Alexander Kukalev, et al. Actin and hnRNP U cooperate for productive transcription by RNA polymerase II. Nat Struct Mol Biol. 2005 Mar;12(3):238-44. [Content Brief]

[7]. M Kipp, et al. SAF-Box, a conserved protein domain that specifically recognizes scaffold attachment region DNA. Mol Cell Biol. 2000 Oct;20(20):7480-9. [Content Brief]

[8]. M Eggert, et al. The glucocorticoid receptor is associated with the RNA-binding nuclear matrix protein hnRNP U. J Biol Chem. 1997 Nov 7;272(45):28471-8. [Content Brief]

[9]. Pauline Douglas, et al. Phosphorylation of SAF-A/hnRNP-U Serine 59 by Polo-Like Kinase 1 Is Required for Mitosis. Mol Cell Biol. 2015 Aug;35(15):2699-713. [Content Brief]

[10]. F O Fackelmayer, et al. hnRNP-U/SAF-A is encoded by two differentially polyadenylated mRNAs in human cells. Biochim Biophys Acta. 1994 Mar 1;1217(2):232-4. [Content Brief]

[11]. Norishige Yamada, et al. Xist Exon 7 Contributes to the Stable Localization of Xist RNA on the Inactive X-Chromosome. PLoS Genet. 2015 Aug 5;11(8):e1005430. [Content Brief]

[12]. Hai-shan Bi, et al. H19 inhibits RNA polymerase II-mediated transcription by disrupting the hnRNP U-actin complex. Biochim Biophys Acta. 2013 Oct;1830(10):4899-906. [Content Brief]

[13]. M K Kim, et al. hnRNP U inhibits carboxy-terminal domain phosphorylation by TFIIH and represses RNA polymerase II elongation. Mol Cell Biol. 1999 Oct;19(10):6833-44. [Content Brief]

[14]. M Kipp, et al. Apoptotic cleavage of scaffold attachment factor A (SAF-A) by caspase-3 occurs at a noncanonical cleavage site. J Biol Chem. 2000 Feb 18;275(7):5031-6. [Content Brief]

[15]. F Göhring, et al. The novel SAR-binding domain of scaffold attachment factor A (SAF-A) is a target in apoptotic nuclear breakdown. EMBO J. 1997 Dec 15;16(24):7361-71. [Content Brief]

[16]. F O Fackelmayer, et al. Purification of two isoforms of hnRNP-U and characterization of their nucleic acid binding activity. Biochemistry. 1994 Aug 30;33(34):10416-22. [Content Brief]

[17]. Ryu-Suke Nozawa, et al. SAF-A Regulates Interphase Chromosome Structure through Oligomerization with Chromatin-Associated RNAs. Cell. 2017 Jun 15;169(7):1214-1227.e18. [Content Brief]

[18]. Rui Xiao, et al. Nuclear matrix factor hnRNP U/SAF-A exerts a global control of alternative splicing by regulating U2 snRNP maturation. Mol Cell. 2012 Mar 9;45(5):656-68. [Content Brief]

[19]. Dragony Fu, et al. Purification of human telomerase complexes identifies factors involved in telomerase biogenesis and telomere length regulation. Mol Cell. 2007 Dec 14;28(5):773-85. [Content Brief]

[20]. F O Fackelmayer, et al. Nucleic-acid-binding properties of hnRNP-U/SAF-A, a nuclear-matrix protein which binds DNA and RNA in vivo and in vitro. Eur J Biochem. 1994 Apr 15;221(2):749-57. [Content Brief]

[21]. H Romig, et al. Characterization of SAF-A, a novel nuclear DNA binding protein from HeLa cells with high affinity for nuclear matrix/scaffold attachment DNA elements. EMBO J. 1992 Sep;11(9):3431-40. [Content Brief]

[22]. F Göhring, et al. The scaffold/matrix attachment region binding protein hnRNP-U (SAF-A) is directly bound to chromosomal DNA in vivo: a chemical cross-linking study. Biochemistry. 1997 Jul 8;36(27):8276-83. [Content Brief]

[23]. Joost H A Martens, et al. Scaffold/matrix attachment region elements interact with a p300-scaffold attachment factor A complex and are bound by acetylated nucleosomes. Mol Cell Biol. 2002 Apr;22(8):2598-606. [Content Brief]

[24]. Nan Ma, et al. The nuclear scaffold protein SAF-A is required for kinetochore-microtubule attachment and contributes to the targeting of Aurora-A to mitotic spindles. J Cell Sci. 2011 Feb 1;124(Pt 3):394-404. [Content Brief]

[25]. Maya Ameyar-Zazoua, et al. Physical and functional interaction between heterochromatin protein 1alpha and the RNA-binding protein heterogeneous nuclear ribonucleoprotein U. J Biol Chem. 2009 Oct 9;284(41):27974-27979. [Content Brief]

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