Author Summary Herpesviruses hijack cellular components to enhance viral gene expression. This is particularly important for the efficient nuclear export of herpesvirus intronless mRNAs to allow the production of viral proteins. We have previously demonstrated that Kaposis sarcoma-associated herpesvirus encodes a conserved protein, ORF57, which recruits essential cellular mRNA export proteins onto the viral intronless mRNAs to form an export competent viral ribonucleoprotein particle. Specifically, we have shown that ORF57 interacts directly with the cellular export adaptor protein, Aly, to recruit other cellular mRNA export proteins. Surprisingly however, depletion of Aly has a limited effect on both cellular and viral mRNA nuclear export levels, suggesting a degree of redundancy in the export pathways and the existence of other export adaptor proteins. Here we have identified a novel interaction between ORF57 and a second export adaptor protein, UIF. We show for the first time that the ORF57-UIF
The worlds first wiki where authorship really matters. Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts.
Influenza A virus nucleoprotein (NP) is a structural component that encapsulates the viral genome into the form of ribonucleoprotein complexes (vRNPs). Efficient assembly of vRNPs is critical for the virus life cycle. The assembly route from RNA-free NP to the NP-RNA polymer in vRNPs has been suggested to require a cellular factor UAP56, but the mechanism is poorly understood. Here, we characterized the interaction between NP and UAP56 using recombinant proteins and showed that UAP56 features two NP binding sites. In addition to the UAP56 core comprised of two RecA domains, we identified the N-terminal extension (NTE) of UAP56 as a previously unknown NP binding site. In particular, UAP56-NTE recognizes the nucleic acid binding region of NP. This corroborates our observation that binding of UAP56-NTE and RNA to NP is mutually exclusive. Collectively, our results reveal the molecular basis for how UAP56 acts on RNA-free NP, and provide new insights into NP-mediated influenza genome packaging ...
A phosphoprotein adapter involved in the XPO1-mediated U snRNA export from the nucleus. Bridge components required for U snRNA export, the cap binding complex (CBC)-bound snRNA on the one hand and the GTPase Ran in its active GTP-bound form together with the export receptor XPO1 on the other. Its phosphorylation in the nucleus is required for U snRNA export complex assembly and export, while its dephosphorylation in the cytoplasm causes export complex disassembly. It is recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Its compartmentalized phosphorylation cycle may also contribute to the directionality of export. Binds strongly to m7G-capped U1 and U5 small nuclear RNAs (snRNAs) in a sequence-unspecific manner and phosphorylation-independent manner (By similarity). Plays also a role in the biogenesis
Component of the SAC3-THP1 complex, which functions in transcription-coupled mRNA export from the nucleus to the cytoplasm. SAC3-THP1 functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), by association with components of the nuclear mRNA export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the nucleoporin NUP1 at the nuclear basket. THP1 binds to RNA in vitro.
We describe a novel RNA binding protein, Y14, a predominantly nuclear nucleocytoplasmic shuttling protein. Interestingly, Y14 associates preferentially with mRNAs produced by splicing but not with pre-mRNAs, introns, or mRNAs produced from intronless cDNAs. Y14 associates with both nuclear mRNAs and newly exported cytoplasmic mRNAs. Splicing of a single intron is sufficient for Y14 association. Y14-containing nuclear complexes are different from general hnRNP complexes. They contain hnRNP proteins and several unique proteins including the mRNA export factor TAP. Thus, Y14 defines novel intermediates in the pathway of gene expression, postsplicing nuclear preexport mRNPs, and newly exported cytoplasmic mRNPs, whose composition is established by splicing. These findings suggest that pre-mRNA splicing imprints mRNA with a unique set of proteins that persists in the cytoplasm and thereby communicates the history of the transcript ...
Many mammalian and viral genes are alternatively spliced and subject to regulation at the post- transcriptional level. However, relatively little is known about the cellular mechanisms for this regulation. We are using retroviruses as model systems to elucidate these mechanisms. Some of our studies focus on HIV Rev, an essential HIV protein. Rev mediates the nucleo-cytoplasmic export of unspliced and incompletely spliced HIV RNAs and provides an important HIV drug target. Another major focus of the laboratory is the function of the constitutive transport element (CTE). The CTE interacts directly with host cell proteins to facilitate export of intron containing RNA. We are currently analyzing the function of cellular proteins that are involved in the CTE mediated export pathway. One is NXF1 (TAP), a protein which has been proposed to play an essential role in cellular mRNA export. A second protein under study is NXT1, an important TAP cofactor. CTE function is also enhanced by SAM68, a major ...
The results described in this paper indicate that HIV unspliced RNA export and Gag trafficking to the plasma membrane are linked. By simply changing the RNA export element from the RRE to 4 × CTE, we can restore Gag assembly and budding in murine cells (Figures 3 and 5). To explain how a pretranslational event, RNA export, could modulate a post‐translational event, membrane trafficking, we hypothesize that HIV RNA is marked at (or by) nuclear export such that the cytosolic fate of the encoded Gag is predetermined. Based on our findings, both the RRE/Rev/Crm1 and 4 × CTE/NXF1 nuclear export pathways successfully mark unspliced gag‐pol mRNA in human cells and promote proper assembly. However, in murine cells, marking through the action of RRE/Rev/Crm1 is defective and HIV assembly is inhibited. Possibilities for the mark include the structure of the mRNA itself or proteins that comprise the mRNP; these could be added or removed as the export complex is formed, as it transits the NPC, ...
In higher eukaryotes, messenger RNAs (mRNAs) are exported from the nucleus to the cytoplasm via factors deposited near the 5 end of the transcript during splicing. The signal sequence coding region (SSCR) can support an alternative mRNA export (ALREX) pathway that does not require splicing. However …
DDX3 is a DEAD-box protein (Figure 3A). Although DDX3 has been shown to interact with RNA transport factors TAP/NXF1 and REF/Aly, it does not appear to play a role in bulk mRNA export [32-34]. It is interesting to note that Ded1 (yeast DDX3 homolog) modulates translation by controlling the conformation of eIF4F-mRNA complex [35], suggesting a role of Ded1/DDX3 in translation. The function of DDX3 in RNA export was not recognized until DDX3 was found to participate in the Rev-dependent export of unspliced and partially spliced HIV-1 RNAs [3]. Rev is co-immunoprecipitated with DDX3, but a direct interaction between the two proteins has not been experimentally demonstrated. Rather, the purified GST-CRM1 is able to pull down the in vitro translated DDX3. This direct interaction depends on the DDX3 fragment at amino acid positions 260 to 517 that does not include the NES (nuclear export signal) sequence, and is Ran-GTP independent (Figure 3A, 3C), which suggests that instead of a cargo, DDX3 acts as ...
1JN5: Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like domain of the TAP/p15 mRNA nuclear export factor.
Deutsch, G.B., Zielonka, E.M., Coutandin, D., Weber, T.A., Schäfer, B., Hannewald, J., Luh, L.M., Durst, F.G., Ibrahim, M., Hoffmann, J., Niesen, F.H., Sentürk, A., Kunkel, H., Brutschy, B., Schleiff, E., Knapp, S., Acker-Palmer, A., Grez, M., McKeon, F. and Dötsch, V. (2011) "DNA damage in oocytes induces an irreversible switch of the quality control factor TAp63α from dimer to tetramer". Cell, 144:566-576.. ...
The coordination and coupling of the several steps in mRNA biogenesis helps to ensure proper regulation of gene expression. The DEAD-box helicase Dbp5/Rat8 is an essential mRNA export factor that has also been implicated in other steps of mRNA ...
The coordination and coupling of the several steps in mRNA biogenesis helps to ensure proper regulation of gene expression. The DEAD-box helicase Dbp5/Rat8 is an essential mRNA export factor that has also been implicated in other steps of mRNA ...
Shop Nuclear transport factor ELISA Kit, Recombinant Protein and Nuclear transport factor Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
IFN-γ induces the expression of a wide variety of genes, many of which are involved in antiviral response (23). To determine whether induction of Nup98 and Nup96 was sufficient to reverse the M protein export block, we tested whether transfection with Nup98 and Nup96 cDNA would substitute for IFN-γ and relieve the inhibition of mRNA export. Using a luciferase reporter gene assay (24), cells were co-transfected with a mixture of plasmids coding for the M protein alone, for Nup98 and Nup96 alone, or for both. M protein expression clearly inhibited luciferase expression, and this inhibition was partially relieved by Nup98 and Nup96 expression (Fig. 4C). Thus, Nup98 and Nup96 expression is capable of reversing M protein-mediated inhibition of nuclear mRNA export.. The mechanism by which increased expression of Nup98 and of Nup96 reverses M protein-mediated inhibition of mRNA export remains to be elucidated. The inhibitory region of the M protein has been mapped (12, 25) and shown to target the ...
mRNA export factor is a protein that in humans is encoded by the RAE1 gene. Mutations in the Schizosaccharomyces pombe Rae1 and Saccharomyces cerevisiae Gle2 genes have been shown to result in accumulation of poly(A)-containing mRNA in the nucleus, suggesting that the encoded proteins are involved in RNA export. The protein encoded by this gene is a homolog of yeast Rae1. It contains four WD40 motifs, and has been shown to localize to distinct foci in the nucleoplasm, to the nuclear rim, and to meshwork-like structures throughout the cytoplasm. This gene is thought to be involved in nucleocytoplasmic transport, and in directly or indirectly attaching cytoplasmic mRNPs to the cytoskeleton. Alternatively spliced transcript variants encoding the same protein have been found for this gene. RAE1 has been shown to interact with NUP98. GRCh38: Ensembl release 89: ENSG00000101146 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000027509 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse ...
1KOH: The crystal structure and mutational analysis of a novel RNA-binding domain found in the human Tap nuclear mRNA export factor.
Although several SR proteins were reported to shuttle poorly in HeLa cells (Cáceres et al., 1998; Lin et al., 2005; Sapra et al., 2009), we have recently shown that all SR proteins act as NXF1 adapters in pluripotent P19 cells (Müller-McNicoll et al., 2016). To investigate this discrepancy, we developed a quantitative shuttling assay to measure the nucleocytoplasmic shuttling of seven canonical family members. Key technical advances were the use of stable clonal cell lines expressing similar and near-endogenous levels of GFP-tagged proteins (donor) and a membrane-bound marker protein (recipient). Quantification of total nuclear fluorescence in a large number of donor and recipient cells allowed for the first time the determination of mean shuttling capacities of individual SR proteins. We could show that all seven SR proteins shuttle in P19 cells; however, they shuttle to different extents, suggesting a differential participation in nuclear export and retention of mRNAs. SR proteins were ...
The large majority of genes encoded by humans and other metazoans contain introns. In general, mRNAs containing introns give rise to a higher level of the encoded protein than do the equivalent intronless, cDNA-derived mRNAs. The mechanisms underlying this difference are complex because splicing can strongly influence not only the efficiency of mRNA 3′ end formation but also mRNA stability and even translation (Ryu and Mertz, 1989; Niwa et al., 1990; Matsumoto et al., 1998). Nevertheless, for most human genes, splicing is not essential for detectable mRNA and protein synthesis. In fact, a recent survey of 15 genes showed that the presence of an excisable intron enhanced gene expression in human cells by an average of 6.3±4.7 fold with a range of from 1.5- to over 20-fold (S. Lu and B. R. Cullen, unpublished).. The first evidence suggesting that splicing also enhances the efficiency of mRNA export came from the demonstration that several intron-containing mRNAs are exported more efficiently ...
The newly formed stable of NXT known as the Undisputed Era reveals what message they have for the rest of NXT. Click to read the full news
Kit Component:- KN311391G1, Nxt1 gRNA vector 1 in pCas-Guide vector- KN311391G2, Nxt1 gRNA vector 2 in pCas-Guide vector- KN311391D, donor vector…
Come Get Her - Rae Sremmurd | Bài hát: Come Get Her - Rae Sremmurd Somebody come to the floor, it feels l... | Nghe nhạc hay online mới nhất chất lượng cao
Makeover using Chanel 65 ESPIÃ Â GLE JOUES CONTRASTE, NARS Pandora Duo Eyeshadow Compact and Urban Decay Dream Surreal Skin Mineral Makeup. Try makeover games at TAAZ.com.
The Best and Worst of WWE NXT for October 9, 2013, featuring Rob Van Dam vs. Aiden English, an un-BO-lievable handshake and more.
bought this car used with 103,000 miles. It has been a workhorse and a daily driver. outstanding quality and fun to drive. It now has 120,000 and going strong.
Profitable Forex indicators without redrawing 2015 #### SUN-JUPITER ASPECTS FOREX Online binary option system MEX #### Vegas tunnel forex
Nuclear mRNA export is a highly complex and regulated process in cells. Cellular transcripts must undergo successful maturation processes, including splicing, 5-, and 3-end processing, which are essential for assembly of an export competent ribonucleoprotein particle. Many viruses replicate in the nucleus of the host cell and require cellular mRNA export factors to efficiently export viral transcripts. However, some viral mRNAs undergo aberrant mRNA processing, thus prompting the viruses to express their own specific mRNA export proteins to facilitate efficient export of viral transcripts and allowing translation in the cytoplasm. This review will focus on the Kaposis sarcoma-associated herpesvirus ORF57 protein, a multifunctional protein involved in all stages of viral mRNA processing and that is essential for virus replication. Using the example of ORF57, we will describe cellular bulk mRNA export pathways and highlight their distinct features, before exploring how the virus has evolved to exploit
Essential messenger RNA (mRNA) export factors execute critical steps to mediate directional transport through nuclear pore complexes (NPCs). At cytoplasmic NPC filaments, the ATPase activity of DEAD-box protein Dbp5 is activated by inositol hexakisphosphate (IP(6))-bound Gle1 to mediate remodeling of mRNA-protein (mRNP) complexes. Whether a single Dbp5 executes multiple remodeling events and how Dbp5 is recycled are unknown. Evidence suggests that Dbp5 binding to Nup159 is required for controlling interactions with Gle1 and the mRNP. Using in vitro reconstitution assays, we found here that Nup159 is specifically required for ADP release from Dbp5. Moreover, Gle1-IP(6) stimulates ATP binding, thus priming Dbp5 for RNA loading. In vivo, a dbp5-R256D/R259D mutant with reduced ADP binding bypasses the need for Nup159 interaction. However, NPC spatial control is important, as a dbp5-R256D/R259D nup42Δ double mutant is temperature-sensitive for mRNA export. Further analysis reveals that remodeling ...
Nuclear export of mRNA is mediated by interactions between soluble factors and nuclear pore complex (NPC) proteins. In Saccharomyces cerevisiae, Nab2 is an essential RNA-binding protein that shuttles between the nucleus and cytoplasm. The mechanism for trafficking of Nab2-bound mRNA through the NPC has not been defined. Gle1 is also required for mRNA export, and Gle1 interactions with NPC proteins, the RNA helicase Dbp5, and Gfd1 have been reported. Here we report that Nab2, Gfd1, and Gle1 associate in a complex. By using immobilized recombinant Gfd1, Nab2 was isolated from total yeast lysate. A similar biochemical assay with immobilized recombinant Nab2 resulted in coisolation of Gfd1 and Gle1. A Nab2-Gfd1 complex was also identified by coimmunoprecipitation from yeast lysates. In vitro binding assays with recombinant proteins revealed a direct association between Nab2 and Gfd1, and two-hybrid assays delineated Gfd1 binding to the N-terminal Nab2 domain. This N-terminal Nab2 domain is distinct ...
In this study, we used multiple functional assays to characterize NXT1, a protein that we identified based on its sequence relatedness to NTF2. The similarities of NXT1 and NTF2 include their amino acid identity (26% within a species), low molecular sizes (NTF2, 127 amino acids; NXT1, 140 amino acids), acidic isoelectric points (NTF2, 5.1; NXT1, 5.0), steady-state nuclear localization (45), interaction with the NPC (6, 31, 36), and direct binding to Ran (31, 34). However, NXT1 and NTF2 also have distinct properties that provide insights into their respective functions. NTF2 binds to Ran-GDP and mediates its import into the nucleus (38, 43,45), thereby functioning as a nuclear import factor. In contrast, NXT1 binds to Ran-GTP. The precise function of this interaction is unknown, but it clearly suggests a role in nuclear export. Indeed, using a permeabilized cell assay (16), we have shown here that NXT1 stimulates nuclear export of PKI. The logical interpretation of this result is that NXT1 ...
In eukaryotic cells, most mRNAs are exported from the nucleus by the transcription export (TREX) complex, which is loaded onto mRNAs after their splicing and capping. We have studied in mammalian cells the nuclear export of mRNAs that code for secretory proteins, which are targeted to the endoplasmic reticulum membrane by hydrophobic signal sequences. The mRNAs were injected into the nucleus or synthesized from injected or transfected DNA, and their export was followed by fluorescent in situ hybridization. We made the surprising observation that the signal sequence coding region (SSCR) can serve as a nuclear export signal of an mRNA that lacks an intron or functional cap. Even the export of an intron-containing natural mRNA was enhanced by its SSCR. Like conventional export, the SSCR-dependent pathway required the factor TAP, but depletion of the TREX components had only moderate effects. The SSCR export signal appears to be characterized in vertebrates by a low content of adenines, as ...
In previous studies, we established a genetic interaction between the NC2-component Bur6 and mRNA export. More specifically, mutations in BUR6 were observed to be synthetic lethal with dbp5-2, yra1-1 or sub2-85 mutant alleles (Estruch and Cole 2003; F. Estruch, L. Peiró-Chova and C. Cole, unpublished results). To gain more information about the causes of the genetic relationships between BUR6 and genes encoding mRNA export factors, we selected for genes that, upon overexpression, could bypass the synthetic lethality of the bur6-1 and dbp5-2 mutations. This genetic screen identified a truncated version of Rpb2 (Rpb2t) as a multicopy suppressor of both the bur6-1 dbp5-2 and the mot1-301 dbp5-2 double-mutant strain (F. Estruch, L. Peiró-Chova and C. Cole, unpublished results). Interestingly, overexpression of different truncated forms of Rpb2 acted as a suppressor of the growth defect caused by a limiting amount of NC2 or Mot1, like that provided by the expression of the PGAL10-BUR6, PGAL10-YDR1, ...
Shop Multidrug export protein ELISA Kit, Recombinant Protein and Multidrug export protein Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
NIH3T3 cells showing the localization of nuclear transport factor RanBP1 and F-actin in interphase cells. Cells were fixed in formaldehyde and labele...
Esant išplitusiai ligai ir skrandžio navikui nekraujuojant, nesant stenozės ir normaliai praeinant maistui operacija nereikalinga. Jei yra stenozė arba navikas kraujuoja gali būti atliekamos paliatyvios operacijos (naviką apeinančioji anastomozė, maitinamoji jenunostomija ar endoskopu įstumiami protezai). Šių operacijų metu skrandžio vėžys neišgydomas, tačiau pagerėja ligonio savijauta. Gydymas priešvėžiniais vaistais pagerina ligonių savijautą, gyvenimo kokybę ir prailgina išgyvenamumą: nuo vidutiniškai 3 mėnesių skiriant tik simptominį gydymą iki 12-14 mėnesių skiriant kombinuotą gydymą vaistais. Būtina ištirti naviko audinį ieškant HER2 receptoriaus. Jei nustatomas HER2 teigiamas navikas, reikia skirti gydymą trastuzumabu, šiuo atveju kombinuojant trastuzumabą ir chemoterapiją pasiekiama ligonių 16 mėnesių išgyvenamumo mediana[8]. Skrandžio adenokarcinoma gydoma 5-fluoruracilo ir platinos preparatų (cisplatina, oksaliplatina) kombinacijomis. ...
In this post, we will see how we can import and export excel data in Asp.net Core. We are using EPPlus.Core library which helps us to perform import and export operations. I hope you will like it.
It speaks to the amazing year Canadian Carly Rae Jepsen has had that her huge upcoming gig at the Grey Cup in front of more than 52,000 fans doesnt even rank as her biggest yet.
食品、饮料与营养保健品 (Shijiazhuang Aopharm Import & Export Trading Co., Ltd.) | 食品、饮料与营养保健品 一站式进行配方,数据表,物质安全数据表搜索,产品特性和样品申请 -- 免费使用
繼承對種族主義的批判. 印度種姓制度以血緣世襲的方式區分人的貴賤,達利特人(賤民)最低等被視為不可接觸,至今仍存。另一邊廂,美國上幾個世紀的黑奴制度以膚色區劃奴隸階級,即使後來黑奴解放,深膚色人種仍然受著嚴重的經濟和文化歧視。. 人為地建構身份階層,對特定族群作出有違人性的區分,是鞏固權力和維持優勢地位的一貫做法。但這做法也反向操作,用來挑戰某些價值和社會規範。例如,應用於性傾向,可得出異性戀中心主義:異性戀是一種由人建構出來的階級體制,令社會裡不是異性戀的人受到排拒,剝削了同性戀的人性和尊嚴……藉由建構同性戀和被壓迫的身份,他們聚集了群眾和得到某種道德力量。在建構出假想敵後,同性戀政治份子批判異性戀中心主義的社會,製作仇恨名單(The Export of ...
ASP.NET GridView to Excel conversion.; Author: pramod.hegde; Updated: 15 Apr 2012; Section: Office Development; Chapter: Enterprise Systems; Updated: 15 Apr 2012
This file exports the most commonly used modules within HLearn-distributions. Most likely this is the only file you will have to import. ...
Kova su antsvoriu tikriausiai yra viena iš pačių seniausių moterų grumtynių. Ši sporto šaka ypatingai išpopuliarėja prieš šventes. O likus keletu
Macromolecular trafficking across the nuclear envelope involves interactions between cytosolic transport factors and nuclear pore complex proteins. The p62 complex, an assembly of 62, 58, 54, and 45-kD O-linked glycoproteins-localized near the central gated channel of the nuclear pore complex, has been directly implicated in nuclear protein import. The cDNA cloning of rat p62 was reported previously. We have now carried out cDNA cloning of rat p58, p54, and p45. We found that p58 contains regions with FG (Phe, Gly) and PA (Pro, Ala) repeats at both its NH2 and COOH termini separated by a predicted alpha-helical coiled-coil region, while p54 has an NH2-terminal FG and PA repeat region and a COOH-terminal predicted coiled-coil region. p45 and p58 appear to be generated by alternative splicing, with p45 containing the NH2-terminal FG repeat region and the coiled-coil region of p58. Using immunogold electron microscopy, we found that p58/p45 and p54 are localized on both sides of the nuclear pore ...
Nuclear pore complexes. Coloured atomic force micrograph (AFM) of the surface of an oocyte (egg cell) nucleus showing the nuclear pore complexes (NPCs). NPCs are complexes of proteins that are embedded in the nuclear envelope. All material moving between the nucleus and the cell cytoplasm passes through these channels. They allow passive transport (diffusion) of ions and small molecules and active transport (energy dependent) of proteins and RNAs (ribonucleic acids). - Stock Image G455/0064
Bidirectional transport of macromolecules between the cytoplasm and nucleus occurs through nuclear pore complexes (NPCs) embedded in the nuclear envelope. NPCs are composed of subcomplexes, and NUP43 is part of one such subcomplex, Nup107-160 (Loiodice et al., 2004 [PubMed 15146057]).[supplied by OMIM, Mar 2008 ...
Plays a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5- and 3-splice site binding components, U1 snRNP and U2AF. Can stimulate binding of U1 snRNP to a 5-splice site-containing pre-mRNA. Binds to purine-rich RNA sequences, either the octamer, 5-RGAAGAAC-3 (r=A or G) or the decamers, AGGACAGAGC/AGGACGAAGC. Binds preferentially to the 5-CGAGGCG-3 motif in vitro. Three copies of the octamer constitute a powerful splicing enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can specifically activate ASE-dependent splicing. Isoform ASF-2 and isoform ASF-3 act as splicing repressors. May function as export adapter involved in mRNA nuclear export through the TAP/NXF1 pathway ...
Our results indicate that disturbed THOC1 and ALY expression are associated with tumorogenesis. Overexpression of THOC1 has previously been correlated to the grade of invasiveness in breast tumor, and also a relationship between the levels of this protein in non-small lung cancers has been suggested [12, 15]. This study shows that not only the expression of THOC1, but also that of THO/TREX complex is upregulated in breast cancer cells. Moreover, new links between the expression of THOC1 and different tumors were found. THOC1 mRNA and protein levels are up-regulated in ovarian, and lung tumors and down-regulated in those of testis and skin. Interestingly, we show that ALY, another mRNP biogenesis factor is highly detected in proliferative cells and overexpressed in a broad range of tumors. The different pattern of expression of THOC1 and ALY in tumors could indicate a different relevance for each factor in tumorogenesis. Nevertheless, since many genes are differentially expressed in cancer ...
Nucleoporin 50 (Nup50) is a protein that in humans is encoded by the NUP50 gene.[1][2] The nuclear pore complex is a massive structure that extends across the nuclear envelope, forming a gateway that regulates the flow of macromolecules between the nucleus and the cytoplasm. Nucleoporins are the main components of the nuclear pore complex in eukaryotic cells. The protein encoded by this gene is a member of the FG-repeat containing nucleoporins that functions as a soluble cofactor in importin-alpha:beta-mediated nuclear protein import. Pseudogenes of this gene are found on chromosomes 5, 6, and 14. Two transcript variants encoding different isoforms have been found for this gene.[2] ...
Paciorkowski AR, Weisenberg J, Kelley JB, Spencer A, Tuttle E, Ghoneim D, Thio LL, Christian SL, Dobyns WB, Paschal BM; European Journal of Human Genetics 22(5) pp 589-593