Intranuclear dynamics of the Nup107-160 complex

Morchoisne-Bolhy, Stéphanie; Geoffroy, M; Bouhlel, Imène; Alves, Annabelle; Audugé, Nicolas; Baudin, Xavier; Bortle, Kevin Van; Powers, Maureen A.; Doye, Valérie

doi:10.1091/mbc.e15-02-0060

Cited by 43 publications

(46 citation statements)

References 59 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We readily observed components of the Nup107/160 scaffold complex, including Nup96, Nup133, Nup107, and Elys, colocalizing with Nup98 (Supplemental Fig. S2B, panels 2,5,8.11) in the nucleoplasm in >90% of cells, similar to what has been shown previously (Morchoisne-Bolhy et al 2015). In contrast to Pom121 and the Nup107/160 complex, we did not observe nuclear basket components, components of the cytoplasmic filaments, the Nup93/205 scaffold complex, or any of the basket and cytoplasmic filament Nups detected by antibody mAB414 colocalizing with intranuclear Nup98 (Supplemental Fig.…”

Section: Alternative Transcription Initiation Produces a Spom121 Isofsupporting

confidence: 86%

“…To test this, we expressed GFPtagged Nup133, a component of the Nup107/160 complex that has also been shown to colocalize with Nup98 in nucleoplasmic foci (Morchoisne-Bolhy et al 2015). Unlike Nup98 and sPom121, intranuclear GFP-Nup133 fluorescence recovers slowly following a photobleach (Fig.…”

Section: Spom121 and Nup98 Have Similar Intranuclear Dynamicsmentioning

confidence: 99%

“…Interestingly, however, other than Sec13, no scaffold Nups have been shown to localize in the nucleoplasm in Drosophila cells, implying that gene expression regulation probably does not occur via an NPC-like scaffold in nonmammalian species but instead involves recruitment of chromatin-modifying complexes to chromatin by individual Nups (Capelson et al 2010;Pascual-Garcia et al 2014). The recent finding that the Nup107/160 scaffold can exist away from the NPC in human cells raises the possibility that larger Nup subcomplexes probably exist in the nucleoplasm in mammalian cells (Morchoisne-Bolhy et al 2015).…”

Section: What Is the Role Of Spom121 In Mammalian Cells?mentioning

confidence: 99%

“…Most of the evidence collected in Drosophila suggested that only peripheral Nups can exist away from the NPC (Capelson et al 2010). However, a soluble fraction of the Nup107/160 scaffold complex was recently shown to colocalize with Nup98 in foci in the nucleoplasm of human HeLa cells (Morchoisne-Bolhy et al 2015).…”

mentioning

confidence: 99%

See 3 more Smart Citations

Evolution of a transcriptional regulator from a transmembrane nucleoporin

et al. 2016

View full text Add to dashboard Cite

Nuclear pore complexes (NPCs) emerged as nuclear transport channels in eukaryotic cells ∼1.5 billion years ago. While the primary role of NPCs is to regulate nucleo-cytoplasmic transport, recent research suggests that certain NPC proteins have additionally acquired the role of affecting gene expression at the nuclear periphery and in the nucleoplasm in metazoans. Here we identify a widely expressed variant of the transmembrane nucleoporin (Nup) Pom121 (named sPom121, for "soluble Pom121") that arose by genomic rearrangement before the divergence of hominoids. sPom121 lacks the nuclear membrane-anchoring domain and thus does not localize to the NPC. Instead, sPom121 colocalizes and interacts with nucleoplasmic Nup98, a previously identified transcriptional regulator, at gene promoters to control transcription of its target genes in human cells. Interestingly, sPom121 transcripts appear independently in several mammalian species, suggesting convergent innovation of Nup-mediated transcription regulation during mammalian evolution. Our findings implicate alternate transcription initiation as a mechanism to increase the functional diversity of NPC components.

show abstract

Section: Alternative Transcription Initiation Produces a Spom121 Isofsupporting

confidence: 86%

Section: Spom121 and Nup98 Have Similar Intranuclear Dynamicsmentioning

confidence: 99%

Section: What Is the Role Of Spom121 In Mammalian Cells?mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Evolution of a transcriptional regulator from a transmembrane nucleoporin

et al. 2016

View full text Add to dashboard Cite

show abstract

“…Plant NPCs are comprised of multiple copies of approximately 30 different proteins called nucleoporins (Parry, 2013;2014). Nucleoporin 98 (NUP98; a gatekeeper) and nucleoporin 96 (NUP96; a scaffold), are essential components of the NPC, and are located at both the cytoplasmic and the nuclear sides of the NPC central channel (Terry and Wente 2009;Parrott et al, 2011;Stuwe et al, 2012;Franks and Hetzer, 2013;Byrne et al, 2014;Morchoisne-Bolhy et al, 2015). In many cells, the conservedNUP98-96genes generate a long mRNA with an open reading frame (ORF) for a polyprotein.…”

Section: Introductionmentioning

confidence: 99%

Cloning, molecular characterization, and expression analysis of a nucleoporin gene (rgNUP98-96) from Rehmannia glutinosa

Yang¹,

Li²

2015

Genet. Mol. Res.

View full text Add to dashboard Cite

ABSTRACT. Nucleoporin 98 (NUP98) and nucleoporin 96 (NUP96) are essential components of the nuclear pore complex (NPC) in eukaryote cells. However, there is a lack of available information about complete Rehmannia glutinosa sequences. Here, the full-length cDNA sequence of rgNUP96-98 was isolated from R. glutinosa using rapid amplification of cDNA ends (RACE) technology, based on a cloned cDNA sequence (GenBank accession No. JZ483329). The identified rgNUP98-96 was 3476 bp, and it encoded a 1041-amino acid peptide. The BLAST search analysis of rgNUP98-96 showed an intermediate degree of similarity (60-79%) to the NUP98-96 protein sequences of 34 other plants, including the dicotyledons Erythranthe guttata, Genlisea aurea, Coffea canephora, Nicotiana benthamiana, Solanum lycopersicum, and Solanum tuberosum. The phylogenetic analysis of NUP96-98 sequences indicated that R. glutinosa and E. guttata sequences shared the closest homology. The calculated molecular mass and predicted isolectric point of the complex protein were 117.6 kDa and 4.99, respectively. The secondary and threedimensional structure studies illustrated that the rgNUP96-98 protein folded into a channel motif comprised of 34 alpha-helices, nine beta-strands, and (2015) several long loops. Using quantitative real-time PCR, the spatio-temporal expression patterns of rgNUP98-96 were analyzed in R. glutinosa, and the results indicated that rgNUP98-96 was highly expressed at the early stage of R. glutinosa tuberous root expansion, which is associated with a higher expression pattern in roots. The study provides a valuable foundation for further investigation of rgNUP96-98 molecular functions in R. glutinosa.

show abstract

You are who your friends are—nuclear pore proteins as components of chromatin‐binding complexes

Capelson

2023

FEBS Letters

View full text Add to dashboard Cite

Nuclear pore complexes (NPCs) are large multi‐component protein complexes that are embedded in the nuclear envelope, where they mediate nucleocytoplasmic transport. In addition to supporting transport, nuclear pore components, termed nucleoporins (Nups), can interact with chromatin and influence genome function. A subset of Nups can also localize to the nuclear interior and bind chromatin intranuclearly, providing an opportunity to investigate chromatin‐associated functions of Nups outside of the transport context. This review focuses on the gene regulatory functions of such intranuclear Nups, with a particular emphasis on their identity as components of several chromatin regulatory complexes. Recent proteomic screens have identified Nups as interacting partners of active and repressive epigenetic machinery, architectural proteins, and DNA replication complexes, providing insight into molecular mechanisms via which Nups regulate gene expression programs. This review summarizes these interactions and discusses their potential functions in the broader framework of nuclear genome organization.

show abstract

Intranuclear dynamics of the Nup107-160 complex

Cited by 43 publications

References 59 publications

Evolution of a transcriptional regulator from a transmembrane nucleoporin

Evolution of a transcriptional regulator from a transmembrane nucleoporin

Cloning, molecular characterization, and expression analysis of a nucleoporin gene (rgNUP98-96) from Rehmannia glutinosa

You are who your friends are—nuclear pore proteins as components of chromatin‐binding complexes

Contact Info

Product

Resources

About