The discovery of a Werner helicase interacting protein (WHIP) association with the nuclear pore complex

Kaur, Simarna; White, Tommy E.; DiGuilio, Amanda L.; Glavy, Joseph S.

doi:10.4161/cc.9.15.12524

Cited by 12 publications

(12 citation statements)

References 55 publications

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“…Similar observations support the association of SET with Nup9840, for instance the fusion of Nup98 to NSD1 (another SET-containing histone methyltransferase)41. The Nup43-DHX15 helicase association found in uncharacterized proteins of multiple insect species, for instance Nasonia vitripennis (GI:345482402), is consistent with the presence of a Werner helicase interacting protein in the Y-complex42 and DDX10 in leukemia43, while it is also detected in Oct4 interactions along with Nup4331 and very strong correlations with multiple Y-Nups (Supplementary Table 3, Figure 4). Most importantly, the interaction of DEAD-box helicases with other nucleoporins, for instance Ddx19 with Nup159, has been reported at the molecular level44.…”

Section: Resultssupporting

confidence: 74%

Functional Genomics Evidence Unearths New Moonlighting Roles of Outer Ring Coat Nucleoporins

Katsani

Irimia

Karapiperis

et al. 2014

Sci Rep

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There is growing evidence for the involvement of Y-complex nucleoporins (Y-Nups) in cellular processes beyond the inner core of nuclear pores of eukaryotes. To comprehensively assess the range of possible functions of Y-Nups, we delimit their structural and functional properties by high-specificity sequence profiles and tissue-specific expression patterns. Our analysis establishes the presence of Y-Nups across eukaryotes with novel composite domain architectures, supporting new moonlighting functions in DNA repair, RNA processing, signaling and mitotic control. Y-Nups associated with a select subset of the discovered domains are found to be under tight coordinated regulation across diverse human and mouse cell types and tissues, strongly implying that they function in conjunction with the nuclear pore. Collectively, our results unearth an expanded network of Y-Nup interactions, thus supporting the emerging view of the Y-complex as a dynamic protein assembly with diverse functional roles in the cell.

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Section: Resultssupporting

confidence: 74%

Functional Genomics Evidence Unearths New Moonlighting Roles of Outer Ring Coat Nucleoporins

Katsani

Irimia

Karapiperis

et al. 2014

Sci Rep

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“…Export factors play a key role in the transport of mRNPs across the nuclear pore complex (NPC) for translation in the cytoplasm (31,(84)(85)(86). It has been reported that WRN interacts with a subset of nuclear pore proteins (33,44,87) including NDC1, a transmembrane nucleoporin (44). Although the signi cance of these interactions is unknown, these ndings suggested that WRN may contribute to a process, such as mRNA export that involves transport through the nuclear pore.…”

Section: Discussionmentioning

confidence: 99%

WRN modulates translation by influencing mRNA export from the nucleus through its interaction with the export receptor NXF1 in HeLa cancer cell

Iglesias-Pedraz¹,

Jara²,

Felice³

et al. 2020

Preprint

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Background The Werner syndrome protein (WRN) belongs to the RecQ family of helicases and its loss of function results in the premature aging disease Werner syndrome (WS). We previously demonstrated that an early cellular change induced by WRN depletion is a posttranscriptional decrease in the levels of enzymes involved in metabolic pathways that control macromolecular synthesis and protect from oxidative stress. This metabolic shift is tolerated by normal cells but causes mitochondria dysfunction and acute oxidative stress in rapidly growing cancer cells, thereby suppressing their proliferation.Results To identify the mechanism underlying this metabolic shift, we examined global protein synthesis and mRNA nucleocytoplasmic distribution after WRN knockdown. We determined that WRN depletion in HeLa cells attenuates global protein synthesis without affecting the level of key components of the mRNA export machinery. We further observed that WRN depletion affects the nuclear export of mRNAs and demonstrated that WRN directly interacts with mRNA and the mRNA export receptor Nuclear Export Factor 1 (NXF1).Conclusions Our findings suggest that WRN influences the export of mRNAs from the nucleus through its interaction with the NXF1 export receptor thereby affecting cellular proteostasis. In summary, we identified a new partner and a novel function of WRN, which is especially important for the proliferation of cancer cells.

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“…Cells were synchronized by double thymidine and nocodazole block (Glavy et al 2007 ; Kaur et al 2010 ). A 2 mM concentration of thymidine was added to the medium for 18 h in which HeLa cells were grown in culture.…”

Section: Methodsmentioning

confidence: 99%

Cyto-3D-print to attach mitotic cells

Castroagudin¹,

Zhai²,

Zhi³

et al. 2015

Cytotechnology

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The Cyto-3D-print is an adapter that adds cytospin capability to a standard centrifuge. Like standard cytospinning, Cyto-3D-print increases the surface attachment of mitotic cells while giving a higher degree of adaptability to other slide chambers than available commercial devices. The use of Cyto-3D-print is cost effective, safe, and applicable to many slide designs. It is durable enough for repeated use and made of biodegradable materials for environment-friendly disposal.Electronic supplementary materialThe online version of this article (doi:10.1007/s10616-015-9917-2) contains supplementary material, which is available to authorized users.

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The discovery of a Werner helicase interacting protein (WHIP) association with the nuclear pore complex

Cited by 12 publications

References 55 publications

Functional Genomics Evidence Unearths New Moonlighting Roles of Outer Ring Coat Nucleoporins

Functional Genomics Evidence Unearths New Moonlighting Roles of Outer Ring Coat Nucleoporins

WRN modulates translation by influencing mRNA export from the nucleus through its interaction with the export receptor NXF1 in HeLa cancer cell

Cyto-3D-print to attach mitotic cells

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