Data on the association of the nuclear envelope protein Sun1 with nucleoli

Moujaber, Ossama; Omran, Nawal; Kodiha, Mohamed; Pié, Brigitte; Cooper, Ellis; Presley, John F.; Stochaj, Ursula

doi:10.1016/j.dib.2017.05.028

Cited by 4 publications

(5 citation statements)

References 21 publications

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“…Indeed, the LINC complex plays roles in mobilization of damaged telomeres and IR-induced DSBs in mouse cells (Lottersberger et al 2015) and also contributes to DSBs clustering in human nuclei (Aymard et al 2017). Interestingly, SUN1, a subunit of the LINC complex localizing to the NE, was also reported recently to be present in nucleoli (Matsumoto et al 2016;Moujaber et al 2017). In agreement, we could indeed confirm that SUN1 forms patches close to RNA Pol I (Supplemental Fig.…”

Section: Transcriptional Repression Requires Hush-mediated H3k9me3 Desupporting

confidence: 87%

A cohesin/HUSH- and LINC-dependent pathway controls ribosomal DNA double-strand break repair

Marnef¹,

Finoux²,

Arnould³

et al. 2019

Genes Dev.

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The ribosomal DNA (rDNA) represents a particularly unstable locus undergoing frequent breakage. DNA doublestrand breaks (DSBs) within rDNA induce both rDNA transcriptional repression and nucleolar segregation, but the link between the two events remains unclear. Here we found that DSBs induced on rDNA trigger transcriptional repression in a cohesin-and HUSH (human silencing hub) complex-dependent manner throughout the cell cycle. In S/G2 cells, transcriptional repression is further followed by extended resection within the interior of the nucleolus, DSB mobilization at the nucleolar periphery within nucleolar caps, and repair by homologous recombination. We showed that nuclear envelope invaginations frequently connect the nucleolus and that rDNA DSB mobilization, but not transcriptional repression, involves the nuclear envelope-associated LINC complex and the actin pathway. Altogether, our data indicate that rDNA break localization at the nucleolar periphery is not a direct consequence of transcriptional repression but rather is an active process that shares features with the mobilization of persistent DSB in active genes and heterochromatin.

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Section: Transcriptional Repression Requires Hush-mediated H3k9me3 Desupporting

confidence: 87%

A cohesin/HUSH- and LINC-dependent pathway controls ribosomal DNA double-strand break repair

Marnef¹,

Finoux²,

Arnould³

et al. 2019

Genes Dev.

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“…A representative image from three independent experiments is shown. As previously reported, multiple bands were detected for endogenous SUN1 protein (Göb et al, 2011 ; Moujaber et al, 2017 ).…”

Section: Resultssupporting

confidence: 72%

Age‐associated reduction of nuclear shape dynamics in excitatory neurons of the visual cortex

Frey,

Murakami,

Maki

et al. 2023

Aging Cell

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Neurons decline in their functionality over time, and age‐related neuronal alterations are associated with phenotypes of neurodegenerative diseases. In nonneural tissues, an infolded nuclear shape has been proposed as a hallmark of aged cells and neurons with infolded nuclei have also been reported to be associated with neuronal activity. Here, we performed time‐lapse imaging in the visual cortex of Nex‐Cre;SUN1‐GFP mice. Nuclear infolding was observed within 10 min of stimulation in young nuclei, while the aged nuclei were already infolded pre‐stimulation and showed reduced dynamics of the morphology. In young nuclei, the depletion of the stimuli restored the nucleus to a spherical shape and reduced the dynamic behavior, suggesting that nuclear infolding is a reversible process. We also found the aged nucleus to be stiffer than the young one, further relating to the age‐associated loss of nuclear shape dynamics. We reveal temporal changes in the nuclear shape upon external stimulation and observe that these morphological dynamics decrease with age.

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“…The human SUN1 gene generates various splicing variants including SUN1_916 and SUN1_888 (Göb et al, 2011; Nishioka et al, 2016; Figure 1a). SUN1 contributes to the maintenance of nucleolar morphology (Matsumoto et al, 2016; Moujaber et al, 2017); however, the role(s) of SUN1 splicing variants in determining nucleolar morphology remain elusive. To reveal the specific functions of the SUN1 splicing variants in nucleolar morphology, we used hTERT‐RPE1 cells, which have a chromosomally stable diploid karyotype and predominantly express SUN1_916 and SUN1_888 (Nishioka et al, 2016).…”

Section: Resultsmentioning

confidence: 99%

“…We previously reported that the depletion of SUN1 but not SUN2 affects nucleolar morphologies using unbiased morphological quantitation strategies (Matsumoto et al, 2016). Others have also proposed the association between the nucleolus and SUN1 (Moujaber et al, 2017). SUN1‐binding partner, nesprins, has been found to comprise a diverse spectrum of tissue‐specific isoforms that has distinct functions (Rajgor & Shanahan, 2013).…”

Section: Introductionmentioning

confidence: 99%

The SUN1 splicing variants SUN1_888 and SUN1_916 differentially regulate nucleolar structure

et al. 2020

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The nucleolar structure is highly dynamic and strictly regulated in response to internal cues, such as metabolic rates, and to external cues, such as mechanical forces applied to cells. Although the multilayered nucleolar structure is largely determined by the liquid‐like properties of RNA and proteins, the mechanisms regulating the morphology and number of nucleoli remain elusive. The linker of the nucleoskeleton and cytoskeleton (LINC) complex comprises inner nuclear membrane Sad1/UNC‐84 (SUN) proteins and outer nuclear membrane‐localized nesprins. We previously showed that the depletion of SUN1 proteins affects nucleolar morphologies. This study focuses on the function of SUN1 splicing variants in determining nucleolar morphology. An RNA interference strategy showed that the predominantly expressed variants, SUN1_888 and SUN1_916, were crucial for nucleolar morphology but functionally distinct. In addition, the depletion of either SUN1_888 or SUN1_916 altered the chromatin structure and affected the distribution of histone modifications. Based on these results, we propose a model in which the LINC complex plays a role in modulating nucleolar morphology and numbers via chromatin.

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Data on the association of the nuclear envelope protein Sun1 with nucleoli

Cited by 4 publications

References 21 publications

A cohesin/HUSH- and LINC-dependent pathway controls ribosomal DNA double-strand break repair

A cohesin/HUSH- and LINC-dependent pathway controls ribosomal DNA double-strand break repair

Age‐associated reduction of nuclear shape dynamics in excitatory neurons of the visual cortex

The SUN1 splicing variants SUN1_888 and SUN1_916 differentially regulate nucleolar structure

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