Dataset Information

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

ABSTRACT: SUN proteins participate in diverse cellular activities, many of which are connected to the nuclear envelope. Recently, the family member SUN1 has been linked to novel biological activities. These include the regulation of nucleoli, intranuclear compartments that assemble ribosomal subunits. We show that SUN1 associates with nucleoli in several mammalian epithelial cell lines. This nucleolar localization is not shared by all cell types, as SUN1 concentrates at the nuclear envelope in ganglionic neurons and non-neuronal satellite cells. Database analyses and Western blotting emphasize the complexity of SUN1 protein profiles in different mammalian cells. We constructed a STRING network which identifies SUN1-related proteins as part of a larger network that includes several nucleolar proteins. Taken together, the current data highlight the diversity of SUN1 proteins and emphasize the possible links between SUN1 and nucleoli.

SUBMITTER: Moujaber O

PROVIDER: S-EPMC5447391 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature

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

Moujaber Ossama O Omran Nawal N Kodiha Mohamed M Pié Brigitte B Cooper Ellis E Presley John F JF Stochaj Ursula U

Data in brief 20170519

SUN proteins participate in diverse cellular activities, many of which are connected to the nuclear envelope. Recently, the family member SUN1 has been linked to novel biological activities. These include the regulation of nucleoli, intranuclear compartments that assemble ribosomal subunits. We show that SUN1 associates with nucleoli in several mammalian epithelial cell lines. This nucleolar localization is not shared by all cell types, as SUN1 concentrates at the nuclear envelope in ganglionic ...[more]

PMID: 28580408

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Project description:BACKGROUND: DYT1 dystonia is an autosomal dominant neurological condition caused by a mutation that removes a single glutamic acid residue (?E) from the torsinA (torA) AAA+ protein. TorA appears to possess a nuclear envelope (NE) localized activity that requires Lamina-Associated-Polypeptide 1 (LAP1), which is an inner nuclear membrane localized torA-binding partner. Although hypoactive, the DYT1 dystonia torA-?E isoform often concentrates in the NE, suggesting that torA-?E also interacts with an NE-localized binding partner. RESULTS: We confirm that NE-localized torA-?E does not co-immunoprecipitate with LAP1, and find that torA-?E continues to concentrate in the NE of cells that lack LAP1. Instead, we find that variability in torA-?E localization correlates with the presence of the SUN-domain and Nesprin proteins that assemble into the LINC complex. We also find that siRNA depletion of SUN1, but not other LINC complex components, removes torA-?E from the NE. In contrast, the LAP1-dependent NE-accumulation of an ATP-locked torA mutant is unaffected by loss of LINC complex proteins. This SUN1 dependent torA-?E localization requires the torA membrane association domain, as well as a putative substrate-interaction residue, Y147, neither of which are required for torA interaction with LAP1. We also find that mutation of these motifs, or depletion of SUN1, decreases the amount of torA-WT that colocalizes with NE markers, indicating that each also underlies a normal NE-localized torA binding interaction. CONCLUSIONS: These data suggest that the disease causing ?E mutation promotes an association between torA and SUN1 that is distinct to the interaction between LAP1 and ATP-bound torA. This evidence for two NE-localized binding partners suggests that torA may act on multiple substrates and/or possesses regulatory co-factor partners. In addition, finding that the DYT1 mutation causes abnormal association with SUN1 implicates LINC complex dysfunction in DYT1 dystonia pathogenesis, and suggests a gain-of-function activity contributes to this dominantly inherited disease.

Dataset Information

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

Publications

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

Similar Datasets

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