Proteomic and targeted analytical identification of BXDC1 and EBNA1BP2 as dynamic scaffold proteins in the nucleolus

Hirano, Yasuhiro; Ishii, Kiyonori; Kumeta, Masahiro; Horigome, Tsuneyoshi

doi:10.1111/j.1365-2443.2008.01262.x

Cited by 26 publications

(28 citation statements)

References 39 publications

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“…Three different types of proteomic analyses of the nuclear matrix, nucleolus and mitotic chromosomes revealed that actinin-4 was located within the nuclear matrix and in mitotic chromosomes, but was not found in the nucleolus (Andersen et al, 2002;Hirano et al, 2009;Ishii et al, 2008;Scherl et al, 2002;Uchiyama et al, 2005). These findings are consistent with our observation that )Western blot analysis demonstrating the knockdown efficiency of siRNA against UBF.…”

Section: Multifunctional Actinin-4 At Focal Adhesions and The Nucleussupporting

confidence: 82%

Molecular mechanisms underlying nucleocytoplasmic shuttling of actinin-4

Kumeta

Yoshimura

Harata

et al. 2010

Journal of Cell Science

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SummaryIn addition to its well-known role as a crosslinker of actin filaments at focal-adhesion sites, actinin-4 is known to be localized to the nucleus. In this study, we reveal the molecular mechanism underlying nuclear localization of actinin-4 and its novel interactions with transcriptional regulators. We found that actinin-4 is imported into the nucleus through the nuclear pore complex in an importinindependent manner and is exported by the chromosome region maintenance-1 (CRM1)-dependent pathway. Nuclear actinin-4 levels were significantly increased in the late G2 phase of the cell cycle and were decreased in the G1 phase, suggesting that active release from the actin cytoskeleton was responsible for increased nuclear actinin-4 in late G2. Nuclear actinin-4 was found to interact with the INO80 chromatin-remodeling complex. It also directs the expression of a subset of cell-cycle-related genes and interacts with the upstream-binding factor (UBF)-dependent rRNA transcriptional machinery in the M phase. These findings provide molecular mechanisms for both nucleocytoplasmic shuttling of proteins that do not contain a nuclear-localization signal and cell-cycle-dependent gene regulation that reflects morphological changes in the cytoskeleton.

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Section: Multifunctional Actinin-4 At Focal Adhesions and The Nucleussupporting

confidence: 82%

Molecular mechanisms underlying nucleocytoplasmic shuttling of actinin-4

Kumeta

Yoshimura

Harata

et al. 2010

Journal of Cell Science

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“…FRAP Analysis-FRAP analyses were performed as described previously with slight modifications (26). The mobility of GFPtagged LBR and its mutants was analyzed using a confocal microscope (LSM510META; Zeiss; operated by the built-in software) with a Plan-Neofluar 40ϫ NA 1.30 oil immersion lens.…”

Section: Methodsmentioning

confidence: 99%

Lamin B Receptor Recognizes Specific Modifications of Histone H4 in Heterochromatin Formation

Hirano

Hizume

Kimura

et al. 2012

Journal of Biological Chemistry

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100

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Background: LBR is an inner nuclear membrane protein that participates in heterochromatin organization. Results: LBR recognizes specific histone modifications and induces chromatin compaction and transcriptional repression. Conclusion: LBR tethers epigenetically marked chromatin to the NE to repress transcription. Significance: This finding provides an implication of how transcriptional activities are repressed beneath the NE.

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“…7; Ishii et al 2008;Hirano et al 2009). In this model, WD-repeat and DO proteins, and other proteins, act as a scaffold for macro-protein complexes, and the complexes act as modules comprising the structures of nuclear bodies and the inter-chromatin region.…”

Section: Dynamic Scaffold Modelmentioning

confidence: 97%

“…It was previously shown that the fluorescence recovery of GFPfused t-UTP sub-complex components, i.e., CIRH1A-GFP, GFP-WDR43, and UTP15-GFP, is very slow (Sato et al 2013), unlike that of typical nucleolar proteins, i.e., GFP-nucleoplasmin/B23 (Hirano et al 2009) and GFP-nucleolin (Chen and Huang 2001), in HeLa cells. It has been suggested from these and other results that these proteins form immobile and stable macromolecular structures in living cells independent of rRNA transcription and act as a part of the structural scaffold or core for the nucleolus in the FC or Cap region (Sato et al 2013).…”

Section: Dynamics Of Gfp-fused Human Wd-repeat Containing Ssu Processmentioning

confidence: 98%

“…In this model, WD-repeat and DO proteins, and other proteins, act as a scaffold for macro-protein complexes, and the complexes act as modules comprising the structures of nuclear bodies and the inter-chromatin region. We have shown previously that two nucleolar proteins, i.e., EBNABP2 and BXDC1, and three FC region proteins, i.e., CIRH1A, WDR43, and UTP15, are immobilized or move very slowly in HeLa cells (Hirano et al 2009;Sato et al 2013). In this study, we further showed the low mobility of GFPfused WD-repeat proteins of the SSU processome, i.e., PWP2-GFP, TBL3-GFP, GFP-UTP18, NOL10-GFP, and GFP-WDR46 (Fig.…”

Section: Dynamic Scaffold Modelmentioning

confidence: 99%

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Dynamics of WD-repeat containing proteins in SSU processome components

Wada

Sato

Araki

et al. 2014

Biochem. Cell Biol.

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Nine WD-repeat containing proteins in human SSU processome components have been found in a HeLa cell nuclear matrix fraction. In these proteins, t-UTP sub-complex components, i.e., CIRH1A, UTP15, and WDR43, were shown to be immobilized in the fibrillar centers of nucleoli in living cells. In this study, the dynamics of the remaining six proteins fused with green fluorescent protein (GFP), i.e., PWP2-GFP, TBL3-GFP, GFP-UTP18, GFP-NOL10, GFP-WDR46, and GFP-WDSOF1, were examined in living cells. The findings were as follows. (i) The majority of UTP-B sub-complex components, i.e., PWP2-GFP, TBL3-GFP, and GFP-UTP18, are localized to the dense fibrillar component and granular component regions in nucleoli; (ii) When rRNA transcription is suppressed, the majority of GFP-fused UTP-B sub-complex components are localized in the cap and body regions of nucleoli. (iii) The mobility of these proteins except for GFP-WDSOF1, and half of GFP-UTP18 and GFP-WDR46, respectively, is very low in living cells. (iv) When rRNA transcription is suppressed, the mobility of these proteins except for GFP-WDSOF1 is accelerated but still slow. These findings and others suggest that these WD-repeat proteins other than GFP-WDSOF1 found in the nuclear matrix fraction bind tightly to some macro-protein complexes and act as a scaffold or a core for the complexes in nucleoli.

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Proteomic and targeted analytical identification of BXDC1 and EBNA1BP2 as dynamic scaffold proteins in the nucleolus

Cited by 26 publications

References 39 publications

Molecular mechanisms underlying nucleocytoplasmic shuttling of actinin-4

Molecular mechanisms underlying nucleocytoplasmic shuttling of actinin-4

Lamin B Receptor Recognizes Specific Modifications of Histone H4 in Heterochromatin Formation

Dynamics of WD-repeat containing proteins in SSU processome components

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