The nucleolus: a model for the organization of nuclear functions

Hernandez‐Verdun, Danièle

doi:10.1007/s00418-006-0212-3

Cited by 125 publications

(101 citation statements)

References 114 publications

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“…The nucleolus needs a large amount of energy to maintain ribosomal biogenesis and the dynamic property of nucleolar organization, such as the continuous inflow and outflow of proteins. It has been well established that the nucleolus is reorganized by transcriptional inhibition (8,24). Our FCS results combined with our CLSM and TEM observations demonstrate that this reorganized nucleolar domain is not in an aggregated state but rather that the molecules can still remain accessible and highly mobile.…”

Section: Discussionsupporting

confidence: 61%

“…On the basis of studies by transmission electron microscopy (TEM) and live cell imaging, it is well known that the morphology or ultra-structure of the nucleolus is dramatically changed by transcriptional inhibition using ActD (8,13,23,24,35). Recently, the combination of mass spectroscopic analyses with fluorescence measurement was conducted to examine the temporal nucleolar dynamics and the effect of ActD on structure of the nucleolus (4,25).…”

Section: Molecular Accessibility and Mobility Of Gfp N And Gfp-la Insmentioning

confidence: 99%

“…The D values of the probe molecules in the nucleoplasm and the nucleolus, which was marked by fibrillarin tagged with red fluorescent protein (RFP), were compared under different physiologic conditions. Because it is well known that the size and morphology of the nucleolus is sensitive to transcriptional inhibition by actinomycin D (ActD) (8,(23)(24)(25), nucleoli of live HeLa cells before and after ActD treatment were first observed by confocal laser scanning microscopy (CLSM) and electron microscopy, and then the statues of the nucleoplasm and nucleolus were characterized by FCS. Furthermore, the effect of ATP depletion on the molecular state inside the nucleolus was examined by the methods used above.…”

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confidence: 99%

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Dynamic and unique nucleolar microenvironment revealed by fluorescence correlation spectroscopy

Park¹,

Han²,

Sako³

et al. 2014

FASEB j.

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Organization and functions of the nucleolus is maintained by mobilities and interactions of nucleolar factors. Because the nucleolus is a densely packed structure, molecular crowding effects determined by the molecular concentrations and mobilities in the nucleolus should also be important for regulating nucleolar organization and functions. However, such molecular property of nucleolar organization is not fully understood. To understand the biophysical property of nucleolar organization, the diffusional behaviors of inert green fluorescent protein (GFP) oligomers with or without nuclear localization signals (NLSs) were analyzed under various conditions by fluorescence correlation spectroscopy. Our result demonstrates that the mobility of GFPs inside the nucleolus and the nucleoplasm can be represented by single free diffusion under normal conditions, even though the mobility in the nucleolus is considerably slower than that in the chromatin region. Moreover, the free diffusion of GFPs is found to be significantly size-and NLS-dependent only in the nucleolus. Interestingly, the mobility in the nucleolus is highly sensitive to ATP depletion, as well as actinomycin D (ActD) treatment. In contrast, the ultra-structure of the nucleolus was not significantly changed by ATP depletion but was changed by ActD treatment. These results suggest that the nucleolus behaves similarly to an open aqueous-phase medium with an increased molecular crowding effect that depends on both energy and transcription.-Park, H., Han, S.-S., Sako, Y., Pack, C.-G. Dynamic and unique nucleolar microenvironment revealed by fluorescence correlation spectroscopy. FASEB J. 29, 837-848 (2015). www.fasebj.org

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Section: Discussionsupporting

confidence: 61%

Section: Molecular Accessibility and Mobility Of Gfp N And Gfp-la Insmentioning

confidence: 99%

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confidence: 99%

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Dynamic and unique nucleolar microenvironment revealed by fluorescence correlation spectroscopy

Park¹,

Han²,

Sako³

et al. 2014

FASEB j.

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“…They include transcription of ribosomal genes (rDNA), processing and modifications of precursor ribosomal RNAs (pre-rRNAs) and assembly with ribosomal proteins. 4 The nucleolar organization in three compartments, fibrillar center (FC), dense fibrillar component (DFC) and granular component (GC) reflects the vectorial progression of ribosome biogenesis from DFC (early processing) to GC (late processing), and it is impaired by blockage at any step of the process. [5][6][7] The nucleolus…”

Section: Introductionmentioning

confidence: 99%

“…Late cleavage-processing steps and assembly of the large ribosome subunits generate the GC. 4,7 The nucleolar organization is modified by inhibition of rDNA transcription producing the typical segregated organization. 30,45,46 It was also demonstrated that the caseine kinase 2 (CK2) inhibitor DRB and the cyclin-dependent kinase (CDK) inhibitor roscovitine disrupt the link between DFC and GC.…”

mentioning

confidence: 99%

The traffic of proteins between nucleolar organizer regions and prenucleolar bodies governs the assembly of the nucleolus at exit of mitosis

Muro¹,

Gébrane-Younès²,

Jobart-Malfait³

et al. 2010

Nucleus

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is also a plurifunctional domain involved in assembly of RNPs and a target for viral proteins and viral RNAs. [8][9][10][11] The assembly of the nucleolus starts during telophase by activation of rDNA transcription of several nucleolar organizer regions (NORs) and by progressive recruitment of early and late processing proteins on rRNA transcripts. In parallel, prenucleolar bodies (PNBs) are assembled. [12][13][14][15][16] The PNBs contain nucleolar processing proteins, pre-rRNAs and snoRNAs. 17 Even though PNBs are formed in all animal and plant cells, their role in the dynamics of DFC and GC assembly is still unknown.It is possible to observe and measure the motion of proteins or RNP complexes in living cells. Using these approaches it was demonstrated that macromolecules within the nucleus are highly mobile by a combination of passive diffusion and highaffinity binding sites. [18][19][20] It was also established that the assembly of nuclear bodies after mitosis is strictly ordered. 14,[21][22][23][24] It is now important to characterize the dynamics of the complexes during the building of the functional domains integrated in the nuclear network. We examined the role of the PNB step in the kinetics of DFC and GC assembly. Using photoactivation, 25 weThe building of nuclear bodies after mitosis is a coordinated event crucial for nuclear organization and function. The nucleolus is assembled during early G 1 phase. Here, two periods (early G1a and early G1b) have been defined. During these periods, the nucleolar compartments (DFC, GC) corresponding to different steps of ribosome biogenesis are progressively assembled. In telophase, rDNA transcription is first activated and PNBs (reservoirs of nucleolar processing proteins) are formed. The traffic of the processing proteins between incipient nucleoli and PNBs was analyzed using photoactivation. We demonstrate that the DFC protein fibrillarin passes from one incipient nucleolus to other nucleoli but not to PNBs, and that the GC proteins, B23/NPM and Nop52, shuttle between PNBs and incipient nucleoli. This difference in traffic suggests a way of regulating assembly first of DFC and then of GC. The time of residency of GC proteins is high in incipient nucleoli compared to interphase nuclei, it decreases in LMB-treated early G1a cells impairing the assembly of GC. Because the assembly of the nucleolus and that of the Cajal body at the exit from mitosis are both sensitive to CRM1 activity, we discuss the fact that assembly of GC and/or its interaction with DFC in early G1a depends on shuttling between PNBs and NORs in a manner dependent on Cajal body assembly.www.landesbioscience.comNucleus 203 RESEARCH PAPER decreases as expected of proteins trafficking between nucleolus and nucleoplasm. Surprisingly, activated PAGFP-B23/NPM is detected in PNBs 5-10 seconds after activation (Fig. 1D). The uptake of B23/NPM in PNBs is observed in all PNBs containing mDsRed-Nop52 visible in the focal plane. This indicates that feedback of activated molecules occurs between incipient nuc...

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Nucleus, Ribosomes, the Golgi Complex, and Secretion

Cheville¹

2009

Ultrastructural Pathology the Comparative Cellular Basis of Disease

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The nucleolus: a model for the organization of nuclear functions

Cited by 125 publications

References 114 publications

Dynamic and unique nucleolar microenvironment revealed by fluorescence correlation spectroscopy

Dynamic and unique nucleolar microenvironment revealed by fluorescence correlation spectroscopy

The traffic of proteins between nucleolar organizer regions and prenucleolar bodies governs the assembly of the nucleolus at exit of mitosis

Nucleus, Ribosomes, the Golgi Complex, and Secretion

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