Association between the nucleolus and the coiled body

Raška, Ivan; Ochs, Robert; Andrade, Luís Eduardo Coelho; Chan, Edward K. L.; Burlingame, Rufus W.; Peebles, Carol; Gruol, D.L.; Tan, Eng M.

doi:10.1016/1047-8477(90)90066-l

Cited by 166 publications

(152 citation statements)

References 18 publications

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“…Ultrastructural ImmunoGold cytochemistry only detected endogenous FLASH in the nucleus, where it was sometimes associated with the nucleolus but, much more strikingly, in bodies 200-800 nm in diameter (Fig. 1a), with the structure and staining characteristics of ''coiled bodies'' (18,19). Like coiled bodies, the FLASH-labeled structures were also devoid of detectable levels of DNA (Fig.…”

Section: Flash Has a Nuclear Localizationmentioning

confidence: 96%

FLASH is an essential component of Cajal bodies

Barcaroli

Dinsdale

Neale

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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Cajal bodies are small nuclear organelles with a number of nuclear functions. Here we show that FLICE-associated huge protein (FLASH), originally described as a component of the apoptosis signaling pathway, is mainly localized in Cajal bodies and is essential for their structure. Reduction in FLASH expression by short hairpin RNA results in disruption of the normal architecture of the Cajal body and relocalization of its components. Because the function of FLASH in the apoptosis receptor signaling pathway has been strongly questioned, we have now identified a clear function for this protein.coiled bodies ͉ nuclear organelles C ajal bodies (CBs) are small nuclear organelles described in vertebrate cells a century ago by Ramon y Cajal and which have since been observed in a variety of animal and plant nuclei. Many components of CBs are shared with the nucleolus, and CBs frequently localize to the nucleolar periphery or within the nucleoli (1-3). CBs disappear from prophase nuclei and reappear in late G 1 after resumption of transcription in the daughter nuclei (for review see refs. 1, 4, and 5). Although their function is still in part elusive, recent work suggests that they are involved in several nuclear functions, including modification of small nuclear RNAs and small nuclear ribonucleoproteins, important for spliceosome formation, and assembly of the three eukaryotic RNA polymerases (pol I, pol II, and pol III) with their respective transcription and processing factors that are then transported as multiprotein complexes to the sites of transcription (1). More recently CBs have been implicated in replication-dependent histone gene transcription and mRNA maturation (1, 6-10), and a subset of CBs is physically associated with histone gene clusters on chromosomes 1 and 6 (11). Here we identify FLASH (FLICEassociated huge protein) (12) as a new component of CBs and show that it is essential for their structure.FLASH was initially identified as a component of the apoptosis signaling complex known as the death-inducing signaling complex (12, 13), which is associated with caspase 8 in the death-inducing signaling complex and thus essential for caspase 8 activation. However, this role of FLASH has been questioned (14). More recently it has been shown that, in response to TNF␣, FLASH translocates to the nucleus and binds the glucocorticoid receptor-interacting protein (GRIP-1), inhibiting both its interaction with, and the transcriptional activity of, the glucocorticoid receptor (15, 16). Results FLASH Has a Nuclear Localization.Despite the presence of three nuclear localization signals FLASH was originally described as a cytoplasmic protein (12,17). Staining endogenous FLASH with four different anti-FLASH antibodies, however, showed that FLASH only localized to the nucleus with a clear punctate appearance (Fig. 5a, which is published as supporting information on the PNAS web site). The specificity of the antibodies used was confirmed by the disappearance of the staining after short hairpin RNA for FLASH (Fig. 4a). West...

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Section: Flash Has a Nuclear Localizationmentioning

confidence: 96%

FLASH is an essential component of Cajal bodies

Barcaroli

Dinsdale

Neale

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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“…3 The term "coilin" first appeared in a paper published a year earlier, in which Ivan Raska and his co-workers named the protein after coiled bodies and used anticoilin autoimmune sera to analyze the relationship between CBs and nucleoli. 4 Soon after human coilin was discovered, the Xenopus laevis homologue was identified and shown to specifically localize to sphere organelles within the germinal vesicles of X. laevis oocytes. 5 Matera and colleagues cloned mouse, rat and zebrafish coilin genes and revealed the conservation of N-and C-terminal regions across these species (Fig.…”

Section: Coilin Historymentioning

confidence: 99%

“…sequence, 12 which might explain coilin's affinity toward the nucleolus, which was noticed already 25 years ago. 4 The conserved C-terminal domain folds into a Tudor domain like structure. 13 Several Tudor domains were found to bind methylated amino acids but direct tests did not show any interaction of coilin Tudor domain with monomethyl-lysine, trimethyl-lysine and dimethyl-arginine.…”

Section: Coilin Historymentioning

confidence: 99%

Coilin: The first 25 years

2015

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“…3 However, it was not until the 1990s that a molecular characterization of Cajal bodies began. [4][5][6][7] Since that time, the number of known cellular components that are enriched in the Cajal body has been growing. 3,[8][9][10] These components include factors important for the maturation and function of Sm-class small nuclear ribonucleoproteins (snRNPs), core particles of the spliceosome.…”

Section: Cajal Bodies and Their Componentsmentioning

confidence: 99%

SMN - A chaperone for nuclear RNP social occasions?

2016

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Survival Motor Neuron (SMN) protein localizes to both the nucleus and the cytoplasm. Cytoplasmic SMN is diffusely localized in large oligomeric complexes with core member proteins, called Gemins. Biochemical and cell biological studies have demonstrated that the SMN complex is required for the cytoplasmic assembly and nuclear transport of Sm-class ribonucleoproteins (RNPs). Nuclear SMN accumulates with spliceosomal small nuclear (sn)RNPs in Cajal bodies, sub-domains involved in multiple facets of snRNP maturation. Thus, the SMN complex forms stable associations with both nuclear and cytoplasmic snRNPs, and plays a critical role in their biogenesis. In this review, we focus on potential functions of the nuclear SMN complex, with particular emphasis on its role within the Cajal body.

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Association between the nucleolus and the coiled body

Cited by 166 publications

References 18 publications

FLASH is an essential component of Cajal bodies

FLASH is an essential component of Cajal bodies

Coilin: The first 25 years

SMN - A chaperone for nuclear RNP social occasions?

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