A nucleolus-associated coiled body

Kinderman, Nancy B.; LaVelle, Arthur

doi:10.1007/bf01175568

Cited by 22 publications

(12 citation statements)

References 14 publications

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“…We prepared total protein extracts using Drosophila PARP1 mutant stock ubiquitously expressing PARP1-ECFP or PARPe-EGFP transgenic constructs. First, we found that PARP1-ECFP, as well as PARPe-EGFP, proteins always co-purify with Coilin, as well as Fibrillarin protein (Figure 1D), which has also been reported as a component of CBs [18]. Additional co-immunoprecipitation experiments with anti-Fibrillarin antibody confirmed the specificity of PARP1-Fibrillarin interaction (Figure S2A).…”

Section: Resultssupporting

confidence: 67%

“…Since PARP1 protein also controls transcription and nucleoli and since automodified PARP1 is targeted into CB, PARP1 could be an important link in this process. Moreover, CBs are often seen attached to the nucleolus and share many nucleolar protein components, such as protein Fibrillarin [18] and p80 protein coilin which is a common specific marker of CBs [19] that we have used in our experiments.…”

Section: Introductionmentioning

confidence: 99%

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Poly (ADP-Ribose) Polymerase 1 Is Required for Protein Localization to Cajal Body

2009

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Recently, the nuclear protein known as Poly (ADP-ribose) Polymerase1 (PARP1) was shown to play a key role in regulating transcription of a number of genes and controlling the nuclear sub-organelle nucleolus. PARP1 enzyme is known to catalyze the transfer of ADP-ribose to a variety of nuclear proteins. At present, however, while we do know that the main acceptor for pADPr in vivo is PARP1 protein itself, by PARP1 automodification, the significance of PARP1 automodification for in vivo processes is not clear. Therefore, we investigated the roles of PARP1 auto ADP-ribosylation in dynamic nuclear processes during development. Specifically, we discovered that PARP1 automodification is required for shuttling key proteins into Cajal body (CB) by protein non-covalent interaction with pADPr in vivo. We hypothesize that PARP1 protein shuttling follows a chain of events whereby, first, most unmodified PARP1 protein molecules bind to chromatin and accumulate in nucleoli, but then, second, upon automodification with poly(ADP-ribose), PARP1 interacts non-covalently with a number of nuclear proteins such that the resulting protein-pADPr complex dissociates from chromatin into CB.

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Section: Resultssupporting

confidence: 67%

Section: Introductionmentioning

confidence: 99%

Poly (ADP-Ribose) Polymerase 1 Is Required for Protein Localization to Cajal Body

2009

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“…The coiled body is formed of a group of dense, distinct elements referred to as "coils" (Fig. 3) in other cell types (Kinderman and LaVelle, 1976;Schultz, 1989) that show moderate to high affinity for heavy metal salts. The more electron-opaque coils are 13-49 nm wide (X = 32, SD = 9, n = 34) and up to 120 nm long.…”

Section: Coiled Bodymentioning

confidence: 99%

Ultrastructural study of the coiled body and a new inclusion, the “mykaryon”, in the nucleus of the adult rat sertoli cell

Schultz

1989

Anat. Rec.

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Random and serial thin sections of the nucleus in adult rat Sertoli cells were examined by electron microscopy. Besides the previously reported nucleoli and heterochromatin masses, the nuclei contain a coiled body and a new structure, the "mykaryon." The coiled body is 835 nm in maximum diameter. It is composed of distinct elements referred to as "coils." They are 32 nm wide on average and resemble the nucleolar pars fibrosa in their intense staining with heavy metal salts and their composition of narrow filaments. The coiled body is often close to a nucleolus, though no direct contact is established, and it sometimes exists at a distance from the nucleolus. The mykaryon is spherical, 460 nm in maximum diameter, and composed of a tridimensional network of 7-26 nm-wide electron-opaque "cords" separated by slightly thinner spaces. It has not been observed in the vicinity of a nucleolus. A literature survey showed no previous mention of a structure similar to the mykaryon. The coiled body and the mykaryon are interpreted as normal constituents of the Sertoli nucleus in the adult rat.

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“…Intranuclear granular inclusions are frequently associated with another inclusion body, which is round in shape and measures about 0.5 pm in diameter; the body is not bounded by a membrane and is composed of electron-opaque, irregularly arranged strands consisting of granular and filamentous elements and intervening material of low electron opacity . This nuclear inclusion may correspond to coiled bodies or similar structures called by different names which are described in nerve cells [Hardin et al, 1969;Grillo, 1970;Le Beux, 1971;Kinderman and LaVelle, 1976;HervLs et al, 1980;Lafarga et al, 1983a1, immature glial cells [Lafarga et al, 1983b1, and nonneuronal cells [Monneron and Bernhard, 19691. In cotton rat pinealocytes, coiled bodies are usually localized distant from the nucleolus.…”

Section: Resultsmentioning

confidence: 99%

Nuclear and Cytoplasmic Inclusion Bodies in Pinealocytes of the Cotton Rat, Sigmodon hispidus: An Electron Microscopic Study

Matsushima¹,

Sakai²,

Aida³

et al. 1984

Journal of Pineal Research

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Electron microscopic observations on pinealocytes of cotton rats (Sigmodon bispidus) killed in October revealed the presence of cytoplasmic inclusion bodies (CIBs) and two kinds of nuclear inclusions--coiled bodies and granular inclusion bodies. These inclusions were usually not bounded by a membrane. CIBs showed round or irregular profiles and consisted of granular and filamentous materials of moderate electron opacity intermingled with electron-lucent areas. Nuclear granular inclusions appeared as homogeneous or heterogeneous granules of variable electron opacity, which usually exhibited round profiles of variable diameters and consisted of granular and filamentous elements. Electron-opaque granules were observed in perinuclear spaces, dilated cisternae of rough endoplasmic reticulum, as well as in the central portion of CIBs. In CIBs containing granules, the peripheral region was composed of the moderately electron-opaque substance seen in usual CIBs, while the central core was occupied by a granular and filamentous substance and an intervening electron-lucent matrix. Since an electron-opaque granular substance in nuclei, perinuclear spaces, cisternae of rough endoplasmic reticulum, and the central portion of CIBs may occur concomitantly, the granules seen in these sites may be related. Coiled bodies were round in profile and were composed of electron-opaque strands consisting of granular and filamentous elements and intervening material of low electron opacity. This structure, frequently located in close proximity to the nuclear granular inclusions, may play a role in the formation of the intranuclear granules in cotton rat pinealocytes.

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A nucleolus-associated coiled body

Cited by 22 publications

References 14 publications

Poly (ADP-Ribose) Polymerase 1 Is Required for Protein Localization to Cajal Body

Poly (ADP-Ribose) Polymerase 1 Is Required for Protein Localization to Cajal Body

Ultrastructural study of the coiled body and a new inclusion, the “mykaryon”, in the nucleus of the adult rat sertoli cell

Nuclear and Cytoplasmic Inclusion Bodies in Pinealocytes of the Cotton Rat, Sigmodon hispidus: An Electron Microscopic Study

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