Interphase Nuclei of Many Mammalian Cell Types Contain Deep, Dynamic, Tubular Membrane-bound Invaginations of the Nuclear Envelope

Fricker, Mark D.; Hollinshead, Michael; White, Nick; Vaux, David J.

doi:10.1083/jcb.136.3.531

Cited by 346 publications

(306 citation statements)

References 56 publications

(74 reference statements)

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“…Although such structures have been observed in a wide range of cell types (Fricker et al, 1997), they might not be universal (Bezin et al, 2008b). For reasons that are unknown, the structure of the nucleoplasmic reticulum seems to vary from being made up of simple solitary projections (Fig.…”

Section: The Nucleoplasmic Reticulummentioning

confidence: 99%

An update on nuclear calcium signalling

Bootman

Fearnley

Smyrnias

et al. 2009

Journal of Cell Science

189

194

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Over the past 15 years or so, numerous studies have sought to characterise how nuclear calcium (Ca 2+ ) signals are generated and reversed, and to understand how events that occur in the nucleoplasm influence cellular Ca 2+ activity, and vice versa. In this Commentary, we describe mechanisms of nuclear Ca 2+ signalling and discuss what is known about the origin and physiological significance of nuclear Ca 2+ transients. In particular, we focus on the idea that the nucleus has an autonomous Ca 2+ signalling system that can generate its own Ca 2+ transients that modulate processes such as gene transcription. We also discuss the role of nuclear pores and the nuclear envelope in controlling ion flux into the nucleoplasm. Journal of Cell Science 2338(which would cause its nuclear export) and through a physical interaction that occludes a nuclear-export sequence (NES) in the NFAT protein.An example of a nuclear-localised transcription factor that is regulated by both nuclear and cytosolic Ca 2+ signals is cyclic AMP response element-binding protein (CREB). The signalling mechanisms that underlie CREB activation have been worked out particularly well in neurons, in which it has been established that depolarisation leads to the rapid phosphorylation of CREB on Ser133 by Ca 2+ -calmodulin-dependent kinase IV, which provides a necessary, but not sufficient, signal for CREB-mediated gene transcription (Dolmetsch et al., 2001). The triggering event is an increase in cytosolic Ca 2+ levels in the immediate vicinity of L-type Ca 2+ channels or N-methyl-D-aspartate receptors that are found in the synapse, at a site that is distal to the nucleus (Shaywitz and Greenberg, 1999). As CREB is only found in the nucleus, the phosphorylation of Ser133 is mediated by one of several Ca 2+ -sensitive signal transduction cascades that convey information from the remote synapses into the nucleus. In the nucleus, phosphorylated CREB binds additional proteins to form a transcriptionally active complex (Shaywitz and Greenberg, 1999). Although the synaptic Ca 2+ signal does not need to propagate to the nucleus to induce phosphorylation of Ser133 on CREB, an increase in the level of nuclear Ca 2+ is required for CREB-mediated gene transcription to occur. This is because additional Ca 2+ -dependent phosphorylation of CREB and its co-activators is required (Chawla et al., 1998;Kornhauser et al., 2002). Indeed, nuclear injection of an artificial Ca 2+ buffer prevents CREB-mediated gene transcription, but not transcription induced by the serum-response element, which is sensitive to cytosolic Ca 2+ buffering (Hardingham et al., 1997).Another well-known target of nuclear Ca 2+ signalling is the transcriptional regulator downstream regulatory element antagonist modulator (DREAM). It is well established that DREAM represses the expression of prodynorphin, an opiate-receptor precursor, and that mice that lack DREAM have a constitutive analgesic condition (Cheng et al., 2002). DREAM contains four Ca 2+ -binding EF hands (a widely expressed structural mo...

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Section: The Nucleoplasmic Reticulummentioning

confidence: 99%

An update on nuclear calcium signalling

Bootman

Fearnley

Smyrnias

et al. 2009

Journal of Cell Science

189

194

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“…The grids were then washed in PBS and incubated for 20 min with a 1 Ϻ 100 dilution of 9-nm protein A-gold stock (Slot and Geuze 1985). After washing in PBS and water, the grids were embedded in methocellulose-uranyl acetate (Tokuyasu 1980) and examined in a Leo EM 912 transmission electron microscope (Fricker et al 1997). Images were collected at 80 keV using a Proscan 1024 ϫ 1024 pixel cooled CCD camera.…”

Section: Methodsmentioning

confidence: 99%

“…All fluorescently labeled specimens were examined using a BioRad MRC 1024 confocal laser scanning microscope as described (Fricker et al 1997). The data shown have been median-filtered with a 3 ϫ 3 box and stretched to fill the entire grayscale range.…”

Section: Methodsmentioning

confidence: 99%

Anti-biotin Antibodies Offer Superior Organelle-specific Labeling of Mitochondria over Avidin or Streptavidin

Hollinshead

Sanderson

Vaux

1997

J Histochem Cytochem.

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SUMMARYThe mitochondrial matrix contains endogenously biotinylated proteins. These proteins can cause unexpected background signal when biotin-avidin-or biotin-streptavidin-based detection systems are used in immunocytochemistry. Here we show that this reactivity can be deliberately exploited, using a simple anti-biotin reagent, to obtain strong and highly specific labeling of mitochondria by both light and electron microscopy. The signal is substantially stronger than when either avidin or streptavidin is used to detect the endogenous biotin. These results confirm the accessibility of protein-bound endogenous biotin to exogenous probes, and localize the biotinylated enzymes to the mitochondrial matrix. (J Histochem Cytochem 45:1053-1057, 1997)

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“…Error bars represent standard deviation. *, p Ͻ 0.05; **, p Ͻ 0.005. some invaginations of the nuclear membrane have been reported to come in close contact with the nucleolus (29). Furthermore, overexpression of the nucleolar protein Nopp140 induces the formation of intranuclear endoplasmic reticulum membranes (30).…”

Section: Age (B and D) A Hdhmentioning

confidence: 99%

Rrs1 Is Involved in Endoplasmic Reticulum Stress Response in Huntington Disease

Carnemolla

Fossale

Agostoni

et al. 2009

Journal of Biological Chemistry

147

135

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The induction of Rrs1 expression is one of the earliest events detected in a presymptomatic knock-in mouse model of Huntington disease (HD). Rrs1 up-regulation fulfills the HD criteria of dominance, striatal specificity, and polyglutamine dependence. Here we show that mammalian Rrs1 is localized both in the nucleolus as well as in the endoplasmic reticulum (ER) of neurons. This dual localization is shared with its newly identified molecular partner 3D3/lyric. We then show that both genes are induced by ER stress in neurons. Interestingly, we demonstrate that ER stress is an early event in a presymptomatic HD mouse model that persists throughout the life span of the rodent. We further show that ER stress also occurs in postmortem brains of HD patients.

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Interphase Nuclei of Many Mammalian Cell Types Contain Deep, Dynamic, Tubular Membrane-bound Invaginations of the Nuclear Envelope

Cited by 346 publications

References 56 publications

An update on nuclear calcium signalling

An update on nuclear calcium signalling

Anti-biotin Antibodies Offer Superior Organelle-specific Labeling of Mitochondria over Avidin or Streptavidin

Rrs1 Is Involved in Endoplasmic Reticulum Stress Response in Huntington Disease

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