A New Model for Nuclear Envelope Breakdown

Terasaki, Mark; Campagnola, Paul J.; Rolls, Melissa M.; Stein, Pascal A.; Ellenberg, Jan; Hinkle, Beth; Slepchenko, Boris M.

doi:10.1091/mbc.12.2.503

Cited by 100 publications

(75 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Entry of 70-kDa dextran indicated that the size cut-off for passive permeability through nuclear pores had increased (Terasaki, 1994). Quantitative studies of dextran entry and time-lapse imaging of a nuclear pore GFP chimera support the idea that nuclear pore disassembly occurs during the period before nuclear envelope breakdown (Terasaki et al, 2001;Lénárt et al, 2003).…”

Section: Accumulation In the Nucleusmentioning

confidence: 59%

“…The constant entry rate is consistent with an active process; it can be contrasted with the passive entry of 10-kDa fluorescent dextran through nuclear pores, which follows an exponential decay because its movement is determined solely by the concentration gradient (Peters, 1984;Terasaki et al, 2001). The constant rate of entry of cyclin B-GFP lasted for several minutes.…”

Section: Accumulation In the Nucleusmentioning

confidence: 60%

“…Also in previous work, it was shown that there was a change in nuclear envelope permeability before nuclear envelope breakdown (Terasaki, 1994;Terasaki et al, 2001). To observe both of these processes together, cyclin B-GFP entry was imaged by confocal microscopy in parallel with entry of 70-kDa Rh dextran.…”

Section: Accumulation In the Nucleusmentioning

confidence: 98%

“…To demonstrate this clearly, cyclin B-GFP was imaged simultaneously with 70-kDa Rh dextran injected into the cytosol. We previously found two phases of 70-kDa dextran entry during maturation, a slow uniform increase throughout the GV beginning around 5 min before GVBD, and then a massive entry from one or two points at the time of GVBD corresponding to a disruption of the membrane permeability barrier of the nuclear envelope (Terasaki, 1994;Terasaki et al, 2001). .…”

mentioning

confidence: 99%

See 3 more Smart Citations

Localization and Dynamics of Cdc2-Cyclin B during Meiotic Reinitiation in Starfish Oocytes

Terasaki

Okumura

Hinkle

et al. 2003

MBoC

Self Cite

View full text Add to dashboard Cite

The Cdc2-cyclin B kinase has a central role in regulating the onset of M phase. In starfish oocytes, Cdc2-cyclin B begins to be activated ϳ10 min after application of maturation hormone, followed by accumulation in the nucleus then nuclear envelope breakdown. By immunofluorescence and by expressing a green fluorescent (GFP) chimera of cyclin B, we find that cyclin B is present in aggregates in the cytoplasm of immature oocytes. The aggregates disperse at ϳ10 min, suggesting that the dispersal is closely related to the activation of the kinase. Using cyclin B-GFP, the dispersion begins from the region containing the centrosomes. Extractability of Cdc2-cyclin B changes with similar kinetics during maturation. Active Cdc25 phosphatase released Cdc2-cyclin B from the detergent-insoluble fraction independently of its phosphatase activity. Live cell imaging also showed that Cdc2-cyclin B begins to accumulate in the nucleus before changes in nuclear pore permeability, consistent with Cdc2-cyclin B-induced disassembly of the pores. INTRODUCTIONThe Cdc2/cdk1 kinase triggers the onset of M phase (Nurse, 1990). Activation of Cdc2 requires association with cyclin B and dephosphorylation of Thr 14 and Tyr 15 on Cdc2; the phosphorylation state is governed by the relative activities of Wee1 family kinases and Cdc25 phosphatase (reviewed in Lew and Kornbluth, 1996). Inactive Cdc2-cyclin B is present in the cytoplasm during interphase and after it is activated, accumulates in the nucleus where it phosphorylates multiple targets to cause nuclear envelope breakdown (Pines and Hunter, 1991;Ookata et al., 1992).There are still many aspects of this system that are not well understood. The pathway leading to activation is different in different organisms and has not been established except in starfish (Okumura et al., 2002). Phosphorylation of cyclin is probably involved in the regulation of nuclear entry (Li et al., 1997;Hagting et al., 1998;Toyoshima et al., 1998;Yang et al., 1998) but may have other roles as well (Peter et al., 2002).Another subject of uncertainty regards Cdc2-cyclin B localization in the cytoplasm and its possible associations with other molecules in the cytoplasm. There are several indications that inactive Cdc2-cyclin B is not free to diffuse in the cytosol but instead, is associated with other molecules or intracellular structures and undergoes changes in associations when it becomes activated. Among various reports, Picard and Peaucellier (1998) observed cyclin B in vesiclelike structures in starfish oocytes, Westendorf et al. (1989) found evidence for cyclin B aggregates in immature clam oocytes, and Lee and Kirschner (1996) found evidence for a binding inhibitor of Cdc2-cyclin B that is associated with membranes. More recently, inactive Cdc2-cyclin B was found to be associated with annulate lamellae in immature Xenopus oocytes (Beckhelling et al., 2003).Current techniques for localization are subject to limitations of various kinds. The use of green fluorescent protein (GFP) chimeras is promising because loc...

show abstract

Section: Accumulation In the Nucleusmentioning

confidence: 59%

Section: Accumulation In the Nucleusmentioning

confidence: 60%

Section: Accumulation In the Nucleusmentioning

confidence: 98%

mentioning

confidence: 99%

See 2 more Smart Citations

Localization and Dynamics of Cdc2-Cyclin B during Meiotic Reinitiation in Starfish Oocytes

Terasaki

Okumura

Hinkle

et al. 2003

MBoC

Self Cite

View full text Add to dashboard Cite

show abstract

“…The idea has received support from subcellular 'fractionation' studies. But direct visualization of mitotic cells expressing fluorescent envelope proteins has shown that these proteins move freely throughout a single, continuous endoplasmic reticulum (ER) membrane system, with no evidence of vesicular intermediates 5,6 . These results have led to an alternative model that involves release and diffusion of envelope proteins and lipids into the ER, probably as a result of phosphorylation events, which abolish protein interactions essential for nuclear-envelope integrity.…”

mentioning

confidence: 99%

Ripping up the nuclear envelope

Lippincott‐Schwartz

2002

Nature

View full text Add to dashboard Cite

Breaking and making of the nuclear envelope

et al. 2005

View full text Add to dashboard Cite

During mitosis, a single nucleus gives rise to two nuclei that are identical to the parent nucleus. Mitosis consists of a continuous sequence of events that must be carried out once and only once. Two such important events are the disassembly of the nuclear envelope (NE) during the first stages of mitosis, and its accurate reassembly during the last stages of mitosis. NE breakdown (NEBD) is initiated when maturation-promoting factor (MPF) enters the nucleus and starts phosphorylating nuclear pore complexes (NPCs) and nuclear lamina proteins, followed by NPC and lamina breakdown. Nuclear reassembly starts when nuclear membranes assemble onto the chromatin. This article focuses on the different models of NEBD and reassembly with emphasis on recent data.

show abstract

A New Model for Nuclear Envelope Breakdown

Cited by 100 publications

References 28 publications

Localization and Dynamics of Cdc2-Cyclin B during Meiotic Reinitiation in Starfish Oocytes

Localization and Dynamics of Cdc2-Cyclin B during Meiotic Reinitiation in Starfish Oocytes

Ripping up the nuclear envelope

Breaking and making of the nuclear envelope

Contact Info

Product

Resources

About