A distinct vesicle population targets membranes and pore complexes to the nuclear envelope in Xenopus eggs.

Vigers, Guy; Lohka, Manfred J.

doi:10.1083/jcb.112.4.545

Cited by 148 publications

(99 citation statements)

References 44 publications

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“…Thus, nuclear envelope assembly required both LVs and HVs. These results agree well with those of Vigers and Lohka (1991).…”

Section: Discussionsupporting

confidence: 92%

“…The first step is the binding of vesicles with the chromatin, and the second step is the fusion of vesicles on the chromatin. Vigers and Lohka (1991) reported that nuclear envelope assembly in cell-free extracts requires two distinct vesicles, called NEP-A and NEP-B. They showed that only NEP-B binds to sperm chromatin, but nuclear envelope assembly requires these two vesicles.…”

Section: Two Distinct Vesicles Lvs and Hvs Are Required For Nuclearmentioning

confidence: 99%

“…They showed that only NEP-B binds to sperm chromatin, but nuclear envelope assembly requires these two vesicles. We prepared two kinds of vesicle fractions from cell-free extracts of Xenopus eggs by the method of Vigers and Lohka (1991) with slight modification (see Section 2). Then, whole membrane fraction (whole vesicles) that was diluted and overlaid with 1.45 M sucrose in elution buffer was rapidly separated into LVs and HVs by ultracentrifugation.…”

Section: Two Distinct Vesicles Lvs and Hvs Are Required For Nuclearmentioning

confidence: 99%

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The interaction of two classes of nuclear vesicles is induced by the dissociation of soluble proteins from one class of vesicles

Oke

Inoue

2003

Biology of the Cell

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The regulatory mechanism of fusion steps in nuclear envelope assembly was studied in vitro using cell-free extracts of Xenopus eggs. The nuclear envelope is formed only around the chromatin at the end of mitosis. Two kinds of vesicles are required for nuclear envelope assembly (J. Cell Biol. 112 (1991) 545). Light vesicles (LVs) have the chromatin-binding activity, but cannot fuse solely. On the other hand, heavy vesicles (HVs) neither bind to the chromatin nor LVs, but are needed for the fusion event. Therefore, the association of HVs with LVs that bind to the chromatin is required at a first step during the fusion of vesicles. We found that salt-treated HVs inhibited the binding of LVs to the chromatin. In addition, when salt-treated HVs were pretreated with the proteins in the residue of salt-treatment of HVs, LVs recovered the chromatin-binding activity. In contrast, salt-treatment of LVs did not influence the binding of LVs with chromatin. By using a fluorescence microscopy assay, we showed directly that salt-treated HVs associated with LVs or salt-treated LVs, but HVs did not. These results suggest that soluble mask proteins on HVs keep the two distinct vesicles separate. We propose that the dissociation of mask protein on HVs allows HVs to bind with LVs that are located on the chromatin, subsequently the fusion of each vesicle occurs and the nuclear envelope is formed.

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“…Thus, nuclear envelope assembly required both LVs and HVs. These results agree well with those of Vigers and Lohka (1991).…”

Section: Discussionsupporting

confidence: 92%

Section: Two Distinct Vesicles Lvs and Hvs Are Required For Nuclearmentioning

confidence: 99%

Section: Two Distinct Vesicles Lvs and Hvs Are Required For Nuclearmentioning

confidence: 99%

See 1 more Smart Citation

The interaction of two classes of nuclear vesicles is induced by the dissociation of soluble proteins from one class of vesicles

Oke

Inoue

2003

Biology of the Cell

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“…S1), consistent with the well-known fact that NE formation in vitro requires both soluble and membrane components of the egg (Vigers and Lohka, 1991;Goldberg et al, 1997;Gant and Wilson, 1997). The light membranes alone (labeled with DiOC 18 , green emitting) did not bind to chromatin and a nuclear membrane did not form (Fig.…”

Section: Introductionsupporting

confidence: 68%

Assembly of nuclear pore complexes mediated by major vault protein

Vollmar

Hacker

Zahedi

et al. 2009

Journal of Cell Science

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The experimental system Previously, we have noted that incubation of egg extract without addition of chromatin promoted the formation of flat membrane cisternae studded with pore complexes, termed annulate lamellae (AL) (Dabauvalle et al., 1991). In a subsequent study, we found that AL formation apparently depleted a specific type of membrane vesicles from the egg extract that were required for NPC assembly from the egg extract (Ewald et al., 1997). Once these pore-forming Supplementary material available online at

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“…Whether this is due to lateral diffusion within the membrane or to vesicle formation and fusion is an open question. In certain cases, extensively exemplified by Xenopus eggs, integral membrane proteins of the nuclear membrane are found in distinct vesicles (Vigers and Lohka, 1991;Buendia and Courvalin, 1997;Drummond et al, 1999). Indeed, recent reports suggest that there are multiple populations of specialized vesicles (Antonin et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Nuclear Envelope Breakdown Is Coordinated by Both Nup358/RanBP2 and Nup153, Two Nucleoporins with Zinc Finger Modules

Prunuske

Liu

Elgort

et al. 2006

MBoC

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When higher eukaryotic cells transition into mitosis, the nuclear envelope, nuclear pore complexes, and nuclear lamina are coordinately disassembled. The COPI coatomer complex, which plays a major role in membrane remodeling at the Golgi, has been implicated in the process of nuclear envelope breakdown and requires interactions at the nuclear pore complex for recruitment to this new site of action at mitosis. Nup153, a resident of the nuclear pore basket, was found to be involved in COPI recruitment, but the molecular nature of the interface between COPI and the nuclear pore has not been fully elucidated. To better understand what occurs at the nuclear pore at this juncture, we have probed the role of the nucleoporin Nup358/RanBP2. Nup358 contains a repetitive zinc finger domain with overall organization similar to a region within Nup153 that is critical to COPI association, yet inspection of these two zinc finger domains reveals features that also clearly distinguish them. Here, we found that the Nup358 zinc finger domain, but not a zinc finger domain from an unrelated protein, binds to COPI and dominantly inhibits progression of nuclear envelope breakdown in an assay that robustly recapitulates this process in vitro. Moreover, the Nup358 zinc finger domain interferes with COPI recruitment to the nuclear rim. Consistent with a role for this pore protein in coordinating nuclear envelope breakdown, Nup358-specific antibodies impair nuclear disassembly. Significantly, targeting either Nup153 or Nup358 for inhibition perturbs nuclear envelope breakdown, supporting a model in which these nucleoporins play nonredundant roles, perhaps contributing to COPI recruitment platforms on both the nuclear and cytoplasmic faces of the pore. We found that an individual zinc finger is the minimal interface for COPI association, although tandem zinc fingers are optimal. These results provide new information about the critical components of nuclear membrane remodeling and lay the foundation for a better understanding of how this process is regulated. INTRODUCTIONThe nuclear envelope creates a barrier that is critical to maintenance of the environment in the nucleus, specialized to support transcription and DNA replication. This double lipid membrane bilayer consists of an outer nuclear membrane, which is continuous with the endoplasmic reticulum (ER), and an inner nuclear membrane, which contains at least 78 different proteins, anchored via protein-protein interactions to the underlying nuclear lamina and chromatin . The nuclear envelope is perforated by nuclear pores, through which communication between the cytoplasm and nucleus occurs (Suntharalingam and Wente, 2003;Weis, 2003;Fahrenkrog et al., 2004;Pante, 2004). Despite the large size of the macromolecular nuclear pore complex (125 MDa in vertebrates), it is comprised of only ϳ30 different proteins, or nucleoporins (Nups), each present in multiple copies (Rout et al., 2000;Cronshaw et al., 2002). In metazoan cells, all these components-the lamina, nuclear pores, as well as the ...

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A distinct vesicle population targets membranes and pore complexes to the nuclear envelope in Xenopus eggs.

Cited by 148 publications

References 44 publications

The interaction of two classes of nuclear vesicles is induced by the dissociation of soluble proteins from one class of vesicles

The interaction of two classes of nuclear vesicles is induced by the dissociation of soluble proteins from one class of vesicles

Assembly of nuclear pore complexes mediated by major vault protein

Nuclear Envelope Breakdown Is Coordinated by Both Nup358/RanBP2 and Nup153, Two Nucleoporins with Zinc Finger Modules

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