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Remodelling the walls of the nucleus

Nature Reviews Molecular Cell Biology volume 3, pages 487–497 (2002)Cite this article

Abstract

The nuclear envelope (NE) acts as a selective barrier around the genome and as a scaffold to organize DNA in the nucleus. During cell division, the NE is broken down and chromosome confinement is taken over by microtubules. After chromosome segregation, a new NE is reassembled in each daughter cell. In this complex cycle of disassembly and reassembly, the fate of the NE is intimately linked to the activity of the mitotic spindle. The finding that components of the nuclear membrane become distributed throughout a continuous endoplasmic reticulum during mitosis indicates new mechanisms by which nuclear membrane domains are established, and highlights unique problems in the establishment of NE topology.

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Figure 1: Topology of the nuclear envelope.
Figure 2: Nuclear envelope, microtubules and chromosomes through the cell cycle.
Figure 3: Model of nuclear envelope breakdown in mammalian cells.
Figure 4: Different modes of nuclear pore assembly.
Figure 5: The sequence of events during nuclear envelope assembly.

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Acknowledgements

The authors would like to thank P. Lénárt for preparing the illustrations and K. Ribbeck for preparing Fig. 2.

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Authors and Affiliations

  1. Department of Anatomy and Cell Biology, The University of Florida, 32610, Florida, Gainesville, USA

    Brian Burke

  2. Gene Expression and Cell Biology/Biophysics Programmes, European Molecular Biology Laboratory, Heidelberg, D-69117, Germany

    Jan Ellenberg

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Correspondence to Brian Burke.

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DATABASES

Interpro

LEM domain

LocusLink

AKAP149

MAN1

RanBP2

<i>Saccharomyces</i> Genome Database

CDC48

Npl4

Ufd1

Swiss-Prot

cdc2

emerin

GFP

gp210

Nup98

Nup133

Nup153

p34cdc2

POM121

Ran

Glossary

LAMINS

Lamins are rod-shaped proteins of the intermediate filament class. They consist of a head and tail domain that flank a conserved α-helical rod domain. Lamins form parallel homo- and probably heterodimers which, in turn, can polymerize in a head-to-tail fashion. These linear polymers are thought to associate laterally into 10-nm lamin fibres, which form the fibrous lamina meshwork in the nuclear periphery.

INTERMEDIATE FILAMENT PROTEINS

Intermediate filaments are protein fibres with a diameter of ∼10 nm that represent the third class of cytoskeletal polymers, after microtubules and actin. Intermediate filaments can be subdivided into five classes. Classes I–IV are found in the cytoplasm and contain, for example, keratins, neurofilaments and vimentin. Class V is nuclear and is comprised exclusively of nuclear lamins.

METAZOANS

Organisms that consist of more than one cell.

CISTERNAE

Flat sheets of endoplasmic reticulum that enclose a lumen like a hollow pancake.

CENTROSOMES

The microtubule-organizing centres in animal cells.

NUCLEAR BASKET

A fishtrap-like structure on the nuclear side of the nuclear pore that is made up of eight fibrils joined by a distal ring.

FLUORESCENCE RECOVERY AFTER PHOTOBLEACHING

(FRAP). A technique in which a pool of fluorescent molecules is destroyed locally by high-intensity laser irradiation. After this 'photobleach', the exchange of the non-fluorescent molecules with the surrounding fluorescent molecules is monitored and measured as 'recovery' of fluorescence in the bleached area.

M-PHASE PROMOTING FACTOR

(MPF). The complex of a B-type cyclin and cyclin-dependent kinase 1, which is also referred to as cdc2 or p34, depending on the species. Only the complex of both proteins in a specific state of phosphorylation is active, and this is the main enzyme that is responsible for entry into M phase in both meiosis and mitosis.

FLUORESCENCE RESONANCE ENERGY TRANSFER

(FRET). A technique to measure the proximity of two fluorophores, a donor and an acceptor. If these are within 2–10 nm of each other and if the emission spectrum of the donor overlaps with the excitation spectrum of the acceptor, energy can be transferred non-radiatively from acceptor to donor by dipole–dipole coupling or 'resonance'. The efficiency of the transfer is extremely distance sensitive, so FRET is often referred to as a molecular ruler.

DYNEIN

A large, cytoplasmic microtubule-dependent motor protein that converts the energy of ATP into motion towards the minus end of microtubules.

DYNACTIN

A complex of several proteins that are associated with dynein, which links the motor to cargo and regulates its activity.

MINUS END

The slower growing end of microtubules.

ASTERS

Many microtubules that are nucleated from one point (such as a centrosome) in a radial manner.

AAA ATPASE

A family of enzymes that hydrolyse ATP and have a common ATPase module. They typically form ring-shaped oligomers and are involved in diverse cellular functions, such as membrane fusion (for example, p97 and NSF), DNA replication and proteolysis.

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Burke, B., Ellenberg, J. Remodelling the walls of the nucleus. Nat Rev Mol Cell Biol 3, 487–497 (2002). https://doi.org/10.1038/nrm860

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