Sorting out the nuclear envelope from the endoplasmic reticulum.

Mattaj IW

doi:10.1038/nrm1263

Abstract

Although the interphase nuclear envelope is continuous with the endoplasmic reticulum, it is distinct from the endoplasmic reticulum in both form and composition. In metazoans, the nuclear envelope breaks down during mitosis and is thought to be completely reabsorbed by the endoplasmic reticulum. How these near neighbours are sorted out at the end of mitosis is an interesting mystery.

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References

Articles referenced by this article (34)

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Sorting out the nuclear envelope from the endoplasmic reticulum.

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Authors

ORCIDs linked to this article

Abstract

Full text links

References

Foisner, R. Inner nuclear membrane proteins and the nuclear lamina. J. Cell Sci. 114, 3791–3792 (2001).

Inner nuclear membrane proteins: functions and targeting.

Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells.

Integral membrane proteins of the nuclear envelope are dispersed throughout the endoplasmic reticulum during mitosis.

Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosis.

Structural organization of the endoplasmic reticulum.

Membrane domains in the secretory and endocytic pathways.

Assembly of the nuclear pore: biochemically distinct steps revealed with NEM, GTP gamma S, and BAPTA.

Removal of a single pore subcomplex results in vertebrate nuclei devoid of nuclear pores.

The conserved Nup107-160 complex is critical for nuclear pore complex assembly.

Citations & impact

Impact metrics

Citations of article over time

Smart citations by scite.ai
Explore citation contexts and check if this article has been supported or disputed.
https://scite.ai/reports/10.1038/nrm1263

Article citations

Melatonin: Regulation of Biomolecular Condensates in Neurodegenerative Disorders.

The Diverse Cellular Functions of Inner Nuclear Membrane Proteins.

Regulation and Physiological Significance of the Nuclear Shape in Plants.

Correlating nuclear morphology and external force with combined atomic force microscopy and light sheet imaging separates roles of chromatin and lamin A/C in nuclear mechanics.

Dynein pulling forces counteract lamin-mediated nuclear stability during nuclear envelope repair.

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Search life-sciences literature (45,104,206 articles, preprints and more)

Sorting out the nuclear envelope from the endoplasmic reticulum.

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Foisner, R. Inner nuclear membrane proteins and the nuclear lamina. J. Cell Sci. 114, 3791–3792 (2001).

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