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© The Rockefeller University Press, 0021-9525/1997//531 $5.00
The Journal of Cell Biology, Volume 136, Number 3, , 1997 531-544

Article

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



Mark Fricker*, Michael Hollinshead{ddagger}, Nick White*, and David Vaux{ddagger}

* Department of Plant Sciences and {ddagger} Sir William Dunn School of Pathology, Oxford, OX1 3RE, United Kingdom

The nuclear envelope consists of a doublemembraned extension of the rough endoplasmic reticulum. In this report we describe long, dynamic tubular channels, derived from the nuclear envelope, that extend deep into the nucleoplasm. These channels show cell-type specific morphologies ranging from single short stubs to multiple, complex, branched structures. Some channels transect the nucleus entirely, opening at two separate points on the nuclear surface, while others terminate at or close to nucleoli. These channels are distinct from other topological features of the nuclear envelope, such as lobes or folds.

The channel wall consists of two membranes continuous with the nuclear envelope, studded with features indistinguishable from nuclear pore complexes, and decorated on the nucleoplasmic surface with lamins. The enclosed core is continuous with the cytoplasm, and the lumenal space between the membranes contains soluble ER-resident proteins (protein disulphide isomerase and glucose-6-phosphatase).

Nuclear channels are also found in live cells labeled with the lipophilic dye DiOC6. Time-lapse imaging of DiOC6-labeled cells shows that the channels undergo changes in morphology and spatial distribution within the interphase nucleus on a timescale of minutes.

The presence of a cytoplasmic core and nuclear pore complexes in the channel walls suggests a possible role for these structures in nucleo–cytoplasmic transport. The clear association of a subset of these structures with nucleoli would also be consistent with such a transport role.

Abbreviations used in this paper: CLSM, confocal laser scanning fluorescent microscopy; G-6-Pase, glucose-6-phosphatase; NPC, nuclear pore complex; PDI, protein disulphide isomerase; TEM, transmission electron microscopy, 3-D, three-dimensional.

The work was partially funded by grants from the Medical Research Council (to D. Vaux) and a major equipment grant from the Wellcome Trust (to D. Vaux). N.S. White is a Royal Society Industry Fellow.

Please address all correspondence to David Vaux, Sir William Dunn School of Pathology, South Parks Road, Oxford, OX1 3 RE, United Kingdom. Tel.: (44) 1865 275544. Fax: (44) 1865 275501. E-mail: VAUX @MOLBIOL.OX.AC.UK


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