Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo

Anderson, Daniel J.; Vargas, Jesse D.; Hsiao, Joshua P; Hetzer, Martin W.

doi:10.1083/jcb.200901106

Cited by 101 publications

(85 citation statements)

References 33 publications

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“…Although the NE disappears as an integral structure in metaphase, large areas of ER-sheets, derived from NE, still outline the shape of the NE (Figs. 3c, 4a) as shown by live cell imaging (Anderson et al 2009). The NE perforates at the regions facing the centrosomes (Figs.…”

Section: Discussionmentioning

confidence: 86%

“…Maximum compaction of the chromatin is reached in late anaphase (Mora-Bermúdez et al 2007), necessary for wrapping of the chromosomes by ER-sheets (Fig. 3d, e, g–h; Movie S2) as shown by LM (Anderson and Hetzer 2008; Anderson et al 2009; Lu et al 2009). The center of chromosome bulk is not covered completely due to the uneven chromosome topography and reduced accessibility for ER-sheets (Fig.…”

Section: Discussionmentioning

confidence: 97%

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Precise and economic FIB/SEM for CLEM: with 2 nm voxels through mitosis

Luckner

Wanner

2018

Histochem Cell Biol

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A portfolio is presented documenting economic, high-resolution correlative focused ion beam scanning electron microscopy (FIB/SEM) in routine, comprising: (i) the use of custom-labeled slides and coverslips, (ii) embedding of cells in thin, or ultra-thin resin layers for correlative light and electron microscopy (CLEM) and (iii) the claim to reach the highest resolution possible with FIB/SEM in xyz. Regions of interest (ROIs) defined in light microscope (LM), can be relocated quickly and precisely in SEM. As proof of principle, HeLa cells were investigated in 3D context at all stages of the cell cycle, documenting ultrastructural changes during mitosis: nuclear envelope breakdown and reassembly, Golgi degradation and reconstitution and the formation of the midzone and midbody.Electronic supplementary materialThe online version of this article (10.1007/s00418-018-1681-x) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 86%

Section: Discussionmentioning

confidence: 97%

Precise and economic FIB/SEM for CLEM: with 2 nm voxels through mitosis

Luckner

Wanner

2018

Histochem Cell Biol

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“…Most of the well-characterized NE transmembrane proteins reside at the INM and bind to lamins, including emerin, lamin B receptor (LBR), lamina associated polypeptide (LAP)1, LAP2 and MAN1 (Gruenbaum et al, 2005; Schirmer and Foisner, 2007). Some of these inner membrane proteins show preferential binding to different lamin isotypes, and appear to promote the membrane association of lamins (Anderson et al, 2009; Gruenbaum et al, 2005; Schirmer and Foisner, 2007). Furthermore, lamins and some lamina associated proteins bind to DNA and/or chromatin proteins (Fig.…”

Section: The Inscrutable Lamina Of Somatic Cellsmentioning

confidence: 99%

Nuclear lamina at the crossroads of the cytoplasm and nucleus

Gerace

Huber

2012

Journal of Structural Biology

106

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The nuclear lamina is a protein meshwork that lines the nuclear envelope in metazoan cells. It is composed largely of a polymeric assembly of lamins, which comprise a distinct sequence homology class of the intermediate filament protein family. On the basis of its structural properties, the lamina originally was proposed to provide scaffolding for the nuclear envelope and to promote anchoring of chromatin and nuclear pore complexes at the nuclear surface. This viewpoint has expanded greatly during the past 25 years, with a host of surprising new insights on lamina structure, molecular composition and functional attributes. It has been established that the self-assembly properties of lamins are very similar to those of cytoplasmic intermediate filament proteins, and that the lamin polymer is physically associated with components of the cytoplasmic cytoskeleton and with a multitude of chromatin and inner nuclear membrane proteins. Cumulative evidence points to an important role for the lamina in regulating signaling and gene activity, and in mechanically coupling the cytoplasmic cytoskeleton to the nucleus. The significance of the lamina has been vaulted to the forefront by the discovery that mutations in lamins and lamina-associated polypeptides lead to an array of human diseases. A key future challenge is to understand how the lamina integrates pathways for mechanics and signaling at the molecular level. Understanding the structure of the lamina from the atomic to supramolecular levels will be essential for achieving this goal.

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“…After mitosis, Man1, 24 and other INM proteins participate in nuclear assembly by re-associating with chromatin and facilitating the conversion of tubular ER into the sheet ER of the reforming the NE 3 , 21 , 23 …”

Section: Introductionmentioning

confidence: 99%

Fission yeast Lem2 and Man1 perform fundamental functions of the animal cell nuclear lamina

González

Saito

Sazer

2012

Nucleus

140

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In animal cells the nuclear lamina, which consists of lamins and lamin-associated proteins, serves several functions: it provides a structural scaffold for the nuclear envelope and tethers proteins and heterochromatin to the nuclear periphery. In yeast, proteins and large heterochromatic domains including telomeres are also peripherally localized, but there is no evidence that yeast have lamins or a fibrous nuclear envelope scaffold. Nonetheless, we found that the Lem2 and Man1 proteins of the fission yeast Schizosaccharomyces pombe, evolutionarily distant relatives of the Lap2/Emerin/Man1 (LEM) sub-family of animal cell lamin-associated proteins, perform fundamental functions of the animal cell lamina. These integral inner nuclear membrane localized proteins, with nuclear localized DNA binding Helix-Extension-Helix (HEH) domains, impact nuclear envelope structure and integrity, are essential for the enrichment of telomeres at the nuclear periphery and by means of their HEH domains anchor chromatin, most likely transcriptionally repressed heterochromatin, to the nuclear periphery. These data indicate that the core functions of the nuclear lamina are conserved between fungi and animal cells and can be performed in fission yeast, without lamins or other intermediate filament proteins.

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Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo

Cited by 101 publications

References 33 publications

Precise and economic FIB/SEM for CLEM: with 2 nm voxels through mitosis

Precise and economic FIB/SEM for CLEM: with 2 nm voxels through mitosis

Nuclear lamina at the crossroads of the cytoplasm and nucleus

Fission yeast Lem2 and Man1 perform fundamental functions of the animal cell nuclear lamina

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