Distribution of emerin during the cell cycle

Dabauvalle, Marie-Christine; Müller, Elvira; Ewald, Andrea; Kreß, Wolfram; Krohne, Georg; Müller, C. R.

doi:10.1016/s0171-9335(99)80043-0

Cited by 45 publications

(29 citation statements)

References 44 publications

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“…in regions adjacent to mitotic spindle (Dabauvalle et al, 1999). The ER marker protein disulfide isomerase was also excluded from this membrane domain.…”

Section: Discussionmentioning

confidence: 99%

“…It has previously been shown that a fraction of the integral INM protein emerin localizes in the vicinity of centrosomes during mitosis (Dabauvalle et al, 1999). We therefore wanted to compare the localization of emerin and Samp1 in mitotic cells, to see whether they are part of the same structure in metaphase.…”

Section: Samp1 Displays An Unexpected Distribution To the Polar Areasmentioning

confidence: 99%

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An integral protein of the inner nuclear membrane localizes to the mitotic spindle in mammalian cells

Buch

Lindberg

Figueroa

et al. 2009

Journal of Cell Science

100

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Here, we characterize a transmembrane protein of the nuclear envelope that we name spindle-associated membrane protein 1 (Samp1). The protein is conserved in metazoa and fission yeast and is homologous to Net5 in rat and Ima1 in Schizosaccharomyces pombe. We show that, in human cells, the protein is a membrane-spanning polypeptide with an apparent molecular mass of 43 kDa. This is consistent with a predicted polypeptide of 392 amino acids that has five transmembrane segments and its C-terminus exposed to the nucleoplasm. During interphase, Samp1 was specifically distributed in the inner nuclear membrane. Post-transcriptional silencing of Samp1 expression resulted in separation of centrosomes from the nuclear envelope, indicating that it is functionally connected to the cytoskeleton. At the onset of mitosis, most of the protein dispersed out into the ER, as expected. However, during mitosis, a significant fraction of the protein specifically localized to the polar regions of the mitotic spindle. We demonstrate for the first time, in human cells, the existence of a membranous structure overlapping with the mitotic spindle. Interestingly, another integral inner nuclear membrane protein, emerin, was absent from the spindle-associated membranes. Thus, Samp1 defines a specific membrane domain associated with the mitotic spindle.

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“…in regions adjacent to mitotic spindle (Dabauvalle et al, 1999). The ER marker protein disulfide isomerase was also excluded from this membrane domain.…”

Section: Discussionmentioning

confidence: 99%

Section: Samp1 Displays An Unexpected Distribution To the Polar Areasmentioning

confidence: 99%

An integral protein of the inner nuclear membrane localizes to the mitotic spindle in mammalian cells

Buch

Lindberg

Figueroa

et al. 2009

Journal of Cell Science

100

View full text Add to dashboard Cite

show abstract

“…LAP2β was first detectable at chromosomes slightly after LAP2α during nuclear reassembly (Vlcek et al, 2002) whereas LBR appeared at chromosomes at detectable levels slightly before LAP2α (see Movies 2 and 3 in supplementary material). However, both LAP2β and LBR mostly localized to more peripheral sites of the chromatin bulk, distinct from the LAP2α-containing core regions (see also Dabauvalle et al, 1999;Haraguchi et al, 2000). In contrast to LBR, LAP2β also accumulated on chromatin core structures, before both LBR and LAP2β spread over the entire surface of decondensing chromatin at later stages of assembly.…”

Section: Lap2α Association With Chromosomes Differs From That Of Nuclmentioning

confidence: 96%

“…LBR and emerin are targeted to chromosomes about 5 minutes after metaphase-anaphase transition, followed by nuclear pore complex assembly (Haraguchi et al, 2000). LAP2β was also found to accumulate at around the same time as emerin (Bodoor et al, 1999;Dabauvalle et al, 1999;Foisner and Gerace, 1993). B-and A-type lamins follow different pathways (Moir et al, 2000).…”

mentioning

confidence: 99%

LAP2α and BAF transiently localize to telomeres and specific regions on chromatin during nuclear assembly

Dechat

Gajewski

Korbei

et al. 2004

Journal of Cell Science

188

206

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Lamina-associated polypeptide (LAP) 2α is a LEM (lamina-associated polypeptide emerin MAN1) family protein associated with nucleoplasmic A-type lamins and chromatin. Using live cell imaging and fluorescence microscopy we demonstrate that LAP2α was mostly cytoplasmic in metaphase and associated with telomeres in anaphase. Telomeric LAP2α clusters grew in size, formed `core' structures on chromatin adjacent to the spindle in telophase, and translocated to the nucleoplasm in G1 phase. A subfraction of lamin C and emerin followed LAP2α to the core region early on, whereas LAP2β, lamin B receptor and lamin B initially bound to more peripheral regions of chromatin, before they spread to core structures with different kinetics. Furthermore, the DNA-crosslinking protein barrier-to-autointegration factor (BAF) bound to LAP2α in vitro and in mitotic extracts, and subfractions of BAF relocalized to core structures with LAP2α. We propose that LAP2α and a subfraction of BAF form defined complexes in chromatin core regions and may be involved in chromatin reorganization during early stages of nuclear assembly.

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“…While antibodies against lamins can block formation of NPCs they do not hinder the assembly of AL stacks (Dabauvalle et al, 1991). Moreover, evidence was found that emerin, a transmembrane protein of the inner nuclear membrane, is not present in AL (Dabauvalle et al, 1999).…”

Section: Biochemical Compositionmentioning

confidence: 99%

Tubulohelical Membrane Arrays, Annulate Lamellae and Nuclear Pores: Tripartite Membrane Architecture with the Participation of Nucleoporins

Reipert¹,

Киселева²

2012

Current Frontiers and Perspectives in Cell Biology

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Distribution of emerin during the cell cycle

Cited by 45 publications

References 44 publications

An integral protein of the inner nuclear membrane localizes to the mitotic spindle in mammalian cells

An integral protein of the inner nuclear membrane localizes to the mitotic spindle in mammalian cells

LAP2α and BAF transiently localize to telomeres and specific regions on chromatin during nuclear assembly

Tubulohelical Membrane Arrays, Annulate Lamellae and Nuclear Pores: Tripartite Membrane Architecture with the Participation of Nucleoporins

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