ArticleThe EMBO journal1994
Type B lamins remain associated with the integral nuclear envelope protein p58 during mitosis: implications for nuclear reassembly.
Article in The EMBO journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 90 citations in OpenAlex.
- Telomeres in mitosis: organization and dynamics.Nucleus (Austin, Tex.) · 2026Review
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- Comprehending a Killer: The Akt/mTOR Signaling Pathways Are Temporally High-Jacked by the Highly Pathogenic 1918 Influenza Virus.EBioMedicine · 2018Article
- Baculovirus infection induces disruption of the nuclear lamina.Scientific reports · 2017Article
- Nuclear Exodus: Herpesviruses Lead the Way.Annual review of virology · 2016Article
- Lamin B receptor regulates the growth and maturation of myeloid progenitors via its sterol reductase domain: implications for cholesterol biosynthesis in regulating myelopoiesis.Journal of immunology (Baltimore, Md. : 1950) · 2012Article
- Requirement for lamin B receptor and its regulation by importin {beta} and phosphorylation in nuclear envelope assembly during mitotic exit.The Journal of biological chemistry · 2010Article
- Expression and localization of nuclear proteins in autosomal-dominant Emery-Dreifuss muscular dystrophy with LMNA R377H mutation.BMC cell biology · 2004Article
- Histones H3/H4 form a tight complex with the inner nuclear membrane protein LBR and heterochromatin protein 1.EMBO reports · 2001Article
- Fate of the inner nuclear membrane protein lamin B receptor and nuclear lamins in herpes simplex virus type 1 infection.Journal of virology · 2001Article
- The inner nuclear membrane: simple, or very complex?The EMBO journal · 2001Review
- Early localization of NPA58, a rat nuclear pore-associated protein, to the reforming nuclear envelope during mitosis.Journal of biosciences · 2001Article
- Nuclear lamins A and B1: different pathways of assembly during nuclear envelope formation in living cells.The Journal of cell biology · 2000Article
- Dynamic associations of heterochromatin protein 1 with the nuclear envelope.The EMBO journal · 2000Article
- Association of prenylated proteins with the plasma membrane and the inner nuclear membrane is mediated by the same membrane-targeting motifs.Molecular biology of the cell · 2000Article
- Detergent-salt resistance of LAP2alpha in interphase nuclei and phosphorylation-dependent association with chromosomes early in nuclear assembly implies functions in nuclear structure dynamics.The EMBO journal · 1998Article
- Dissociation of Oct-1 from the nuclear peripheral structure induces the cellular aging-associated collagenase gene expression.Molecular biology of the cell · 1997Article
- The inner nuclear membrane protein LAP1 forms a native complex with B-type lamins and partitions with spindle-associated mitotic vesicles.The EMBO journal · 1997Article
- Topogenesis of a nucleolar protein: determination of molecular segments directing nucleolar association.Molecular biology of the cell · 1997Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
p58 (also referred to as the lamin B receptor) is an integral membrane protein of the nuclear envelope known to form a multimeric complex with the lamins and other nuclear proteins during interphase. To examine the fate of this complex during mitosis, we have investigated the partitioning and the molecular interactions of p58 in dividing chicken hepatoma (DU249) cells. Using confocal microscopy and double immunolabelling, we show here that lamins B1 and B2 co-localize with p58 during all phases of mitosis and co-assemble around reforming nuclei. A close juxtaposition of p58/lamin B-containing vesicles and chromosomes is already detectable in metaphase; however, p58 and lamin reassembly proceeds slowly and is completed in late telophase--G1. Flotation of mitotic membranes in sucrose density gradients and analysis of mitotic vesicles by immunoelectron microscopy confirms that p58 and most of the type B lamins reside in the same compartment. Co-immunoprecipitation of both proteins by affinity-purified anti-p58 antibodies shows that they are physically associated in the context of a mitotic p58 'sub-complex'. This sub-assembly does not include the type A lamins which are fully solubilized during mitosis. Our data provide direct, in vivo and in vitro evidence that the majority of type B lamins remain connected to nuclear membrane 'receptors' during mitosis. The implications of these findings in nuclear envelope reassembly are discussed below.
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