ArticleThe Journal of cell biology1993
Regulated docking of nuclear membrane vesicles to vimentin filaments during mitosis.
Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 63 citations in OpenAlex.
- Distinct roles of haspin in stem cell division and male gametogenesis.Scientific reports · 2021Article
- Nuclear Translocation of SRPKs Is Associated with 5-FU and Cisplatin Sensitivity in HeLa and T24 Cells.Cells · 2021Article
- A vimentin binding small molecule leads to mitotic disruption in mesenchymal cancers.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Solution structure and molecular interactions of lamin B receptor Tudor domain.The Journal of biological chemistry · 2012Article
- Seven kinds of intermediate filament networks in the cytoplasm of polarized cells: structure and function.Acta histochemica et cytochemica · 2010Article
- Evaluation of mammalian cell-free systems of nuclear disassembly and assembly.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2008Article
- Dynamic associations of heterochromatin protein 1 with the nuclear envelope.The EMBO journal · 2000Article
- Vimentin filaments in fibroblasts are a reservoir for SNAP23, a component of the membrane fusion machinery.Molecular biology of the cell · 2000Article
- Desmin cytoskeleton in healthy and failing heart.Heart failure reviews · 2000Review
- Wheatgerm agglutinin-mediated toxicity in pancreatic cancer cells.British journal of cancer · 1999Article
- 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
- Integral membrane proteins of the nuclear envelope are dispersed throughout the endoplasmic reticulum during mitosis.The Journal of cell biology · 1997Article
- The lamin B receptor (LBR) provides essential chromatin docking sites at the nuclear envelope.The EMBO journal · 1996Article
- Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions.The Journal of cell biology · 1996Article
- Mitosis-specific phosphorylation of vimentin by protein kinase C coupled with reorganization of intracellular membranes.The Journal of cell biology · 1996Article
- Vimentin-associated mitotic vesicles interact with chromosomes in a lamin B- and phosphorylation-dependent manner.The EMBO journal · 1995Article
- Type B lamins remain associated with the integral nuclear envelope protein p58 during mitosis: implications for nuclear reassembly.The EMBO journal · 1994Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During mitosis, several types of intermediate-sized filaments (IFs) undergo an extensive remodelling in response to phosphorylation by cdc 2 and other protein kinases. However, unlike the nuclear lamins, the cytoplasmic IFs do not seem to follow a fixed disassembly stereotype and often retain their physical continuity without depolymerizing into soluble subunits. To investigate potential interactions between mitotically modified IFs and other cellular structures, we have examined prometaphase-arrested cells expressing the IF protein vimentin. We demonstrate here that vimentin filaments associate in situ and co-fractionate with a distinct population of mitotic vesicles. These vesicles carry on their surfaces nuclear lamin B, the inner nuclear membrane protein p58, and wheat germ agglutinin (WGA)-binding proteins. Consistent with a tight interaction between the IFs and the mitotic membranes, vimentin, nuclear lamin B, and a 180-kD WGA-binding protein are co-isolated when whole mitotic homogenates are incubated with anti-vimentin or anti-lamin B antibodies immobilized on magnetic beads. The vimentin-associated vesicles are essentially depleted of ER, Golgi and endosomal membrane proteins. The interaction of vimentin with lamin B-carrying membranes depends on phosphorylation and is weakened by dephosphorylation during nuclear reassembly in vitro. These observations reveal a novel interaction between IFs and cellular membranes and further suggest that the vimentin filaments may serve as a transient docking site for inner nuclear membrane vesicles during mitosis.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.