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https://olympias.lib.uoi.gr/jspui/handle/123456789/18713Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Maison, C. | en |
| dc.contributor.author | Horstmann, H. | en |
| dc.contributor.author | Georgatos, S. D. | en |
| dc.date.accessioned | 2015-11-24T18:54:39Z | - |
| dc.date.available | 2015-11-24T18:54:39Z | - |
| dc.identifier.issn | 0021-9525 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/18713 | - |
| dc.rights | Default Licence | - |
| dc.subject | Animals | en |
| dc.subject | Cell Compartmentation | en |
| dc.subject | Cell Line | en |
| dc.subject | Cricetinae | en |
| dc.subject | Fluorescent Antibody Technique | en |
| dc.subject | Immunohistochemistry | en |
| dc.subject | Intermediate Filaments/*metabolism | en |
| dc.subject | Lamin Type B | en |
| dc.subject | Lamins | en |
| dc.subject | *Mitosis | en |
| dc.subject | Nuclear Envelope/*metabolism | en |
| dc.subject | Nuclear Proteins/metabolism | en |
| dc.subject | Phosphorylation | en |
| dc.subject | Vimentin/*metabolism | en |
| dc.title | Regulated docking of nuclear membrane vesicles to vimentin filaments during mitosis | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.secondary | http://www.ncbi.nlm.nih.gov/pubmed/8253846 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής | el |
| heal.publicationDate | 1993 | - |
| heal.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. | en |
| heal.journalName | J Cell Biol | en |
| heal.journalType | peer-reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Georgatos-1993-regulated docking of.pdf | 5.59 MB | Adobe PDF | View/Open |
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