• Login
    View Item 
    •   Home
    • The Manchester Institute Cancer Research UK
    • All Paterson Institute for Cancer Research
    • View Item
    •   Home
    • The Manchester Institute Cancer Research UK
    • All Paterson Institute for Cancer Research
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of ChristieCommunitiesTitleAuthorsIssue DateSubmit DateSubjectsThis CollectionTitleAuthorsIssue DateSubmit DateSubjects

    My Account

    LoginRegister

    Local Links

    The Christie WebsiteChristie Library and Knowledge Service

    Statistics

    Display statistics

    Concentration of Ran on chromatin induces decondensation, nuclear envelope formation and nuclear pore complex assembly.

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Authors
    Zhang, Chuanmao
    Goldberg, Martin W
    Moore, William J
    Allen, Terence D
    Clarke, Paul R
    Affiliation
    Department of Structural Cell Biology, Paterson Institute for Cancer Research, Christie Hopsital, Masnchester M20 4BX, UK
    Issue Date
    2002-11
    
    Metadata
    Show full item record
    Abstract
    Nuclear envelope (NE) formation can be studied in a cell-free system made from Xenopus eggs. In this system, NE formation involves the small GTPase Ran. Ran associates with chromatin early in nuclear assembly and concentration of Ran on inert beads is sufficient to induce NE formation. Here, we show that Ran binds to chromatin prior to NE formation and recruits RCC1, the nucleotide exchange factor that generates Ran-GTP. In extracts prepared by high-speed centrifugation, increased concentrations of Ran are sufficient to induce chromatin decondensation and NE assembly. Using field emission in-lens scanning electron microscopy (FEISEM), we show that Ran promotes the formation of smoothed membranes and the assembly of nuclear pore complexes (NPCs). In contrast, RanT24N, a mutant that fails to bind GTP and inhibits RCC1, does not support efficient NE assembly, whereas RanQ69L, a mutant locked in a GTP-bound state, permits some membrane vesicle recruitment to chromatin, but inhibits vesicle fusion and NPC assembly. Thus, binding of Ran to chromatin, followed by local generation of Ran-GTP and GTP hydrolysis by Ran, induces chromatin decondensation, membrane vesicle recruitment, membrane formation and NPC assembly. We propose that the biological activity of Ran is determined by its targeting to structures such as chromatin as well as its guanine nucleotide bound state.
    Citation
    Concentration of Ran on chromatin induces decondensation, nuclear envelope formation and nuclear pore complex assembly. 2002, 81 (11):623-33 Eur. J. Cell Biol.
    Journal
    European Journal of Cell Biology
    URI
    http://hdl.handle.net/10541/84333
    PubMed ID
    12494999
    Type
    Article
    Language
    en
    ISSN
    0171-9335
    Collections
    All Paterson Institute for Cancer Research

    entitlement

    Related articles

    • GTP hydrolysis by Ran is required for nuclear envelope assembly.
    • Authors: Hetzer M, Bilbao-Cortés D, Walther TC, Gruss OJ, Mattaj IW
    • Issue date: 2000 Jun
    • Chromatin-independent nuclear envelope assembly induced by Ran GTPase in Xenopus egg extracts.
    • Authors: Zhang C, Clarke PR
    • Issue date: 2000 May 26
    • Spatial and temporal control of nuclear envelope assembly by Ran GTPase.
    • Authors: Clarke PR, Zhang C
    • Issue date: 2004
    • Ran binds to chromatin by two distinct mechanisms.
    • Authors: Bilbao-Cortés D, Hetzer M, Längst G, Becker PB, Mattaj IW
    • Issue date: 2002 Jul 9
    • Chromatin-bound NLS proteins recruit membrane vesicles and nucleoporins for nuclear envelope assembly via importin-α/β.
    • Authors: Lu Q, Lu Z, Liu Q, Guo L, Ren H, Fu J, Jiang Q, Clarke PR, Zhang C
    • Issue date: 2012 Nov
    DSpace software (copyright © 2002 - 2023)  DuraSpace
    Quick Guide | Contact Us
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.