Document Detail

Nuclear assembly.
MedLine Citation:
PMID:  9442884     Owner:  NLM     Status:  MEDLINE    
We review old and new insights into the structure of the nuclear envelope and the components responsible for its dynamic reassembly during mitosis. New information is coming to light about several of the proteins that mediate nuclear reassembly. These proteins include the lamins and their emerging relationship with proteins such as otefin and the MAN antigens: peripheral proteins that might participate in lamina structure. There are four identified proteins localized to the inner nuclear membrane: the lamina-associated proteins LAP1 and LAP2, emerin, and the lamin B receptor (LBR). LBR can interact independently with lamin B and a chromodomain protein, Hp1, and appears to be a central player in targeting nuclear membranes to chromatin. Intermediates in the assembly of nuclear pore complexes (NPCs) can now be studied biochemically and visualized by high resolution scanning electron microscopy. We discuss the possibility that the filament-forming proteins Tpr/p270, NuMA, and perhaps actin may have roles in nuclear assembly.
T M Gant; K L Wilson
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.; Review    
Journal Detail:
Title:  Annual review of cell and developmental biology     Volume:  13     ISSN:  1081-0706     ISO Abbreviation:  Annu. Rev. Cell Dev. Biol.     Publication Date:  1997  
Date Detail:
Created Date:  1998-02-13     Completed Date:  1998-02-13     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  9600627     Medline TA:  Annu Rev Cell Dev Biol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  669-95     Citation Subset:  IM    
Department of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
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MeSH Terms
Cell Nucleus / physiology,  ultrastructure*
Nuclear Envelope / chemistry,  physiology,  ultrastructure
Nuclear Proteins / analysis
Grant Support
Reg. No./Substance:
0/Nuclear Proteins

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