Publication Date:
2006-04-22
Description:
Nuclear pore complexes are multiprotein channels that span the double lipid bilayer of the nuclear envelope. How new pores are inserted into the intact nuclear envelope of proliferating and differentiating eukaryotic cells is unknown. We found that the Nup107-160 complex was incorporated into assembly sites in the nuclear envelope from both the nucleoplasmic and the cytoplasmic sides. Nuclear pore insertion required the generation of Ran guanosine triphosphate in the nuclear and cytoplasmic compartments. Newly formed nuclear pore complexes did not contain structural components of preexisting pores, suggesting that they can form de novo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉D'Angelo, Maximiliano A -- Anderson, Daniel J -- Richard, Erin -- Hetzer, Martin W -- New York, N.Y. -- Science. 2006 Apr 21;312(5772):440-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Salk Institute for Biological Studies, Molecular and Cell Biology Laboratory, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16627745" target="_blank"〉PubMed〈/a〉
Keywords:
Active Transport, Cell Nucleus
;
Animals
;
Cell-Free System
;
Cytoplasm/metabolism
;
Egtazic Acid/analogs & derivatives/pharmacology
;
Fluorescent Antibody Technique
;
Guanosine Triphosphate/metabolism
;
HeLa Cells
;
Humans
;
Image Processing, Computer-Assisted
;
Microscopy, Confocal
;
Nuclear Envelope/*metabolism/*ultrastructure
;
Nuclear Pore/*metabolism/*ultrastructure
;
Nuclear Pore Complex Proteins/*metabolism
;
Recombinant Proteins/metabolism
;
Wheat Germ Agglutinins/metabolism/pharmacology
;
Xenopus
;
beta Karyopherins/metabolism/pharmacology
;
ran GTP-Binding Protein/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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