Linked Life Data

15039779

Source:http://linkedlifedata.com/resource/pubmed/id/15039779

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2004-3-24
pubmed:abstractText
Translocation through nuclear pore complexes (NPCs) requires interactions between receptor-cargo complexes and phenylalanine-glycine (FG) repeats in multiple FG domain-containing NPC proteins (FG-Nups). We have systematically deleted the FG domains of 11 Saccharomyces cerevisiae FG-Nups in various combinations. All five asymmetrically localized FG domains deleted together were non-essential. However, specific combinations of symmetrically localized FG domains were essential. Over half the total mass of FG domains could be deleted without loss of viability or the NPC's normal permeability barrier. Significantly, symmetric deletions caused mild reductions in Kap95-Kap60-mediated import rates, but virtually abolished Kap104 import. These results suggest the existence of multiple translocation pathways.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1465-7392
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
197-206
pubmed:dateRevised
2009-7-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Minimal nuclear pore complexes define FG repeat domains essential for transport.
pubmed:affiliation
Department of Cell and Developmental Biology, Vanderbilt University Medical Center, 3120A MRBIII, 465 21st Avenue South, Nashville, TN 37232-8240, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.