Linked Life Data

12559755

Source:http://linkedlifedata.com/resource/pubmed/id/12559755

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2003-1-31
pubmed:abstractText
Until very recently, the vertebrate protein Npap60/Nup50 was thought merely to be a component of the nuclear pore complex (NPC). This conclusion was based on the observations that Npap60/Nup50 localizes at the NPC by immunofluorescence and electron microscopy and also contains FG (Phe-Gly) repeats, a motif commonly found in nucleoporins but not in proteins located elsewhere. However, far from being a fixed structural component of the NPC, it now appears as though Npap60 can shuttle from one side of the NPC to the other. Most significantly, a recent paper shows that Npap60 enhances the nuclear import of a cargo possessing a basic nuclear localization sequence by associating directly with the import cargo-carrier complex and (presumably) moving through the NPC with it. Several NPC proteins have now been shown to be mobile in the NPC, and this new report might indicate that these 'mobile' nucleoporins play a more active role in the nuclear transport of cargo than was previously appreciated.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0962-8924
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
61-4
pubmed:dateRevised
2005-11-16
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Npap60: a new player in nuclear protein import.
pubmed:affiliation
Dept of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030, USA. mmoore@bcm.tmc.edu
pubmed:publicationType
Journal Article, Review