Linked Life Data

1623516

Source:http://linkedlifedata.com/resource/pubmed/id/1623516

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1992-8-11
pubmed:databankReference
pubmed:abstractText
Nopp140 is a nucleolar phosphoprotein of 140 kd that we originally identified and purified as a nuclear localization signal (NLS)-binding protein. Molecular characterization revealed a 10-fold repeated motif of highly conserved acidic serine clusters that contain an abundance of phosphorylation consensus sites for casein kinase II (CK II). Indeed, Nopp140 is one of the most phosphorylated proteins in the cell, and NLS binding was dependent on phosphorylation. Nopp140 was shown to shuttle between the nucleolus and the cytoplasm. Shuttling is likely to proceed on tracks that were revealed by immunoelectron microscopy. These tracks extend from the dense fibrillar component of the nucleolus across the nucleoplasm to some nuclear pore complexes. We suggest that Nopp140 functions as a chaperone for import into and/or export from the nucleolus.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
127-38
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Nopp140 shuttles on tracks between nucleolus and cytoplasm.
pubmed:affiliation
Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York, New York 10021.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't