Linked Life Data

9013710

Source:http://linkedlifedata.com/resource/pubmed/id/9013710

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-2-20
pubmed:abstractText
Coiled bodies are conserved subnuclear organelles that contain splicing snRNPs, a subset of nucleolar antigens, and the autoantigen p80 coilin. Most nuclei contain one to five nucleoplasmic coiled bodies, often with one or more located at the nucleolar periphery. Here we show that exposure of mammalian cells to low levels of the specific Ser/Thr protein phosphatase inhibitor, okadaic acid, results in the accumulation of p80 coilin and splicing snRNPs within nucleoli. Mutation of a single serine residue in p80 coilin to aspartate (S202D) also causes coiled bodies and splicing snRNPs to localize within nucleoli when the mutant is transiently transfected and expressed in HeLa cells. Neither okadaic acid nor the S202D coilin mutant causes nucleolar accumulation of serine-arginine-domain proteins. These data indicate that protein dephosphorylation is required to allow normal formation of nucleoplasmic coiled bodies and point to p80 coilin as a substrate whose phosphorylation state may regulate snRNP-nucleolar interactions. The data are consistent with a trafficking mechanism whereby splicing snRNPs cycle through the nucleolus.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-4827
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
230
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
84-93
pubmed:dateRevised
2009-9-29
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Inhibition of protein dephosphorylation results in the accumulation of splicing snRNPs and coiled bodies within the nucleolus.
pubmed:affiliation
Department of Biochemistry, University of Dundee, Scotland, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't