Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2002-10-3
pubmed:abstractText
Cajal bodies (CBs) are nuclear suborganelles involved in biogenesis of small RNAs. Twin structures, called gems, contain high concentrations of the survival motor neurons (SMN) protein complex. CBs and gems often colocalize, and communication between these subdomains is mediated by coilin, the CB marker. Coilin contains symmetrical dimethylarginines that modulate its affinity for SMN, and, thus, localization of SMN complexes to CBs. Inhibition of methylation or mutation of the coilin RG box dramatically decreases binding of coilin to SMN, resulting in gem formation. Coilin is hypomethylated in cells that display gems, but not in those that primarily contain CBs. Likewise, extracts prepared from cells that display gems are less efficient in methylating coilin and Sm constructs in vitro. These results demonstrate that alterations in protein methylation status can affect nuclear organization.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine, http://linkedlifedata.com/resource/pubmed/chemical/Arginine, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP Response..., http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Peptides, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Arginine..., http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SMN Complex Proteins, http://linkedlifedata.com/resource/pubmed/chemical/p80-coilin
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1534-5807
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
329-37
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:12361597-Adenosine, pubmed-meshheading:12361597-Amino Acid Sequence, pubmed-meshheading:12361597-Animals, pubmed-meshheading:12361597-Arginine, pubmed-meshheading:12361597-Cell Line, pubmed-meshheading:12361597-Cell Nucleus, pubmed-meshheading:12361597-Cells, Cultured, pubmed-meshheading:12361597-Coiled Bodies, pubmed-meshheading:12361597-Cyclic AMP Response Element-Binding Protein, pubmed-meshheading:12361597-Enzyme Inhibitors, pubmed-meshheading:12361597-Fibroblasts, pubmed-meshheading:12361597-Gene Deletion, pubmed-meshheading:12361597-Green Fluorescent Proteins, pubmed-meshheading:12361597-HeLa Cells, pubmed-meshheading:12361597-Humans, pubmed-meshheading:12361597-Luminescent Proteins, pubmed-meshheading:12361597-Methylation, pubmed-meshheading:12361597-Mice, pubmed-meshheading:12361597-Molecular Sequence Data, pubmed-meshheading:12361597-Mutation, pubmed-meshheading:12361597-Nerve Tissue Proteins, pubmed-meshheading:12361597-Nuclear Proteins, pubmed-meshheading:12361597-Peptides, pubmed-meshheading:12361597-Protein-Arginine N-Methyltransferases, pubmed-meshheading:12361597-RNA-Binding Proteins, pubmed-meshheading:12361597-SMN Complex Proteins, pubmed-meshheading:12361597-Transfection, pubmed-meshheading:12361597-Tumor Cells, Cultured
pubmed:year
2002
pubmed:articleTitle
Coilin methylation regulates nuclear body formation.
pubmed:affiliation
Department of Genetics, Center for Human Genetics, Case Western Reserve University, Cleveland, OH 44106, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't