Linked Life Data

18664458

Source:http://linkedlifedata.com/resource/pubmed/id/18664458

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
2008-10-2
pubmed:abstractText
Tudor domains are widespread among proteins involved in RNA metabolism, but only in a few cases their cellular function has been analyzed in detail. Here, we report on the characterization of the ubiquitously expressed Tudor domain containing protein Tdrd3. Apart from its Tudor domain, we show that Tdrd3 possesses an oligosaccharide/nucleotide binding fold (OB-fold) and an ubiquitin associated domain capable of binding tetra-ubiquitin. A set of biochemical experiments revealed an interaction of Tdrd3 with FMRP, the product of the gene affected in Fragile X syndrome, and its autosomal homologs FXR1 and FXR2. FMRP has been implicated in the translational regulation of target mRNAs and shown to be a component of stress granules (SG). We demonstrate that overexpression of Tdrd3 in cells induces the formation of SGs and as a result leads to its co-localization with endogenous FMRP in these structures. Interestingly, the disease-associated FMRP missense mutation I304N identified in a Fragile X patient severely impairs the interaction with Tdrd3 in biochemical experiments. We propose a contribution of Tdrd3 to FMRP-mediated translational repression and suggest that the loss of the FMRP-Tdrd3 interaction caused by the I304N mutation might contribute to the pathogenesis of Fragile X syndrome.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1460-2083
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3236-46
pubmed:meshHeading
pubmed-meshheading:18664458-Amino Acid Sequence, pubmed-meshheading:18664458-Amino Acid Substitution, pubmed-meshheading:18664458-Cytosol, pubmed-meshheading:18664458-Fragile X Mental Retardation Protein, pubmed-meshheading:18664458-Fragile X Syndrome, pubmed-meshheading:18664458-HeLa Cells, pubmed-meshheading:18664458-Humans, pubmed-meshheading:18664458-Molecular Sequence Data, pubmed-meshheading:18664458-Mutation, Missense, pubmed-meshheading:18664458-Protein Binding, pubmed-meshheading:18664458-Protein Interaction Domains and Motifs, pubmed-meshheading:18664458-Protein Interaction Mapping, pubmed-meshheading:18664458-RNA, Messenger, pubmed-meshheading:18664458-RNA-Binding Proteins, pubmed-meshheading:18664458-Recombinant Proteins, pubmed-meshheading:18664458-Sequence Homology, Amino Acid
pubmed:year
2008
pubmed:articleTitle
Tdrd3 is a novel stress granule-associated protein interacting with the Fragile-X syndrome protein FMRP.
pubmed:affiliation
Department of Biochemistry, Theodor Boveri Institute, Am Hubland, D-97074 Würzburg, Germany.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't