Linked Life Data

19794129

Source:http://linkedlifedata.com/resource/pubmed/id/19794129

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2009-11-25
pubmed:abstractText
Four major glutamate receptor 2 (GluR2) transcripts differing in size (approximately 4 and approximately 6 kilobases) due to alternative 3' untranslated regions (UTRs), and also containing alternative 5'UTRs, exist in the brain. Both the long 5'UTR and long 3'UTR repress translation of GluR2 mRNA; repression by the 3'UTR is relieved after seizures. To understand the mechanism of translational repression, we used rabbit reticulocyte lysates as an in vitro translation system to examine the expression profiles of firefly reporter mRNAs bearing alternative combinations of GluR2 5'UTR and 3'UTR in the presence of inhibitors of either translational elongation or initiation. Translation of reporter mRNAs bearing the long GluR2 3'UTR was insensitive to low concentrations of the translation elongation inhibitors cycloheximide (0.7-70 nM) and anisomycin (7.5-750 nM), in contrast to a reporter bearing the short 3'UTR, which was inhibited. These data suggest that the rate-limiting step for translation of GluR2 mRNA bearing the long 3'UTR is not elongation. Regardless of the GluR2 UTR length, translation of all reporter mRNAs was equally sensitive to desmethyl-desamino-pateamine A (0.2-200 nM), an initiation inhibitor. Kasugamycin, which can facilitate recognition of certain mRNAs by ribosomes leading to alternative initiation, had no effect on translation of a capped reporter bearing both short 5'UTR and short 3'UTR, but increased the translation rate of reporters bearing either the long GluR2 5'UTR or long 3'UTR. Our findings suggest that both the long 5'UTR and long 3'UTR of GluR2 mRNA repress translation at the initiation step.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/3' Untranslated Regions, http://linkedlifedata.com/resource/pubmed/chemical/5' Untranslated Regions, http://linkedlifedata.com/resource/pubmed/chemical/Aminoglycosides, http://linkedlifedata.com/resource/pubmed/chemical/Anisomycin, http://linkedlifedata.com/resource/pubmed/chemical/Cycloheximide, http://linkedlifedata.com/resource/pubmed/chemical/Epoxy Compounds, http://linkedlifedata.com/resource/pubmed/chemical/Macrolides, http://linkedlifedata.com/resource/pubmed/chemical/Protein Synthesis Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, AMPA, http://linkedlifedata.com/resource/pubmed/chemical/Thiazoles, http://linkedlifedata.com/resource/pubmed/chemical/glutamate receptor ionotropic..., http://linkedlifedata.com/resource/pubmed/chemical/kasugamycin, http://linkedlifedata.com/resource/pubmed/chemical/pateamine A
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1521-0111
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
76
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1145-9
pubmed:dateRevised
2011-3-3
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Control of glutamate receptor 2 (GluR2) translational initiation by its alternative 3' untranslated regions.
pubmed:affiliation
Department of Pharmacology, Emory University School of Medicine, Rollins Research Center, Room 5002, 1510 Clifton Rd NE, Atlanta, GA 30322, USA. hirier@emory.edu
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural