| pubmed-article:17562857 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17562857 | lifeskim:mentions | umls-concept:C0205252 | lld:lifeskim |
| pubmed-article:17562857 | lifeskim:mentions | umls-concept:C0035696 | lld:lifeskim |
| pubmed-article:17562857 | lifeskim:mentions | umls-concept:C0242611 | lld:lifeskim |
| pubmed-article:17562857 | lifeskim:mentions | umls-concept:C1157567 | lld:lifeskim |
| pubmed-article:17562857 | lifeskim:mentions | umls-concept:C0162610 | lld:lifeskim |
| pubmed-article:17562857 | lifeskim:mentions | umls-concept:C0332256 | lld:lifeskim |
| pubmed-article:17562857 | lifeskim:mentions | umls-concept:C1708936 | lld:lifeskim |
| pubmed-article:17562857 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:17562857 | pubmed:dateCreated | 2007-7-31 | lld:pubmed |
| pubmed-article:17562857 | pubmed:abstractText | Eukaryotic mRNAs containing premature translation termination codons (PTCs) are rapidly degraded by a process termed "nonsense-mediated mRNA decay" (NMD). We examined protein-protein and protein-RNA interactions among Caenorhabditis elegans proteins required for NMD. SMG-2, SMG-3, and SMG-4 are orthologs of yeast (Saccharomyces cerevisiae) and mammalian Upf1, Upf2, and Upf3, respectively. A combination of immunoprecipitation and yeast two-hybrid experiments indicated that SMG-2 interacts with SMG-3, SMG-3 interacts with SMG-4, and SMG-2 interacts indirectly with SMG-4 via shared interactions with SMG-3. Such interactions are similar to those observed in yeast and mammalian cells. SMG-2-SMG-3-SMG-4 interactions require neither SMG-2 phosphorylation, which is abolished in smg-1 mutants, nor SMG-2 dephosphorylation, which is reduced or eliminated in smg-5 mutants. SMG-2 preferentially associates with PTC-containing mRNAs. We monitored the association of SMG-2, SMG-3, and SMG-4 with mRNAs of five endogenous genes whose mRNAs are alternatively spliced to either contain or not contain PTCs. SMG-2 associates with both PTC-free and PTC-containing mRNPs, but it strongly and preferentially associates with ("marks") those containing PTCs. SMG-2 marking of PTC-mRNPs is enhanced by SMG-3 and SMG-4, but SMG-3 and SMG-4 are not detectably associated with the same mRNPs. Neither SMG-2 phosphorylation nor dephosphorylation is required for selective association of SMG-2 with PTC-containing mRNPs, indicating that SMG-2 is phosphorylated only after premature terminations have been discriminated from normal terminations. We discuss these observations with regard to the functions of SMG-2 and its phosphorylation during NMD. | lld:pubmed |
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| pubmed-article:17562857 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17562857 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17562857 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17562857 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17562857 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17562857 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:17562857 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:17562857 | pubmed:author | pubmed-author:JohnsLisaL | lld:pubmed |
| pubmed-article:17562857 | pubmed:author | pubmed-author:GrimsonAndrew... | lld:pubmed |
| pubmed-article:17562857 | pubmed:author | pubmed-author:AndersonPhili... | lld:pubmed |
| pubmed-article:17562857 | pubmed:author | pubmed-author:NewmanCarrie... | lld:pubmed |
| pubmed-article:17562857 | pubmed:author | pubmed-author:KuchmaSherry... | lld:pubmed |
| pubmed-article:17562857 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17562857 | pubmed:volume | 27 | lld:pubmed |
