Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
|
pubmed:dateCreated |
1992-8-14
|
pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M79310,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M81118,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S39480,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S49473,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S49475,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X01023,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X65112,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X65113,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X66097,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X66098
|
pubmed:abstractText |
c-myc belongs to a small, yet growing, group of eukaryotic mRNAs that initiate translation inefficiently from a non-AUG codon upstream from a more efficient AUG codon. We have examined the translational regulation of non-AUG-initiated c-myc 1 and AUG-initiated c-myc 2 protein synthesis in avian and mouse cells during proliferation. As lymphoid, erythroid, and embryo fibroblast cells approached high densities in culture, there was a sustained 5- to 10-fold induction in the synthesis of c-myc 1 protein to levels greater than or equal to c-myc 2 protein synthesis. Treatment with conditioned/depleted media from high-density cells was able to reproduce this activation in low-density cells within 5 hr. Additional studies with the conditioned/depleted media revealed that amino acid availability, specifically methionine deprivation, was responsible for this unique translational control. Our results describe a specific and dramatic regulation of dual translational initiation. Furthermore, these results represent a novel translational activation of a specific gene in higher eukaryotes in response to nutrient deprivation.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
0890-9369
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
6
|
pubmed:geneSymbol |
c-myc
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1229-40
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:1628829-Amino Acid Sequence,
pubmed-meshheading:1628829-Animals,
pubmed-meshheading:1628829-Base Sequence,
pubmed-meshheading:1628829-Cell Count,
pubmed-meshheading:1628829-Codon,
pubmed-meshheading:1628829-DNA,
pubmed-meshheading:1628829-Gene Expression Regulation,
pubmed-meshheading:1628829-Humans,
pubmed-meshheading:1628829-Kinetics,
pubmed-meshheading:1628829-Methionine,
pubmed-meshheading:1628829-Molecular Sequence Data,
pubmed-meshheading:1628829-Protein Biosynthesis,
pubmed-meshheading:1628829-Proto-Oncogene Proteins c-myc,
pubmed-meshheading:1628829-Tumor Cells, Cultured
|
pubmed:year |
1992
|
pubmed:articleTitle |
Translational activation of the non-AUG-initiated c-myc 1 protein at high cell densities due to methionine deprivation.
|
pubmed:affiliation |
Department of Cell Biology, Vanderbilt University, School of Medicine, Nashville, Tennessee 37232-2175.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|