rdf:type |
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lifeskim:mentions |
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pubmed:issue |
32
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pubmed:dateCreated |
1998-9-10
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pubmed:abstractText |
The Elav-like proteins are specific mRNA-binding proteins that regulate mRNA stability. The neuronal members of this family (HuD, HuC, and Hel-N1) are required for neuronal differentiation. In this report, using purified HuD protein we have localized a high affinity HuD binding site to a 42-nucleotide region within a U-rich tract in the 3'-untranslated region p21(waf1) mRNA. The binding of HuD to this site is readily displaced by an RNA oligonucleotide encoding the HuD binding site of c-fos. The sequence of this binding site is well conserved in human, mouse, and rat p21(waf1) mRNA. p21(waf1) is an inhibitor of cyclin-dependent kinases and proliferating cell nuclear antigen and induces cell cycle arrest at G1/S, a requisite early step in cell differentiation. The identification of an Elav-like protein binding site in the 3'-untranslated region of p21(waf1) provides a novel link between the induction of differentiation, mRNA stability, and the termination of the cell cycle.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CDKN1A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cdkn1a protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cdkn1a protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase Inhibitor...,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclins,
http://linkedlifedata.com/resource/pubmed/chemical/ELAVL4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Elavl4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Hu Paraneoplastic...,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
20511-6
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9685407-Animals,
pubmed-meshheading:9685407-Base Sequence,
pubmed-meshheading:9685407-Binding, Competitive,
pubmed-meshheading:9685407-Binding Sites,
pubmed-meshheading:9685407-Cell Cycle,
pubmed-meshheading:9685407-Cell Differentiation,
pubmed-meshheading:9685407-Conserved Sequence,
pubmed-meshheading:9685407-Cyclin-Dependent Kinase Inhibitor p21,
pubmed-meshheading:9685407-Cyclin-Dependent Kinases,
pubmed-meshheading:9685407-Cyclins,
pubmed-meshheading:9685407-Enzyme Inhibitors,
pubmed-meshheading:9685407-Genes, fos,
pubmed-meshheading:9685407-Hu Paraneoplastic Encephalomyelitis Antigens,
pubmed-meshheading:9685407-Humans,
pubmed-meshheading:9685407-Mice,
pubmed-meshheading:9685407-Molecular Sequence Data,
pubmed-meshheading:9685407-Nerve Tissue Proteins,
pubmed-meshheading:9685407-Oligonucleotides,
pubmed-meshheading:9685407-RNA, Messenger,
pubmed-meshheading:9685407-RNA-Binding Proteins,
pubmed-meshheading:9685407-Rats,
pubmed-meshheading:9685407-Ribonucleases,
pubmed-meshheading:9685407-Ribonucleoproteins
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pubmed:year |
1998
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pubmed:articleTitle |
p21(waf1) mRNA contains a conserved element in its 3'-untranslated region that is bound by the Elav-like mRNA-stabilizing proteins.
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pubmed:affiliation |
Program in Molecular Pharmacology and Therapeutics, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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