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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2005-5-30
pubmed:abstractText
Notch signaling plays a pivotal role in numerous cell fate determination events during development, and therefore its regulation has been studied intensively. MSX2-interacting nuclear target protein (MINT) modifies the Notch signaling by interacting with and inhibiting the downstream transcription factor RBP-J/CBF-1 of Notch. In this study, by a yeast two hybrid screening, we found that the C terminal fragment of MINT interacted with each other. We confirmed the interaction between two MINT C terminal fragments both in vitro and in vivo. We further demonstrated that the overexpression of the C terminal fragment of MINT cancelled its inhibitory effect on the transactivation of an RBP-J-dependent promoter by Notch. These results suggest that MINT may form a dimer or multimer in cells through its C terminus, and that the C terminal fragment of MINT may work as its dominant-negative version.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/APBA1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin J Recombination..., http://linkedlifedata.com/resource/pubmed/chemical/MSX2 protein, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RBPJ protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Notch, http://linkedlifedata.com/resource/pubmed/chemical/Spen protein, mouse
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
1729
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
50-6
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:15777657-Adaptor Proteins, Signal Transducing, pubmed-meshheading:15777657-Animals, pubmed-meshheading:15777657-COS Cells, pubmed-meshheading:15777657-Cercopithecus aethiops, pubmed-meshheading:15777657-DNA-Binding Proteins, pubmed-meshheading:15777657-Gene Expression Regulation, pubmed-meshheading:15777657-Homeodomain Proteins, pubmed-meshheading:15777657-Humans, pubmed-meshheading:15777657-Immunoglobulin J Recombination Signal Sequence-Binding..., pubmed-meshheading:15777657-Membrane Proteins, pubmed-meshheading:15777657-Nerve Tissue Proteins, pubmed-meshheading:15777657-Nuclear Proteins, pubmed-meshheading:15777657-Promoter Regions, Genetic, pubmed-meshheading:15777657-Protein Structure, Tertiary, pubmed-meshheading:15777657-Receptors, Notch, pubmed-meshheading:15777657-Signal Transduction, pubmed-meshheading:15777657-Transcription, Genetic
pubmed:year
2005
pubmed:articleTitle
The C terminus of MINT forms homodimers and abrogates MINT-mediated transcriptional repression.
pubmed:affiliation
Department of Medical Genetics and Developmental Biology, State Key Laboratory of GI Cancer Biology, Fourth Military Medical University, Xian 710032, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't