Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
2002-4-29
pubmed:databankReference
pubmed:abstractText
Receptor-interacting protein (RIP) is a serine/threonine protein kinase that is critically involved in tumor necrosis factor receptor-1 (TNF-R1)-induced NF-kappa B activation. In a yeast two-hybrid screening for potential RIP-interacting proteins, we identified ZIN (zinc finger protein inhibiting NF-kappa B), a novel protein that specifically interacts with RIP. ZIN contains four RING-like zinc finger domains at the middle and a proline-rich domain at the C terminus. Overexpression of ZIN inhibits RIP-, IKK beta-, TNF-, and IL1-induced NF-kappa B activation in a dose-dependent manner in 293 cells. Domain mapping experiments indicate that the RING-like zinc finger domains of ZIN are required for its interaction with RIP and inhibition of RIP-mediated NF-kappa B activation. Overexpression of ZIN also potentiates RIP- and TNF-induced apoptosis. Moreover, immunofluorescent staining indicates that ZIN is a cytoplasmic protein and that it colocalizes with RIP. Our findings suggest that ZIN is an inhibitor of TNF- and IL1-induced NF-kappa B activation pathways.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1, http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RIPK1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Receptor-Interacting Protein..., http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha, http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15985-91
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:11854271-Amino Acid Sequence, pubmed-meshheading:11854271-Carrier Proteins, pubmed-meshheading:11854271-Cell Line, pubmed-meshheading:11854271-Humans, pubmed-meshheading:11854271-Interleukin-1, pubmed-meshheading:11854271-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:11854271-Molecular Sequence Data, pubmed-meshheading:11854271-NF-kappa B, pubmed-meshheading:11854271-Protein-Serine-Threonine Kinases, pubmed-meshheading:11854271-Proteins, pubmed-meshheading:11854271-Receptor-Interacting Protein Serine-Threonine Kinases, pubmed-meshheading:11854271-Recombinant Proteins, pubmed-meshheading:11854271-Transfection, pubmed-meshheading:11854271-Tumor Necrosis Factor-alpha, pubmed-meshheading:11854271-Ubiquitin-Protein Ligases, pubmed-meshheading:11854271-Zinc Fingers
pubmed:year
2002
pubmed:articleTitle
A novel zinc finger protein interacts with receptor-interacting protein (RIP) and inhibits tumor necrosis factor (TNF)- and IL1-induced NF-kappa B activation.
pubmed:affiliation
Department of Cell Biology and Genetics, College of Life Sciences, Peking University, Beijing 100871, China.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't