Linked Life Data

12048196

Source:http://linkedlifedata.com/resource/pubmed/id/12048196

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
34
pubmed:dateCreated
2002-8-19
pubmed:databankReference
pubmed:abstractText
We have previously described a new aspect of the Inhibitor of Apoptosis (IAP) family of proteins anti-apoptotic activity that involves the TAK1/JNK1 signal transduction pathway (1,2). Our findings suggest the existence of a novel mechanism that regulates the anti-apoptotic activity of IAPs that is separate from caspase inhibition but instead involves TAK1-mediated activation of JNK1. In a search for proteins involved in the XIAP/TAK1/JNK1 signaling pathway we isolated by yeast two-hybrid screening a novel X chromosome-linked IAP (XIAP)-interacting protein that we called ILPIP (hILP-Interacting Protein). Whereas ILPIP moderately activates JNK family members when expressed alone, it strongly enhances XIAP-mediated activation of JNK1, JNK2, and JNK3. The expression of a catalytically inactive mutant of TAK1 blocked XIAP/ILPIP synergistic activation of JNK1 thereby implicating TAK1 in this signaling pathway. ILPIP moderately protects against interleukin-1beta converting enzyme- or Fas-induced apoptosis and significantly potentiates the anti-apoptotic activity of XIAP. In vivo co-precipitation experiments show that both ILPIP and XIAP interact with TAK1 and tumor necrosis factor receptor-associated factor 6. Finally, expression of ILPIP did not affect the ability of XIAP to inhibit caspase activation, further supporting the idea that XIAP protection against apoptosis is achieved by two separate mechanisms: one requiring JNK1 activation and a second involving caspase inhibition.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
30454-62
pubmed:dateRevised
2011-11-2
pubmed:meshHeading
pubmed-meshheading:12048196-Amino Acid Sequence, pubmed-meshheading:12048196-Apoptosis, pubmed-meshheading:12048196-Base Sequence, pubmed-meshheading:12048196-Caspases, pubmed-meshheading:12048196-Cells, Cultured, pubmed-meshheading:12048196-Enzyme Activation, pubmed-meshheading:12048196-Humans, pubmed-meshheading:12048196-MAP Kinase Kinase Kinases, pubmed-meshheading:12048196-Mitogen-Activated Protein Kinase 8, pubmed-meshheading:12048196-Mitogen-Activated Protein Kinases, pubmed-meshheading:12048196-Molecular Sequence Data, pubmed-meshheading:12048196-Protein Kinases, pubmed-meshheading:12048196-Proteins, pubmed-meshheading:12048196-Signal Transduction, pubmed-meshheading:12048196-TNF Receptor-Associated Factor 6, pubmed-meshheading:12048196-Two-Hybrid System Techniques, pubmed-meshheading:12048196-X-Linked Inhibitor of Apoptosis Protein
pubmed:year
2002
pubmed:articleTitle
ILPIP, a novel anti-apoptotic protein that enhances XIAP-mediated activation of JNK1 and protection against apoptosis.
pubmed:affiliation
Department of Immunology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, CA 92037, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.