Receptor interacting protein is ubiquitinated by cellular inhibitor of apoptosis proteins (c-IAP1 and c-IAP2) in vitro

Research output: Contribution to journalArticle

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Abstract

Receptor interacting protein (RIP) is recruited to tumor necrosis factor-α receptor 1 (TNFR1) complex upon stimulation and plays a crucial role in the receptor-mediated NF-κB activation. Among the components of the TNFR1 complex are proteins that possess ubiquitin-protein isopeptide ligase (E3) activities, such as TNFR1-associated factor 2 (TRAF2), cellular inhibitor of apoptosis proteins (c-IAPs) namely, c-IAP1 and c-IAP2. Here, we showed that ectopically expressed RIP is ubiquitinated, and either the intermediate or death domain of RIP is required for this modification. Expression of c-IAP1 and c-IAP2 decreased the steady-state level of RIP, which was blocked by inhibition of the 26S proteasome. RIP degradation requires intact c-IAP2 containing the RING domain. Our in vitro ubiquitination assay revealed that while TRAF2 had no effect, both c-IAP1 and c-IAP2-mediated RIP ubiquitination with similar efficiency, indicating that c-IAPs can function as E3 toward RIP.

Original languageEnglish
Pages (from-to)151-156
Number of pages6
JournalFEBS Letters
Volume566
Issue number1-3
DOIs
Publication statusPublished - 2004 May 21

Fingerprint

Receptor-Interacting Protein Serine-Threonine Kinases
Inhibitor of Apoptosis Proteins
Tumor Necrosis Factor Receptors
Ubiquitination
Tumor Necrosis Factor Receptor-Associated Peptides and Proteins
Receptors, Tumor Necrosis Factor, Type I
Death Domain Receptors
Ubiquitin-Protein Ligases
In Vitro Techniques
Proteolysis
Assays
Chemical activation
Degradation

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

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title = "Receptor interacting protein is ubiquitinated by cellular inhibitor of apoptosis proteins (c-IAP1 and c-IAP2) in vitro",
abstract = "Receptor interacting protein (RIP) is recruited to tumor necrosis factor-α receptor 1 (TNFR1) complex upon stimulation and plays a crucial role in the receptor-mediated NF-κB activation. Among the components of the TNFR1 complex are proteins that possess ubiquitin-protein isopeptide ligase (E3) activities, such as TNFR1-associated factor 2 (TRAF2), cellular inhibitor of apoptosis proteins (c-IAPs) namely, c-IAP1 and c-IAP2. Here, we showed that ectopically expressed RIP is ubiquitinated, and either the intermediate or death domain of RIP is required for this modification. Expression of c-IAP1 and c-IAP2 decreased the steady-state level of RIP, which was blocked by inhibition of the 26S proteasome. RIP degradation requires intact c-IAP2 containing the RING domain. Our in vitro ubiquitination assay revealed that while TRAF2 had no effect, both c-IAP1 and c-IAP2-mediated RIP ubiquitination with similar efficiency, indicating that c-IAPs can function as E3 toward RIP.",
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Receptor interacting protein is ubiquitinated by cellular inhibitor of apoptosis proteins (c-IAP1 and c-IAP2) in vitro. / Park, Sun Mi; Yoon, Jong Bok; Lee, Tae H.

In: FEBS Letters, Vol. 566, No. 1-3, 21.05.2004, p. 151-156.

Research output: Contribution to journalArticle

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AB - Receptor interacting protein (RIP) is recruited to tumor necrosis factor-α receptor 1 (TNFR1) complex upon stimulation and plays a crucial role in the receptor-mediated NF-κB activation. Among the components of the TNFR1 complex are proteins that possess ubiquitin-protein isopeptide ligase (E3) activities, such as TNFR1-associated factor 2 (TRAF2), cellular inhibitor of apoptosis proteins (c-IAPs) namely, c-IAP1 and c-IAP2. Here, we showed that ectopically expressed RIP is ubiquitinated, and either the intermediate or death domain of RIP is required for this modification. Expression of c-IAP1 and c-IAP2 decreased the steady-state level of RIP, which was blocked by inhibition of the 26S proteasome. RIP degradation requires intact c-IAP2 containing the RING domain. Our in vitro ubiquitination assay revealed that while TRAF2 had no effect, both c-IAP1 and c-IAP2-mediated RIP ubiquitination with similar efficiency, indicating that c-IAPs can function as E3 toward RIP.

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