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

Sun Mi Park; Jong Bok Yoon; Tae H. Lee

doi:10.1016/j.febslet.2004.04.021

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

Sun Mi Park, Jong Bok Yoon, Tae H. Lee

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71 Citations (Scopus)

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 language	English
Pages (from-to)	151-156
Number of pages	6
Journal	FEBS Letters
Volume	566
Issue number	1-3
DOIs	https://doi.org/10.1016/j.febslet.2004.04.021
Publication status	Published - 2004 May 21

Bibliographical note

Funding Information:
We thank H.S. Park, E.Y. Ko, and E.H. Shin for supplying reagents (E1, E2, and Flag-c-IAP2). This work was supported by grants from the Korean Ministry of Science and Technology through 21C Frontier Project and from the basic research program (R02-2002-000-00043-0) of the Korea Science and Engineering Foundation. S.-M.P. is a recipient of a predoctoral fellowship provided by the Korea Research Foundation.

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2004.04.021

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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.",

author = "Park, {Sun Mi} and Yoon, {Jong Bok} and Lee, {Tae H.}",

note = "Funding Information: We thank H.S. Park, E.Y. Ko, and E.H. Shin for supplying reagents (E1, E2, and Flag-c-IAP2). This work was supported by grants from the Korean Ministry of Science and Technology through 21C Frontier Project and from the basic research program (R02-2002-000-00043-0) of the Korea Science and Engineering Foundation. S.-M.P. is a recipient of a predoctoral fellowship provided by the Korea Research Foundation.",

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N1 - Funding Information: We thank H.S. Park, E.Y. Ko, and E.H. Shin for supplying reagents (E1, E2, and Flag-c-IAP2). This work was supported by grants from the Korean Ministry of Science and Technology through 21C Frontier Project and from the basic research program (R02-2002-000-00043-0) of the Korea Science and Engineering Foundation. S.-M.P. is a recipient of a predoctoral fellowship provided by the Korea Research Foundation.

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N2 - 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.

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

Abstract

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