PMID- 22297296
OWN - NLM
STAT- MEDLINE
DCOM- 20120724
LR  - 20211021
IS  - 2041-4889 (Electronic)
VI  - 3
IP  - 2
DP  - 2012 Feb 2
TI  - CLIPR-59 regulates TNF-alpha-induced apoptosis by controlling ubiquitination of RIP1.
PG  - e264
LID - 10.1038/cddis.2012.3 [doi]
AB  - Tumor necrosis factor-alpha (TNF-alpha) has important roles in several immunological 
      events by regulating apoptosis and transcriptional activation of cytokine genes. 
      Intracellular signaling mediated by TNF-receptor-type 1 (TNFR1) is constituted by 
      two sequential protein complexes: Complex-I containing the receptor and 
      Complex-II-containing Caspase-8. Protein modifications, particularly 
      ubiquitination, are associated with the regulation of the formation of these 
      complexes. However, the underlying mechanisms remain poorly defined. Here, we 
      identified CLIP-170-related 59 kDa protein (CLIPR-59) as a novel adaptor protein 
      for TNFR1. Experimental reduction of CLIPR-59 levels prevented induction of 
      apoptosis and activation of caspases in the context of TNF-alpha signaling. CLIPR-59 
      binds TNFR1 but dissociates in response to TNF-alpha stimulation. However, CLIPR-59 
      is also involved in and needed for the formation of Complex-II. Moreover, 
      CLIPR-59 regulates TNF-alpha-induced ubiquitination of receptor-interacting protein 1 
      (RIP1) by its association with CYLD, a de-ubiquitinating enzyme. These findings 
      suggest that CLIPR-59 modulates ubiquitination of RIP1, resulting in the 
      formation of Complex-II and thus promoting Caspase-8 activation to induce 
      apoptosis by TNF-alpha.
FAU - Fujikura, D
AU  - Fujikura D
AD  - Department of Bioresources, Hokkaido University Research Center for Zoonosis 
      Control, North-20, West-10, Kita-ku, Sapporo, Hokkaido 001-0020, Japan. 
      d-fuji@czc.hokudai.ac.jp
FAU - Ito, M
AU  - Ito M
FAU - Chiba, S
AU  - Chiba S
FAU - Harada, T
AU  - Harada T
FAU - Perez, F
AU  - Perez F
FAU - Reed, J C
AU  - Reed JC
FAU - Uede, T
AU  - Uede T
FAU - Miyazaki, T
AU  - Miyazaki T
LA  - eng
GR  - P01 CA069381/CA/NCI NIH HHS/United States
GR  - CA69381/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20120202
PL  - England
TA  - Cell Death Dis
JT  - Cell death & disease
JID - 101524092
RN  - 0 (AGFG1 protein, human)
RN  - 0 (CLIP3 protein, human)
RN  - 0 (Microtubule-Associated Proteins)
RN  - 0 (Nuclear Pore Complex Proteins)
RN  - 0 (RNA, Small Interfering)
RN  - 0 (RNA-Binding Proteins)
RN  - 0 (Receptors, Tumor Necrosis Factor, Type I)
RN  - 0 (Tumor Necrosis Factor-alpha)
RN  - 0 (Tumor Suppressor Proteins)
RN  - EC 3.4.19.12 (CYLD protein, human)
RN  - EC 3.4.19.12 (Deubiquitinating Enzyme CYLD)
RN  - EC 3.4.22.- (Caspase 8)
SB  - IM
MH  - Apoptosis/drug effects/*genetics
MH  - Caspase 8/genetics/metabolism
MH  - Deubiquitinating Enzyme CYLD
MH  - Gene Expression Regulation
MH  - HEK293 Cells
MH  - HeLa Cells
MH  - Humans
MH  - Microtubule-Associated Proteins/*genetics/metabolism
MH  - Nuclear Pore Complex Proteins/*genetics/metabolism
MH  - Protein Binding/drug effects
MH  - RNA, Small Interfering/genetics
MH  - RNA-Binding Proteins/*genetics/metabolism
MH  - Receptors, Tumor Necrosis Factor, Type I/genetics/metabolism
MH  - Signal Transduction
MH  - Tumor Necrosis Factor-alpha/pharmacology
MH  - Tumor Suppressor Proteins/genetics/metabolism
MH  - Two-Hybrid System Techniques
MH  - Ubiquitination
PMC - PMC3288345
EDAT- 2012/02/03 06:00
MHDA- 2012/07/25 06:00
PMCR- 2012/02/01
CRDT- 2012/02/03 06:00
PHST- 2012/02/03 06:00 [entrez]
PHST- 2012/02/03 06:00 [pubmed]
PHST- 2012/07/25 06:00 [medline]
PHST- 2012/02/01 00:00 [pmc-release]
AID - cddis20123 [pii]
AID - 10.1038/cddis.2012.3 [doi]
PST - epublish
SO  - Cell Death Dis. 2012 Feb 2;3(2):e264. doi: 10.1038/cddis.2012.3.