PMID- 25912078
OWN - NLM
STAT- MEDLINE
DCOM- 20150803
LR  - 20150527
IS  - 1873-135X (Electronic)
IS  - 0027-5107 (Linking)
VI  - 777
DP  - 2015 Jul
TI  - Functional interaction between hMYH and hTRADD in the TNF-alpha-mediated survival and 
      death pathways of HeLa cells.
PG  - 11-9
LID - S0027-5107(15)00086-X [pii]
LID - 10.1016/j.mrfmmm.2015.04.004 [doi]
AB  - The tumor necrosis factor (TNF) signaling pathway is a classical immune system 
      pathway that plays a key role in regulating cell survival and apoptosis. The TNF 
      receptor-associated death domain (TRADD) protein is recruited to the death domain 
      of TNF receptor 1 (TNFR1), where it interacts with TNF receptor-associated factor 
      2 (TRAF2) and receptor-interacting protein (RIP) for the induction of apoptosis, 
      necrosis, nuclear factor kappa-light-chain-enhancer of activated B cells (NFkappaB), 
      and mitogen-activated protein (MAP) kinase activation. In this study, we found 
      that the human MutY homolog (hMYH) interacted with human TRADD (hTRADD) via the 
      C-terminal domain of hMYH. Moreover, under conditions promoting TNF-alpha-induced 
      cell death or survival in HeLa cells, this interaction was weakened or enhanced, 
      respectively. The interaction between hMYH and hTRADD was important for signaling 
      pathways mediated by TNF-alpha. Our results also suggested that the hTRADD-hMYH 
      association was involved in the nuclear translocation of NFkappaB and formation of 
      the TNFR1-TRADD complex. Thus, this study identified a novel mechanism through 
      which the hMYH-hTRADD interaction may affect the TNF-alpha signaling pathway. 
      IMPLICATIONS: In HeLa cells, the hTRADD-hMYH interaction functioned in both cell 
      survival and apoptosis pathways following TNF-alpha stimulation.
CI  - Copyright (c) 2015 Elsevier B.V. All rights reserved.
FAU - Vy Tran, An Hue
AU  - Vy Tran AH
AD  - Department of Advanced Technology Fusion, Konkuk University, Hwayang-dong, 
      Gwangjin-gu, Seoul 143-701, Republic of Korea.
FAU - Hahm, Soo-Hyun
AU  - Hahm SH
AD  - Department of Advanced Technology Fusion, Konkuk University, Hwayang-dong, 
      Gwangjin-gu, Seoul 143-701, Republic of Korea.
FAU - Han, Se Hee
AU  - Han SH
AD  - Department of Advanced Technology Fusion, Konkuk University, Hwayang-dong, 
      Gwangjin-gu, Seoul 143-701, Republic of Korea.
FAU - Chung, Ji Hyung
AU  - Chung JH
AD  - Department of Applied Bioscience, College of Life Science, CHA University, 
      Gyeonggi-do 463-836, Republic of Korea.
FAU - Park, Geon Tae
AU  - Park GT
AD  - Cornell University, Ithaca, NY 14850, USA.
FAU - Han, Ye Sun
AU  - Han YS
AD  - College of Global Integrated Studies, Division of Interdisciplinary Studies, 
      Konkuk University, Hwayang-dong, Gwangjin-gu, Seoul 143-701, Republic of Korea. 
      Electronic address: yshan@konkuk.ac.kr.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20150415
PL  - Netherlands
TA  - Mutat Res
JT  - Mutation research
JID - 0400763
RN  - 0 (NF-kappa B)
RN  - 0 (Receptors, Tumor Necrosis Factor, Type I)
RN  - 0 (TNF Receptor-Associated Death Domain Protein)
RN  - 0 (Tumor Necrosis Factor-alpha)
RN  - EC 3.2.2.- (DNA Glycosylases)
RN  - EC 3.2.2.- (mutY adenine glycosylase)
SB  - IM
MH  - Apoptosis
MH  - DNA Glycosylases/genetics/*metabolism
MH  - HeLa Cells
MH  - Humans
MH  - NF-kappa B/genetics/metabolism
MH  - Necrosis
MH  - Protein Interaction Domains and Motifs
MH  - Receptors, Tumor Necrosis Factor, Type I/genetics/metabolism
MH  - Signal Transduction
MH  - TNF Receptor-Associated Death Domain Protein/genetics/*metabolism
MH  - Tumor Necrosis Factor-alpha/genetics/*metabolism
OTO - NOTNLM
OT  - Death-inducing signaling complex
OT  - MutY homolog (MYH)
OT  - NFkappaB nuclear translocation
OT  - TNFR-associated death domain (TRADD)
OT  - Tumor necrosis factor alpha (TNF-alpha)
EDAT- 2015/04/29 06:00
MHDA- 2015/08/04 06:00
CRDT- 2015/04/28 06:00
PHST- 2014/11/04 00:00 [received]
PHST- 2015/04/04 00:00 [revised]
PHST- 2015/04/06 00:00 [accepted]
PHST- 2015/04/28 06:00 [entrez]
PHST- 2015/04/29 06:00 [pubmed]
PHST- 2015/08/04 06:00 [medline]
AID - S0027-5107(15)00086-X [pii]
AID - 10.1016/j.mrfmmm.2015.04.004 [doi]
PST - ppublish
SO  - Mutat Res. 2015 Jul;777:11-9. doi: 10.1016/j.mrfmmm.2015.04.004. Epub 2015 Apr 
      15.