PMID- 28734548
OWN - NLM
STAT- MEDLINE
DCOM- 20171011
LR  - 20180319
IS  - 1873-135X (Electronic)
IS  - 0027-5107 (Linking)
VI  - 803-805
DP  - 2017 Oct
TI  - Ubiquitin-like modifications in the DNA damage response.
PG  - 56-75
LID - S0027-5107(17)30080-5 [pii]
LID - 10.1016/j.mrfmmm.2017.07.001 [doi]
AB  - Genomic DNA is damaged at an extremely high frequency by both endogenous and 
      environmental factors. An improper response to DNA damage can lead to genome 
      instability, accelerate the aging process and ultimately cause various human 
      diseases, including cancers and neurodegenerative disorders. The mechanisms that 
      underlie the cellular DNA damage response (DDR) are complex and are regulated at 
      many levels, including at the level of post-translational modification (PTM). 
      Since the discovery of ubiquitin in 1975 and ubiquitylation as a form of PTM in 
      the early 1980s, a number of ubiquitin-like modifiers (UBLs) have been 
      identified, including small ubiquitin-like modifiers (SUMOs), neural precursor 
      cell expressed, developmentally down-regulated 8 (NEDD8), interferon-stimulated 
      gene 15 (ISG15), human leukocyte antigen (HLA)-F adjacent transcript 10 (FAT10), 
      ubiquitin-fold modifier 1 (UFRM1), URM1 ubiquitin-related modifier-1 (URM1), 
      autophagy-related protein 12 (ATG12), autophagy-related protein 8 (ATG8), fan 
      ubiquitin-like protein 1 (FUB1) and histone mono-ubiquitylation 1 (HUB1). All of 
      these modifiers have known roles in the cellular response to various forms of 
      stress, and delineating their underlying molecular mechanisms and functions is 
      fundamental in enhancing our understanding of human disease and longevity. To 
      date, however, the molecular mechanisms and functions of these UBLs in the DDR 
      remain largely unknown. This review summarizes the current status of PTMs by UBLs 
      in the DDR and their implication in cancer diagnosis, therapy and drug discovery.
CI  - Copyright (c) 2017 Elsevier B.V. All rights reserved.
FAU - Wang, Zhifeng
AU  - Wang Z
AD  - Guangdong Key Laboratory of Genome Stability & Disease Prevention, Shenzhen 
      University School of Medicine, Shenzhen, Guangdong 518060, China.
FAU - Zhu, Wei-Guo
AU  - Zhu WG
AD  - Guangdong Key Laboratory of Genome Stability & Disease Prevention, Shenzhen 
      University School of Medicine, Shenzhen, Guangdong 518060, China.
FAU - Xu, Xingzhi
AU  - Xu X
AD  - Guangdong Key Laboratory of Genome Stability & Disease Prevention, Shenzhen 
      University School of Medicine, Shenzhen, Guangdong 518060, China; Beijing Key 
      Laboratory of DNA Damage Response, Capital Normal University College of Life 
      Sciences, Beijing 100048, China. Electronic address: Xingzhi.Xu@szu.edu.cn.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20170711
PL  - Netherlands
TA  - Mutat Res
JT  - Mutation research
JID - 0400763
RN  - 0 (ATG12 protein, human)
RN  - 0 (Autophagy-Related Protein 12)
RN  - 0 (Autophagy-Related Proteins)
RN  - 0 (Cytokines)
RN  - 0 (NEDD8 Protein)
RN  - 0 (NEDD8 protein, human)
RN  - 0 (Proteins)
RN  - 0 (SUMO-1 Protein)
RN  - 0 (UBD protein, human)
RN  - 0 (UFM1 protein, human)
RN  - 0 (Ubiquitins)
RN  - 0 (Urm1 protein, human)
RN  - 60267-61-0 (ISG15 protein, human)
SB  - IM
MH  - Autophagy-Related Protein 12/genetics/metabolism
MH  - Autophagy-Related Proteins/genetics/metabolism
MH  - Cytokines/genetics/metabolism
MH  - *DNA Damage
MH  - Down-Regulation
MH  - Drug Discovery
MH  - Humans
MH  - NEDD8 Protein
MH  - Neoplasms/drug therapy/genetics
MH  - Protein Processing, Post-Translational
MH  - Proteins/genetics/metabolism
MH  - SUMO-1 Protein/genetics/metabolism
MH  - *Ubiquitination
MH  - Ubiquitins/genetics/metabolism
OTO - NOTNLM
OT  - DNA damage response
OT  - FATylation
OT  - ISGylation
OT  - NEDDylation
OT  - SUMOylation
OT  - UFMylation
OT  - Ubiquitin-like modifiers (UBLs)
EDAT- 2017/07/25 06:00
MHDA- 2017/10/12 06:00
CRDT- 2017/07/24 06:00
PHST- 2017/04/17 00:00 [received]
PHST- 2017/06/03 00:00 [revised]
PHST- 2017/07/03 00:00 [accepted]
PHST- 2017/07/25 06:00 [pubmed]
PHST- 2017/10/12 06:00 [medline]
PHST- 2017/07/24 06:00 [entrez]
AID - S0027-5107(17)30080-5 [pii]
AID - 10.1016/j.mrfmmm.2017.07.001 [doi]
PST - ppublish
SO  - Mutat Res. 2017 Oct;803-805:56-75. doi: 10.1016/j.mrfmmm.2017.07.001. Epub 2017 
      Jul 11.