PMID- 30799306
OWN - NLM
STAT- MEDLINE
DCOM- 20191016
LR  - 20211204
IS  - 1083-351X (Electronic)
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 294
IP  - 14
DP  - 2019 Apr 5
TI  - Aminoacyl-tRNA synthetases and tRNAs in human disease: an introduction to the JBC 
      Reviews thematic series.
PG  - 5292-5293
LID - 10.1074/jbc.REV119.007721 [doi]
AB  - Aminoacyl-tRNA synthetases (ARSs) catalyze the attachment of specific amino acids 
      to cognate tRNAs for use in protein synthesis. This historical function of ARSs 
      and tRNAs is fairly well understood. However, ARSs and tRNAs also perform 
      noncanonical functions that are continuing to be unveiled at a rapid pace. The 
      expanded functions of these essential molecules of life range from roles in 
      retroviral replication to stimulation of mammalian target of rapamycin (mTOR) 
      activity; DNA repair, splicing, and transcriptional and translational regulation; 
      and other aspects of cellular homeostasis. Furthermore, mutations in tRNAs and 
      synthetases are known to drive human maladies, such as the neurodegenerative 
      disorder Charcot-Marie-Tooth disease along with other central nervous system 
      dysfunctions and cancer. This series of reviews focuses on the diseases that 
      result from natural variations in human cytoplasmic tRNAs, as well as from 
      mutations in mitochondrial tRNAs and ARSs. Ultimately, the exciting work in this 
      rapidly emerging area may lead to new therapies for microbial and parasitic 
      infections, cancer, and neurodegenerative diseases.
CI  - (c) 2019 Musier-Forsyth.
FAU - Musier-Forsyth, Karin
AU  - Musier-Forsyth K
AUID- ORCID: 0000-0002-0354-4172
AD  - From the Department of Chemistry and Biochemistry, Center for RNA Biology, and 
      Center for Retroviral Research, The Ohio State University, Columbus, Ohio 43210 
      musier-forsyth.1@osu.edu.
LA  - eng
PT  - Introductory Journal Article
DEP - 20190224
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Neoplasm Proteins)
RN  - 0 (RNA, Neoplasm)
RN  - 9014-25-9 (RNA, Transfer)
RN  - EC 2.7.1.1 (MTOR protein, human)
RN  - EC 2.7.11.1 (TOR Serine-Threonine Kinases)
RN  - EC 6.1.1.- (Amino Acyl-tRNA Synthetases)
SB  - IM
MH  - Amino Acyl-tRNA Synthetases/genetics/*metabolism
MH  - Charcot-Marie-Tooth Disease/genetics/*metabolism/pathology
MH  - DNA Repair
MH  - Humans
MH  - *Mutation
MH  - Neoplasm Proteins/genetics/*metabolism
MH  - Neoplasms/genetics/*metabolism/pathology
MH  - RNA, Neoplasm/genetics/metabolism
MH  - RNA, Transfer/genetics/metabolism
MH  - Retroviridae/physiology
MH  - Retroviridae Infections/genetics/*metabolism
MH  - TOR Serine-Threonine Kinases/genetics/metabolism
MH  - Virus Replication
PMC - PMC6462500
OTO - NOTNLM
OT  - Charcot-Marie-Tooth disease (CMT)
OT  - aminoacyl tRNA synthetase
OT  - cancer
OT  - human disease
OT  - human immunodeficiency virus (HIV)
OT  - mitochondrial tRNA-synthetases
OT  - multisynthetase complex
OT  - neurological disease
OT  - therapeutic targets
OT  - transfer RNA (tRNA)
COIS- The author declares that she has no conflicts of interest with the contents of 
      this article.
EDAT- 2019/02/26 06:00
MHDA- 2019/10/17 06:00
PMCR- 2019/02/24
CRDT- 2019/02/26 06:00
PHST- 2019/02/26 06:00 [pubmed]
PHST- 2019/10/17 06:00 [medline]
PHST- 2019/02/26 06:00 [entrez]
PHST- 2019/02/24 00:00 [pmc-release]
AID - S0021-9258(20)35492-2 [pii]
AID - REV119.007721 [pii]
AID - 10.1074/jbc.REV119.007721 [doi]
PST - ppublish
SO  - J Biol Chem. 2019 Apr 5;294(14):5292-5293. doi: 10.1074/jbc.REV119.007721. Epub 
      2019 Feb 24.