PMID- 29463470
OWN - NLM
STAT- MEDLINE
DCOM- 20181005
LR  - 20240213
IS  - 0968-0004 (Print)
IS  - 0968-0004 (Linking)
VI  - 43
IP  - 4
DP  - 2018 Apr
TI  - Metabolic Kinases Moonlighting as Protein Kinases.
PG  - 301-310
LID - S0968-0004(18)30020-3 [pii]
LID - 10.1016/j.tibs.2018.01.006 [doi]
AB  - Protein kinases regulate every aspect of cellular activity, whereas metabolic 
      enzymes are responsible for energy production and catabolic and anabolic 
      processes. Emerging evidence demonstrates that some metabolic enzymes, such as 
      pyruvate kinase M2 (PKM2), phosphoglycerate kinase 1 (PGK1), ketohexokinase (KHK) 
      isoform A (KHK-A), hexokinase (HK), and nucleoside diphosphate kinase 1 and 2 
      (NME1/2), that phosphorylate soluble metabolites can also function as protein 
      kinases and phosphorylate a variety of protein substrates to regulate the Warburg 
      effect, gene expression, cell cycle progression and proliferation, apoptosis, 
      autophagy, exosome secretion, T cell activation, iron transport, ion channel 
      opening, and many other fundamental cellular functions. The elevated protein 
      kinase functions of these moonlighting metabolic enzymes in tumor development 
      make them promising therapeutic targets for cancer.
CI  - Copyright (c) 2018 Elsevier Ltd. All rights reserved.
FAU - Lu, Zhimin
AU  - Lu Z
AD  - Brain Tumor Center and Department of Neuro-Oncology, The University of Texas MD 
      Anderson Cancer Center, Houston, TX 77030, USA; Department of Molecular and 
      Cellular Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX 
      77030, USA; Cancer Biology Program, MD Anderson Cancer Center UTHealth Graduate 
      School of Biomedical Sciences, The University of Texas, Houston, TX 77030, USA. 
      Electronic address: zhiminlu@mdanderson.org.
FAU - Hunter, Tony
AU  - Hunter T
AD  - Molecular and Cell Biology Laboratory, Salk Institute for Biological Studies, La 
      Jolla, CA 92037, USA. Electronic address: hunter@salk.edu.
LA  - eng
GR  - R01 CA082683/CA/NCI NIH HHS/United States
GR  - P30 CA016672/CA/NCI NIH HHS/United States
GR  - R01 CA080100/CA/NCI NIH HHS/United States
GR  - R01 CA169603/CA/NCI NIH HHS/United States
GR  - R01 CA109035/CA/NCI NIH HHS/United States
GR  - R01 NS089754/NS/NINDS NIH HHS/United States
GR  - P50 CA127001/CA/NCI NIH HHS/United States
GR  - R01 CA204996/CA/NCI NIH HHS/United States
GR  - R01 CA194584/CA/NCI NIH HHS/United States
GR  - P30 CA014195/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Review
DEP - 20180217
PL  - England
TA  - Trends Biochem Sci
JT  - Trends in biochemical sciences
JID - 7610674
RN  - EC 2.7.- (Protein Kinases)
SB  - IM
MH  - Animals
MH  - Humans
MH  - Neoplasms/drug therapy/*enzymology/metabolism/*pathology
MH  - Protein Kinases/*metabolism
PMC - PMC5879014
MID - NIHMS946170
OTO - NOTNLM
OT  - metabolic enzymes
OT  - phosphorylation
OT  - protein kinase
EDAT- 2018/02/22 06:00
MHDA- 2018/10/06 06:00
PMCR- 2019/04/01
CRDT- 2018/02/22 06:00
PHST- 2017/11/21 00:00 [received]
PHST- 2018/01/15 00:00 [revised]
PHST- 2018/01/25 00:00 [accepted]
PHST- 2018/02/22 06:00 [pubmed]
PHST- 2018/10/06 06:00 [medline]
PHST- 2018/02/22 06:00 [entrez]
PHST- 2019/04/01 00:00 [pmc-release]
AID - S0968-0004(18)30020-3 [pii]
AID - 10.1016/j.tibs.2018.01.006 [doi]
PST - ppublish
SO  - Trends Biochem Sci. 2018 Apr;43(4):301-310. doi: 10.1016/j.tibs.2018.01.006. Epub 
      2018 Feb 17.