HSP40 interacts with pyruvate kinase M2 and regulates glycolysis and cell proliferation in tumor cells.
PLoS One
; 9(3): e92949, 2014.
Article
in En
| MEDLINE
| ID: mdl-24658033
ABSTRACT
Pyruvate kinase M2 (PKM2) is predominantly expressed in cancers, which is considered as a key regulator of the Warburg effect. In this study, HSP40 was identified as a novel binding partner of PKM2. HSP40-PKM2 association destabilized PKM2 protein through HSC70. In the presence of HSP40, PKM2 protein level and PKM2-mediated PDK1 expression were down-regulated. Moreover, HSP40 was involved in regulating glucose metabolism on PKM2 dependent way and at the mean time had an effect on mitochondrial oxygen respiration. In line with inhibition effect of HSP40 on glycolysis, the growth of cancer cells was inhibited by HSP40.Our data provided a new regulation mechanism of PKM2, which suggested a new therapeutic target for cancer therapy.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Pyruvate Kinase
/
HSP40 Heat-Shock Proteins
/
Neoplasms
Limits:
Humans
Language:
En
Journal:
PLoS One
Journal subject:
CIENCIA
/
MEDICINA
Year:
2014
Document type:
Article