HSP40 interacts with pyruvate kinase M2 and regulates glycolysis and cell proliferation in tumor cells.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 24658033.
- Also identified by DOI 10.1371/journal.pone.0092949 and PMC identifier 3962495.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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.
Medical subject headings
- HSP40 Heat-Shock Proteins
- Neoplasms
- Pyruvate Kinase