HSP60 Takes a Hit: Inhibition of Mitochondrial Protein Folding

Sundararajan Venkatesh; Carolyn K Suzuki

doi:10.1016/j.chembiol.2017.05.011

HSP60 Takes a Hit: Inhibition of Mitochondrial Protein Folding

Cell Chem Biol. 2017 May 18;24(5):543-545. doi: 10.1016/j.chembiol.2017.05.011.

Authors

Sundararajan Venkatesh¹, Carolyn K Suzuki²

Affiliations

¹ Department of Microbiology, Biochemistry and Molecular Genetics, New Jersey Medical School, Rutgers, The State University of New Jersey, Newark, NJ 07103, USA.
² Department of Microbiology, Biochemistry and Molecular Genetics, New Jersey Medical School, Rutgers, The State University of New Jersey, Newark, NJ 07103, USA. Electronic address: [email protected].

PMID: 28525768
DOI: 10.1016/j.chembiol.2017.05.011

Abstract

In this issue of Cell Chemical Biology,Wiechmann et al. (2017) identify mitochondrial chaperonin HSP60 as a direct target of myrtucommulone (MC), a nonprenylated acylphloroglucinol that is well known for its apoptotic activity in cancer cells. The authors propose MC as a chemical probe to study HSP60 biology and a potential chemotherapeutic agent in treating cancer and other HSP60-associated diseases.

MeSH terms

Antineoplastic Agents / pharmacology*
Chaperonin 60 / chemistry*
Mitochondrial Proteins / chemistry*
Phloroglucinol / analogs & derivatives
Phloroglucinol / pharmacology
Protein Folding / drug effects*

Substances

Antineoplastic Agents
Chaperonin 60
Mitochondrial Proteins
myrtucommulone A
Phloroglucinol