MUDENG is cleaved by caspase-3 during TRAIL-induced cell death

Biochem Biophys Res Commun. 2013 May 31;435(2):234-8. doi: 10.1016/j.bbrc.2013.04.075. Epub 2013 May 7.

Abstract

MUDENG, also known as AP5M1, was originally identified as an adaptin domain-containing gene that induced cell death in lymphoma cell lines. However, little is known of the mechanism responsible for MUDENG-mediated cell death. In this study, we investigated MUDENG changes during TRAIL-induced cell death. We found that MUDENG is rapidly processed in response to TRAIL in Jurkat and BJAB cells with time line similar to that of caspase activation. Caspase-3-mediated MUDENG cleavage was confirmed by an in vitro cleavage assay using recombinant active caspase proteins. Caspase cleavage sites (D276 and D290) were located in the adaptin domain of MUDENG, and cleaved MUDENG showed the reduced killing activity. These results suggest that the adaptin domain plays a key role in MUDENG-mediated cell death.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apoptosis / drug effects*
  • Apoptosis Regulatory Proteins / metabolism*
  • Caspase 3 / metabolism*
  • Enzyme Activation
  • HeLa Cells
  • Humans
  • Jurkat Cells
  • Neoplasms, Experimental
  • Protein Binding
  • TNF-Related Apoptosis-Inducing Ligand / pharmacology*

Substances

  • AP5M1 protein, human
  • Apoptosis Regulatory Proteins
  • TNF-Related Apoptosis-Inducing Ligand
  • TNFSF10 protein, human
  • Caspase 3