Subcellular localization determines the delicate balance between the anti- and pro-apoptotic activity of Livin

Boaz Nachmias, Itay Lazar, Meital Elmalech, Ihab Abed-El-Rahaman, Yaqoub Asshab, Ofer Mandelboim, Riki Perlman, Dina Ben-Yehuda*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

26 Scopus citations


Livin is a member of the Inhibitor of Apoptosis Protein family which inhibits apoptosis induced by a variety of stimuli. We previously identified Livin and demonstrated that following apoptotic stimuli, Livin is cleaved by effector caspases to produce a truncated form with paradoxical pro-apoptotic activity. In the present study, we reveal that while full-length Livin shows diffuse cytoplasmic localization, truncated Livin (tLivin) is found in a peri-nuclear distribution with marked localization to the Golgi apparatus. Using mutation analysis, we identified two domains that are crucial for the pro-apoptotic activity of tLivin: the N-terminal region of tLivin which is exposed by cleavage, and the RING domain. We demonstrate that, of the N-terminal sequence, only the first N-terminal glycine residue dictates the peri-nuclear distribution of tLivin. However, while the perinuclear localization of tLivin is essential, it is not sufficient for tLivin to exert its pro-apoptotic function. Once tLivin is properly localized, an intact RING domain enables its pro-apoptotic function.

Original languageAmerican English
Pages (from-to)1129-1142
Number of pages14
JournalApoptosis : an international journal on programmed cell death
Issue number7
StatePublished - Jul 2007


  • Apoptosis
  • Golgi apparatus
  • IAPs
  • Livin
  • RING domain
  • Subcellular localization


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