Investigation of the Bcl-2 multimerisation process: Structural and functional implications

Alessia Camperchioli, Marisa Mariani, Silvia Bartollino, Lella Petrella, Marco Persico, Nausicaa Orteca, Giovanni Scambia, Shohreh Shahabi, Cristiano Ferlini, Caterina Fattorusso*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


Bcl-2 plays a prominent role in regulating the function of mitochondria during respiration and in determining the threshold of apoptotic sensitivity. Despite its relevance, the mechanism through which these processes are achieved is still unknown. Using surface plasmon resonance technology to monitor Bcl-2 multimerisation we discovered that a simple dimeric model does not fit with experimental data. A molecular model of the experimentally observed Bcl-2 homomeric complex has been developed. Accordingly, using a panel of mutants we identified in the loop a critical region for the process of Bcl-2 multimerisation. Our results indicate that the Bcl-2 loop posttranscriptional changes can modulate its ability to make homo and hetero-complexes, ultimately leading to functional modulation, suggesting an intriguing relationship between the ability of Bcl-2 to form multimeric complexes and its multi-functional role as a membrane channel. This article is part of a Special Issue entitled: 11th European Symposium on Calcium.

Original languageEnglish (US)
Pages (from-to)850-857
Number of pages8
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Issue number5
StatePublished - May 2011


  • Apoptosis
  • Bcl-2 structure/function
  • Multimeric protein complexes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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