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

Giovanni Scambia, Alessia Camperchioli, Marisa Mariani, Silvia Bartollino, Laura Petrella, Cristiano Ferlini, M Persico, N Orteca, S Shahabi, C. Fattorusso

Risultato della ricerca: Contributo in rivistaArticolo in rivista

13 Citazioni (Scopus)

Abstract

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.
Lingua originaleEnglish
pagine (da-a)850-857
Numero di pagine8
RivistaBIOCHIMICA ET BIOPHYSICA ACTA
Volume1813
DOI
Stato di pubblicazionePubblicato - 2011

Keywords

  • Humans
  • Immunoblotting
  • Kinetics
  • Models, Molecular
  • Protein Binding
  • Protein Multimerization
  • Proto-Oncogene Proteins c-bcl-2
  • Structure-Activity Relationship
  • Surface Plasmon Resonance

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