Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 538, Issue 2, Pages 64-70Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2013.07.027
Keywords
Apoptosis; Cell proliferation; IAP; Protein-protein interaction
Categories
Funding
- Fundacao para a Ciencia e a Tecnologia (FCT, Portugal
- ) [PEst-C/QUI/UI0062/2013, SFRH/BD/91067/2012, CENTRO-07-ST24-FEDER-002034]
- European Union [PEst-C/QUI/UI0062/2013, SFRH/BD/91067/2012, CENTRO-07-ST24-FEDER-002034]
- QREN [PEst-C/QUI/UI0062/2013, SFRH/BD/91067/2012, CENTRO-07-ST24-FEDER-002034]
- FEDER [PEst-C/QUI/UI0062/2013, SFRH/BD/91067/2012, CENTRO-07-ST24-FEDER-002034]
- COMPETE [PEst-C/QUI/UI0062/2013, SFRH/BD/91067/2012, CENTRO-07-ST24-FEDER-002034]
- Mais Centro- Programa Operacional Regional do Centro e Uniao Europeia/Fundo Europeu de Desenvolvimento Regional
- Fundação para a Ciência e a Tecnologia [SFRH/BD/91067/2012] Funding Source: FCT
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Survivin is a member of the inhibitor of apoptosis protein (IAP) family with crucial roles in apoptosis and cell cycle regulation. Post-translational modifications (PTMs) have a ubiquitous role in the regulation of a diverse range of proteins' cellular functions and survivin is not an exception. Phosphorylation, acetylation and ubiquitination seem to regulate survivin anti-apoptotic and mitotic roles and also its nuclear localization. In the present review we explore the role of PTMs on protein-protein interactions focused on survivin to provide new insights into the functions and cell localization of this IAP in pathophysiological conditions, which might help the envisioning of novel targeted therapies for diseases characterized by impaired survivin activity. Protein-protein interaction analysis was performed with bioinformatics tools based on published data aiming to give an integrated perspective of this IAP's role in the cell. (c) 2013 Elsevier Inc. All rights reserved.
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