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Arch Biochem Biophys. 2013 Oct 15;538(2):64-70. doi: 10.1016/j.abb.2013.07.027. Epub 2013 Aug 11.

Exploring the role of post-translational modifications on protein-protein interactions with survivin.

Author information

1
QOPNA, Department of Chemistry, University of Aveiro, Aveiro, Portugal; Department of Physiology and Cardiothoracic Surgery, Faculty of Medicine, University of Porto, Porto, Portugal.

Abstract

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.

KEYWORDS:

Apoptosis; Cell proliferation; IAP; Protein–protein interaction

PMID:
23938875
DOI:
10.1016/j.abb.2013.07.027
[Indexed for MEDLINE]
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