Exploring the role of post-translational modifications on protein-protein interactions with survivin.
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.
QOPNA, Department of Chemistry, University of Aveiro, Aveiro, Portugal; Department of Physiology and Cardiothoracic Surgery, Faculty of Medicine, University of Porto, Porto, Portugal.
Rita
R
Nogueira-Ferreira
Rui
R
Vitorino
Manuel J
MJ
Ferreira-Pinto
Rita
R
Ferreira
Tiago
T
Henriques-Coelho
D000818:Animals; D017209:Apoptosis; D049109:Cell Proliferation; D006801:Humans; D051034:Inhibitor of Apoptosis Proteins / Q000032:analysis* / Q000235:genetics / Q000378:metabolism*; D060066:Protein Interaction Maps; D011499:Protein Processing, Post-Translational; D000077022:Survivin
C107489:BIRC5 protein, human; D051034:Inhibitor of Apoptosis Proteins; D000077022:Survivin
Apoptosis; Cell proliferation; IAP; Protein–protein interaction