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

• Type: Another Publication in an International Scientific Journal
• Date: 2013

Authors

Nogueira Ferreira, R (Author) Other; Vitorino, R (Author) Other; Ferreira Pinto, MJ (Author) FMUP; Ferreira, R (Author) Other; Henriques-Coelho, T (Author) FMUP

Journal

Title: Archives of Biochemistry and Biophysics

Vol. 538

Pages: 64-70

ISSN: 0003-9861

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 24 Citations

Scopus - 27 Citations

Other information

Authenticus ID: P-006-6JX

DOI: 10.1016/j.abb.2013.07.027

Abstract (EN): 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 7