Survivin Acetylation: Affecting Apoptosis and Cancer

Thu, 06/02/2011 - 11:48

Survivin (BRIC5) is an inhibitor of apoptosis that also promotes cellular adaptation under stressful conditions and helps to regulate cell division. Recently, an antibody study by Dr. H Wang et al. at Brown University [PMID: 20826784] found that Survivin is acetylated at lysine residue 129, thereby affecting its subsequent subcellular localization. Specifically, acetylation promotes Survivin to homodimerize and localize in the nucleus, whereas deacetylation causes heterodimerization with CRM1 and export from the nucleus.

Additionally, the authors found that acetylation causes the nuclear-localized Survivin to bind to STAT3 and inhibit the activation of STAT3 target oncogenes. This was confirmed using a mutated 129K nucleotide to prevent survivin nuclear localization, thereby allowing STAT3 transactivation to proceed.

Immunocytochemistry/Immunofluorescence: Survivin [ac Lys129] Antibody

These results demonstrate that Survivin acetylation affects both the protein localization and its interaction with the tumor activator STAT3. Therefore, therapies controlling Survivin acetylation will potentially prove useful for treating STAT3-dependent tumors.

Novus Biologicals recently released the acetyl-specific-Survivin [acetyl K129] antibody used in this study. The antibody has been validated for Western blot and immunostaining human samples and will be useful for researchers studying survivin apoptosis pathways and STAT3 activated cancers.

Novus Biologicals offers many Survivin reagents for your research needs including:

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