DNA damage-induced translocation of S100A11 into the nucleus regulates cell proliferation.

ABSTRACT:

Background

Proteins are able to react in response to distinct stress stimuli by alteration of their subcellular distribution. The stress-responsive protein S100A11 belongs to the family of multifunctional S100 proteins which have been implicated in several key biological processes. Previously, we have shown that S100A11 is directly involved in DNA repair processes at damaged chromatin in the nucleus. To gain further insight into the underlying mechanism subcellular trafficking of S100A11 in response to DNA damage was analyzed.

Results

We show that DNA damage induces a nucleolin-mediated translocation of S100A11 from the cytoplasm into the nucleus. This translocation is impeded by inhibition of the phosphorylation activity of PKCα. Translocation of S100A11 into the nucleus co

SUBMITTER: Gorsler T 

PROVIDER: S-EPMC3018407 | biostudies-literature | 2010 Dec

REPOSITORIES: biostudies-literature