A short acidic motif in ARF guards against mitochondrial dysfunction and melanoma susceptibility View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2014-12

AUTHORS

Claus Christensen, Jirina Bartkova, Martin Mistrík, Arnaldur Hall, Marina Krarup Lange, Ulrik Ralfkiær, Jiri Bartek, Per Guldberg

ABSTRACT

ARF is a small, highly basic protein that can be induced by oncogenic stimuli and exerts growth-inhibitory and tumour-suppressive activities through the activation of p53. Here we show that, in human melanocytes, ARF is cytoplasmic, constitutively expressed, and required for maintaining low steady-state levels of superoxide under conditions of mitochondrial dysfunction. This mitochondrial activity of ARF is independent of its known autophagic and p53-dependent functions, and involves the evolutionarily conserved acidic motif GHDDGQ, which exhibits weak homology to BCL-2 homology 3 (BH3) domains and mediates interaction with BCL-xL--an important regulator of mitochondrial redox homeostasis. Melanoma-predisposing CDKN2A germline mutations, which affect conserved glycine and aspartate residues within the GHDDGQ motif, impair the ability of ARF to control superoxide production and suppress growth of melanoma cells in vivo. These results reveal an important cell-protective function of ARF that links mitochondrial dysfunction and susceptibility to melanoma. More... »

PAGES

5348

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/ncomms6348

    DOI

    http://dx.doi.org/10.1038/ncomms6348

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1005416281

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/25370744


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