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FEBS Lett. 2012 Sep 21;586(19):3236-41. doi: 10.1016/j.febslet.2012.06.042. Epub 2012 Jul 4.

Acetylation regulates subcellular localization of eukaryotic translation initiation factor 5A (eIF5A).

Author information

1
Chemical Genetic Laboratory, RIKEN Advanced Science Institute, Wako, Saitama, Japan.

Erratum in

  • FEBS Lett. 2014 Aug 19;588(16):2754.

Abstract

Eukaryotic translation initiation factor 5A (eIF5A) is a protein subject to hypusination, which is essential for its function. eIF5A is also acetylated, but the role of that modification is unknown. Here, we report that acetylation regulates the subcellular localization of eIF5A. We identified PCAF as the major cellular acetyltransferase of eIF5A, and HDAC6 and SIRT2 as its major deacetylases. Inhibition of the deacetylases or impaired hypusination increased acetylation of eIF5A, leading to nuclear accumulation. As eIF5A is constitutively hypusinated under physiological conditions, we suggest that reversible acetylation plays a major role in controlling the subcellular localization of eIF5A.

PMID:
22771473
DOI:
10.1016/j.febslet.2012.06.042
[Indexed for MEDLINE]
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