The role of acetylation in the subcellular localization of an oncogenic isoform of translation factor eIF5A

Muhammad Ishfaq; Kazuhiro Maeta; Satoko Maeda; Toru Natsume; Akihiro Ito; Minoru Yoshida

doi:10.1271/bbb.120620

The role of acetylation in the subcellular localization of an oncogenic isoform of translation factor eIF5A

Biosci Biotechnol Biochem. 2012;76(11):2165-7. doi: 10.1271/bbb.120620. Epub 2012 Nov 7.

Authors

Muhammad Ishfaq¹, Kazuhiro Maeta, Satoko Maeda, Toru Natsume, Akihiro Ito, Minoru Yoshida

Affiliation

¹ Chemical Genetics Laboratory, RIKEN Advanced Science Institute, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.

PMID: 23132580
DOI: 10.1271/bbb.120620

Abstract

Mammalian cells express two isoforms of eIF5A, eIF5A1 and eIF5A2, but little is known about the function of eIF5A2. Here we report that eIF5A2 is reversibly acetylated at lysine-47. HDAC6 and SIRT2 were identified as the enzymes responsible for deacetylating eIF5A2. Analysis using acetylation-deficient mutants indicated that acetylation regulates the subcellular localization of eIF5A2.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Acetylation
Eukaryotic Translation Initiation Factor 5A
HeLa Cells
Humans
Intracellular Space / metabolism*
Oncogenes*
Peptide Initiation Factors / genetics
Peptide Initiation Factors / metabolism*
Protein Isoforms / genetics
Protein Isoforms / metabolism
Protein Transport
RNA-Binding Proteins / genetics
RNA-Binding Proteins / metabolism*

Substances

Peptide Initiation Factors
Protein Isoforms
RNA-Binding Proteins