The Role of Acetylation in the Subcellular Localization of an Oncogenic Isoform of Translation Factor eIF5A

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-defici...

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Veröffentlicht in:	Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2012, Vol.76 (11), p.2165-2167
Hauptverfasser:	ISHFAQ, Muhammad, MAETA, Kazuhiro, MAEDA, Satoko, NATSUME, Toru, ITO, Akihiro, YOSHIDA, Minoru
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetylation Biological and medical sciences eIF5A2 Eukaryotic Translation Initiation Factor 5A Fundamental and applied biological sciences. Psychology HDAC HeLa Cells Humans hypusination 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 subcellular localization
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Zusammenfassung:	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.
ISSN:	0916-8451 1347-6947
DOI:	10.1271/bbb.120620