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The Role of Acetylation in the Subcellular Localization of an Oncogenic Isoform of Translation Factor eIF5A
Author(s) -
Muhammad Ishfaq,
Kazuhiro Maeta,
Satoko Maeda,
Tohru Natsume,
Akihiro Ito,
Minoru Yoshida
Publication year - 2012
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.120620
Subject(s) - acetylation , gene isoform , eukaryotic translation , subcellular localization , lysine , sirt2 , eukaryotic initiation factor , initiation factor , translation (biology) , biology , microbiology and biotechnology , chemistry , biochemistry , messenger rna , gene , sirtuin , amino acid
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.

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