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Acetylation regulates subcellular localization of eukaryotic translation initiation factor 5A (eIF5A) |
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| Authors: | Muhammad Ishfaq Kazuhiro Maeta Satoko Maeda Toru Natsume Akihiro Ito Minoru Yoshida |
| Affiliation: | a Chemical Genetic Laboratory, RIKEN Advanced Science Institute, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan b Chemical Genomics Research Group, RIKEN Advanced Science Institute, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan c Graduate School of Science and Engineering, Saitama University, 645 Shimo-Okubo, Sakura-ku, Saitama 338-8570, Japan d Department of Biotechnology, Kohat University of Science and Technology, Kohat, Khyber Pakhtunkhwa 26000, Pakistan e Biomedicinal Information Research Center, The National Institute of Advanced Industrial Science and Technology, Aomi 2-4-7, Koto-ku, Tokyo 135-0064, Japan f Japan Science and Technology Corporation, CREST Research Project, Kawaguchi, Saitama 332-0012, Japan |
| 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. |
| Keywords: | eIF5A Acetylation Hypusination Subcellular localization |
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