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