Related Experiment Video
Updated: May 28, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
Published on: February 27, 2020
Acetylation of Prrp K150 regulates the subcellular localization
Kenta Sasaki1, Atsushi Suzuki, Satoshi Kagatsume
1Graduate School of Environment and Information Science, Yokohama National University, Tokiwadai, Hodogaya-ku, Yokohama 240-8501, Japan.
Abstract:
Posttranslational modifications of proteins have profound effects on many aspects of their function and have received much attention due to the importance of these processes in epigenetic regulation. In this study, we report that deleted azoospermia associated protein 1 (DAZAP1)/proline-rich RNA binding protein (Prrp), a multifunctional RNA binding protein which is essential for spermatogenesis and normal cell growth, is acetylated at Lysine 150 within its RNA binding domain. The acetylation is predominantly observed in nuclear Prrp, and the nonacetylated form is in cytoplasm. Considering that Prrp is a shuttling protein, we suggest that the acetylation cycle at Prrp K150 regulates nucleocytoplasmic transport in cells.
Related Concept Videos
Regulation of Nuclear Protein Sorting
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Directing Proteins to the Rough Endoplasmic Reticulum
Phase II Reactions: Acetylation Reactions
The substrates for acetylation are typically drugs or their metabolites with an amino, sulfonamide, or hydrazine functional group. Acetylation can occur at several points in the drug molecule, including primary, secondary, and...
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Chromatin Structure Regulates pre-mRNA Processing
The chromatin structure, especially...

