Abstract
Protein phosphorylation is the most common post-translational modification of proteins and functions as a molecular switch for their regulation. This modification is reversibly regulated by protein kinases and phosphatases. In most cases, the phosphorylation of enzymes positively or negatively regulates enzyme activity. However, we found that the phosphorylation of DDHD1 phospholipase A1 (PLA1) did not affect PLA1 activity. Integrated analyses, including phospho-proteomics, Phos-tag SDS-PAGE, PLA1 enzyme assays, and immunofluorescent microscopy, revealed the subcellular localization of DDHD1 without greatly affecting its PLA1 activity. Our findings may contribute to understanding rare clinical cases that concern the implications of protein phosphorylation.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
