Abstract
During mitosis, proteins undergo a variety of post‐translational modifications (PTM) in order to alter function and localization. Our objective is to determine the interplay between O‐GlcNAcylation and phosphorylation on proteins during mitotic progression. O‐GlcNAc is the attachment of a single N‐acetylglucosamine moiety to serine and threonine residues in nuclear and cytoplasmic proteins. O‐GlcNAc transferase (OGT) adds the modification and O‐GlcNAcase (OGA) removes the modification. O‐GlcNAc is similar to phosphorylation as both modifications are responsive to the extracellular environment, nutrients, and growth hormones. Using SILAC (Stable Isotope Labeling of Amino Acids in Cell culture) labeling, we are able to quantitate differences in cells with either an OGT or OGA gain of function. Combined samples were digested and fractionated to enrich for O‐GlcNAcylated or phosphorylated peptides. We identified numerous proteins whose expression or phosphorylation status was altered by aberrant O‐GlcNAcylation. These results demonstrate the interconnectedness of these two modifications in regulating mitotic progression. Furthermore, these data suggest that diseases that disrupt one PTM will also alter the actions of the other PTM.
Sign-in/Register to access full text options 
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.
