Alterations to O‐GlcNAc cycling disrupt mitotic phosphorylation (555.16)

• DOI: 10.1096/fasebj.28.1_supplement.555.16
• Publication Date: 2021-06-15T17:31:27Z
• Authors: Stephen Whelan; Ee Phie Tan; Catherine Costello; Mark McComb; Chad Slawson
• Keywords: 0301 basic medicine; 03 medical and health sciences

O‐GlcNAc is a post‐translational modification (PTM) consisting of single N‐acetylglucosamine moiety attached to serine and threonine residues in nuclear cytoplasmic proteins. levels can cycle dynamically response hormones, nutrients, or stress order regulate multitude cellular processes. For instance cycling an important regulator mitosis. Recently, we demonstrated that cells with gain function either transferase (OGT) O‐GlcNAcase (OGA) have disrupted mitotic spindles exit defects. OGT/OGA caused the formation large poorly condensed spindle chromosomes, misaligned kinetochores, increase multipolar spindles. This phenotype was partially by disruption phosphorylation. In this current study, our objective determine how alterations disrupt phosphorylation cascades. We employed quantitative proteomics identify changes were able quantitate both protein expression as well PTM’s OGT OGA cells. identified over 1000 proteins whose PTM status altered aberrant O‐GlcNAcylation. These results demonstrate cross‐talk between modifications involved regulating progression suggest diseases one will also alter actions other PTM’s. Grant Funding Source : NIH‐NHLBI Contracts: HHSN268201000031C ‐ CPC; NIH Grants: P41 RR010888/GM104603 – MSR R21 HL107993 ;