Glucosamine Treatment-mediated O-GlcNAc Modification of Paxillin Depends on Adhesion State of Rat Insulinoma INS-1 Cells

• DOI: 10.1074/jbc.m110.129601
• Publication Date: 2010-09-10T04:14:43Z
• Authors: Tae Kyoung Kwak; Hyeonjung Kim; Oisun Jung; Sin-Ae Lee; Minkyung Kang; Hyun Jeong Kim; Ji-Min Park; Sung-Hoon Kim; Jung Weon Lee
• Keywords: Paxillin

Protein-protein interactions and/or signaling activities at focal adhesions, where integrin-mediated adhesion to extracellular matrix occurs, are critical for the regulation of adhesion-dependent cellular functions. Although phosphorylation and molecules have been intensively studied, effects O-GlcNAc modification their Ser/Thr residues on functions largely unexplored. We investigated actin reorganization morphology rat insulinoma INS-1 cells after glucosamine (GlcN) treatment. found that paxillin, a key adaptor molecule in could be modified by treated with GlcN pancreatic islets from mice streptozotocin. Ser-84/85 human paxillin appeared O-GlcNAc, which was inversely correlated Ser-85 (Ser-83 paxillin). Integrin-mediated inhibited treatment-enhanced paxillin. Adherent showed restricted protrusions, whereas untreated active protrusions multiple-elongated morphologies. Upon treatment, expression triple mutation (S83A/S84A/S85A) resulted no further restriction protrusions. Together these observations suggest murine β may organization upon treatment virtue can antagonized persistent cell process.