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Glucosamine Treatment-mediated O-GlcNAc Modification of Paxillin Depends on Adhesion State of Rat Insulinoma INS-1 Cells
DC Field | Value | Language |
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dc.contributor.author | Kwak, Tae Kyoung | - |
dc.contributor.author | Kim, Hyeonjung | - |
dc.contributor.author | Jung, Oisun | - |
dc.contributor.author | Lee, Sin-Ae | - |
dc.contributor.author | Kim, Hyun Jeong | - |
dc.contributor.author | Kim, Sung-Hoon | - |
dc.contributor.author | Lee, Jung Weon | - |
dc.contributor.author | Park, Ji-Min | - |
dc.contributor.author | Kang, Minkyung | - |
dc.date.accessioned | 2012-07-03T04:20:47Z | - |
dc.date.available | 2012-07-03T04:20:47Z | - |
dc.date.issued | 2010-11-12 | - |
dc.identifier.citation | JOURNAL OF BIOLOGICAL CHEMISTRY; Vol.285 46; 36021-36031 | ko_KR |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | https://hdl.handle.net/10371/78208 | - |
dc.description.abstract | 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 the phosphorylation and activities of focal adhesion molecules have been intensively studied, the effects of the O-GlcNAc modification of their Ser/Thr residues on cellular functions have been largely unexplored. We investigated the effects of O-GlcNAc modification on actin reorganization and morphology of rat insulinoma INS-1 cells after glucosamine (GlcN) treatment. We found that paxillin, a key adaptor molecule in focal adhesions, could be modified by O-GlcNAc in INS-1 cells treated with GlcN and in pancreatic islets from mice treated with streptozotocin. Ser-84/85 in human paxillin appeared to be modified by O-GlcNAc, which was inversely correlated to Ser-85 phosphorylation (Ser-83 in rat paxillin). Integrin-mediated adhesion signaling inhibited the GlcN treatment-enhanced O-GlcNAc modification of paxillin. Adherent INS-1 cells treated with GlcN showed restricted protrusions, whereas untreated cells showed active protrusions for multiple-elongated morphologies. Upon GlcN treatment, expression of a triple mutation (S83A/S84A/S85A) resulted in no further restriction of protrusions. Together these observations suggest that murine pancreatic beta cells may have restricted actin organization upon GlcN treatment by virtue of the O-GlcNAc modification of paxillin, which can be antagonized by a persistent cell adhesion process. | ko_KR |
dc.language.iso | en | ko_KR |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | ko_KR |
dc.title | Glucosamine Treatment-mediated O-GlcNAc Modification of Paxillin Depends on Adhesion State of Rat Insulinoma INS-1 Cells | ko_KR |
dc.type | Article | ko_KR |
dc.contributor.AlternativeAuthor | 곽태경 | - |
dc.contributor.AlternativeAuthor | 김현정 | - |
dc.contributor.AlternativeAuthor | 정외선 | - |
dc.contributor.AlternativeAuthor | 이신애 | - |
dc.contributor.AlternativeAuthor | 강민경 | - |
dc.contributor.AlternativeAuthor | 김현정 | - |
dc.contributor.AlternativeAuthor | 박지민 | - |
dc.contributor.AlternativeAuthor | 김성훈 | - |
dc.contributor.AlternativeAuthor | 이정원 | - |
dc.identifier.doi | 10.1074/jbc.M110.129601 | - |
dc.citation.journaltitle | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
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