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Glucosamine treatment-mediated O-GlcNAc modification of paxillin depends on adhesion state of rat insulinoma INS-1 cells.

Cited 11 time in Web of Science Cited 12 time in Scopus
Authors
Kwak, Tae Kyoung; Kim, Hyeonjung; Jung, Oisun; Lee, Sin-Ae; Kang, Minkyung; Kim, Hyun Jeong; Park, Ji-Min; Kim, Sung-Hoon; Lee, Jung Weon
Issue Date
2010-11
Publisher
American Society for Biochemistry and Molecular Biology
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY Vol.285 No.46, pp. 36021-36031
Keywords
의약학paxillinposttranslational modificationcell protrusiondiabetes
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 adhesiondependent
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 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.
ISSN
0021-9258
Language
English
URI
https://hdl.handle.net/10371/82061
DOI
https://doi.org/10.1074/jbc.M110.129601
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College of Pharmacy (약학대학)Dept. of Pharmacy (약학과)Journal Papers (저널논문_약학과)
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