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Cell Adhesion-Dependent Serine 85 Phosphorylation of Paxillin Modulates Focal Adhesion Formation and Haptotactic Migration via an Association with the C-Terminal Tail Domain of Talin.
Cited 13 time in
Web of Science
Cited 13 time in Scopus
- Authors
- Issue Date
- 2012-08
- Citation
- JOURNAL OF BIOLOGICAL CHEMISTRY Vol.287 No.33, pp. 27499-27509
- Keywords
- 복합학 ; cell adhesion ; paxillin ; talin ; phosphorlation
- Abstract
- Integrin-mediated adhesion to extracellular matrix proteins
is dynamically regulated during morphological changes and cell
migration. Upon cell adhesion, protein-protein interactions
among molecules at focal adhesions (FAs) play major roles in the
regulation of cell morphogenesis and migration. Although tyrosine
phosphorylation of paxillin is critically involved in adhesion-
mediated signaling, the significance of paxillin phosphorylation
at Ser-85 and the mechanism by which it regulates cell
migration remain unclear. In this study, we examined how
Ser-85 phosphorylation of paxillin affects FA formation and cell
migration. We found that paxillin phosphorylation at Ser-85
occurred during HeLa cell adhesion to collagen I and was concomitant
with tyrosine phosphorylation of both focal adhesion
kinase and talin. However, the non-phosphorylatable S85A
mutant of paxillin impaired cell spreading, FA turnover, and
migration toward collagen I but not toward serum. Furthermore,
whereas the (presumably indirect) interaction between
paxillin and the C-terminal tail of talin led to dynamic FAs at the
cell boundary, S85A paxillin did not bind talin and caused stabilized
FAs in the central region of cells. Together, these observations
suggest that cell adhesion-dependent Ser-85 phosphorylation
of paxillin is important for its interaction with talin and
regulation of dynamic FAs and cell migration.
- ISSN
- 0021-9258
- Language
- English
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