Abstract:
:Regulation of integrin affinity for its ligand is essential for cell adhesion and migration. Here, we found that direct interaction of vimentin with integrin β1 can enhance binding of integrin α5β1 to its ligand, fibronectin. Conversely, blocking the interaction reduced fibronectin binding, cell migration on a fibronectin-coated surface, and neural tube closure during Xenopus embryogenesis. We also found that withaferin A (WFA), a natural compound known to inhibit vimentin function, can suppress the vimentin-integrin interaction and abolish fibronectin binding. Finally, we identified Ser38 of vimentin as a critical residue for integrin binding. Our results suggest that phosphorylation of vimentin at Ser38 may regulate the integrin-ligand interaction, thus providing a molecular basis for antivimentin therapeutic strategies.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Kim J,Jang J,Yang C,Kim EJ,Jung H,Kim Cdoi
10.1002/1873-3468.12430subject
Has Abstractpub_date
2016-10-01 00:00:00pages
3517-3525issue
20eissn
0014-5793issn
1873-3468journal_volume
590pub_type
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