title: Vimentin filament controls integrin α5β1-mediated cell adhesion by binding to integrin through its Ser38 residue.
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.
authors.affiliation: Department of Life Sciences, Korea University, Seoul, Korea.
authors.forename: Jiyoon
authors.initials: J
authors.lastname: Kim
authors.affiliation: Department of Anatomy, Brain Research Institute, and Brain Korea 21 PLUS Project for Medical Science, Yonsei University College of Medicine, Seoul, Korea.
authors.forename: Jungim
authors.initials: J
authors.lastname: Jang
authors.affiliation: Department of Life Sciences, Korea University, Seoul, Korea.|School of Biological Sciences, Seoul National University, Seoul, Korea.
authors.forename: Chansik
authors.initials: C
authors.lastname: Yang
authors.affiliation: Department of Life Sciences, Korea University, Seoul, Korea.
authors.forename: Eun Jin
authors.initials: EJ
authors.lastname: Kim
authors.affiliation: Department of Anatomy, Brain Research Institute, and Brain Korea 21 PLUS Project for Medical Science, Yonsei University College of Medicine, Seoul, Korea.
authors.forename: Hosung
authors.initials: H
authors.lastname: Jung
authors.affiliation: Department of Life Sciences, Korea University, Seoul, Korea. chungho@korea.ac.kr.
authors.forename: Chungho
authors.initials: C
authors.lastname: Kim
mesh_terms: D000818:Animals; D001665:Binding Sites / Q000187:drug effects; D016466:CHO Cells; D002448:Cell Adhesion; D002465:Cell Movement / Q000187:drug effects; D003412:Cricetulus; D005353:Fibronectins / Q000378:metabolism; D039081:Integrin alpha5beta1 / Q000737:chemistry / Q000378:metabolism*; D019012:Integrin beta1 / Q000737:chemistry / Q000378:metabolism*; D054259:Neural Tube / Q000378:metabolism; D011485:Protein Binding / Q000187:drug effects; D012694:Serine / Q000378:metabolism*; D014746:Vimentin / Q000737:chemistry* / Q000378:metabolism*; D054358:Withanolides / Q000494:pharmacology; D014981:Xenopus / Q000196:embryology* / Q000378:metabolism; D029867:Xenopus Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D005353:Fibronectins; D039081:Integrin alpha5beta1; D019012:Integrin beta1; D014746:Vimentin; D054358:Withanolides; D029867:Xenopus Proteins; D012694:Serine; C009684:withaferin A
keywords: cell adhesion; integrin; migration; vimentin; withaferin A