The focal adhesion scaffold protein Hic-5 regulates vimentin organization in fibroblasts.
Actins
/ metabolism
Animals
Cell Adhesion
/ genetics
Cells, Cultured
Cytoskeletal Proteins
/ metabolism
Cytoskeleton
/ metabolism
DNA-Binding Proteins
/ metabolism
Fibroblasts
/ metabolism
Focal Adhesions
/ metabolism
Humans
Intermediate Filaments
/ metabolism
LIM Domain Proteins
/ metabolism
Mice
Mice, Knockout
Microtubules
/ metabolism
Phosphorylation
Transcription Factors
/ metabolism
Vimentin
/ metabolism
Journal
Molecular biology of the cell
ISSN: 1939-4586
Titre abrégé: Mol Biol Cell
Pays: United States
ID NLM: 9201390
Informations de publication
Date de publication:
01 12 2019
01 12 2019
Historique:
pubmed:
24
10
2019
medline:
23
6
2020
entrez:
24
10
2019
Statut:
ppublish
Résumé
Focal adhesion (FA)-stimulated reorganization of the F-actin cytoskeleton regulates cellular size, shape, and mechanical properties. However, FA cross-talk with the intermediate filament cytoskeleton is poorly understood. Genetic ablation of the FA-associated scaffold protein Hic-5 in mouse cancer-associated fibroblasts (CAFs) promoted a dramatic collapse of the vimentin network, which was rescued following EGFP-Hic-5 expression. Vimentin collapse correlated with a loss of detergent-soluble vimentin filament precursors and decreased vimentin S72/S82 phosphorylation. Additionally, fluorescence recovery after photobleaching analysis indicated impaired vimentin dynamics. Microtubule (MT)-associated EB1 tracking and Western blotting of MT posttranslational modifications indicated no change in MT dynamics that could explain the vimentin collapse. However, pharmacological inhibition of the RhoGTPase Cdc42 in Hic-5 knockout CAFs rescued the vimentin collapse, while pan-formin inhibition with SMIFH2 promoted vimentin collapse in Hic-5 heterozygous CAFs. Our results reveal novel regulation of vimentin organization/dynamics by the FA scaffold protein Hic-5 via modulation of RhoGTPases and downstream formin activity.
Identifiants
pubmed: 31644368
doi: 10.1091/mbc.E19-08-0442
pmc: PMC6880880
doi:
Substances chimiques
Actins
0
Cytoskeletal Proteins
0
DNA-Binding Proteins
0
LIM Domain Proteins
0
Tgfb1i1 protein, mouse
0
Transcription Factors
0
Vimentin
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
3037-3056Subventions
Organisme : NIDDK NIH HHS
ID : R01 DK120623
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM047607
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM131709
Pays : United States
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