The Structural Function of Nestin in Cell Body Softening is Correlated with Cancer Cell Metastasis.
Actins
/ chemistry
Animals
CRISPR-Cas Systems
Cell Line, Tumor
Chemotaxis
Cytoskeleton
/ chemistry
Female
Humans
Mice
Mice, Inbred BALB C
Microscopy, Atomic Force
Neoplasm Invasiveness
Neoplasm Metastasis
/ pathology
Nestin
/ chemistry
Protein Domains
Sequence Analysis, RNA
Stress, Mechanical
Vimentin
/ chemistry
Atomic force microscope
Cancer metastasis
Cell stiffness
Intermediate filament
Nestin
Journal
International journal of biological sciences
ISSN: 1449-2288
Titre abrégé: Int J Biol Sci
Pays: Australia
ID NLM: 101235568
Informations de publication
Date de publication:
2019
2019
Historique:
received:
23
01
2019
accepted:
02
05
2019
entrez:
25
7
2019
pubmed:
25
7
2019
medline:
17
4
2020
Statut:
epublish
Résumé
Intermediate filaments play significant roles in governing cell stiffness and invasive ability. Nestin is a type VI intermediate filament protein that is highly expressed in several high-metastatic cancer cells. Although inhibition of nestin expression was shown to reduce the metastatic capacity of tumor cells, the relationship between this protein and the mechanism of cancer cell metastasis remains unclear. Here, we show that nestin softens the cell body of the highly metastatic mouse breast cancer cell line FP10SC2, thereby enhancing the metastasis capacity. Proximity ligation assay demonstrated increased binding between actin and vimentin in nestin knockout cells. Because nestin copolymerizes with vimentin and nestin has an extremely long tail domain in its C-terminal region, we hypothesized that the tail domain functions as a steric inhibitor of the vimentin-actin interaction and suppresses association of vimentin filaments with the cortical actin cytoskeleton, leading to reduced cell stiffness. To demonstrate this function, we mechanically pulled vimentin filaments in living cells using a nanoneedle modified with vimentin-specific antibodies under manipulation by atomic force microscopy (AFM). The tensile test revealed that mobility of vimentin filaments was increased by nestin expression in FP10SC2 cells.
Identifiants
pubmed: 31337983
doi: 10.7150/ijbs.33423
pii: ijbsv15p1546
pmc: PMC6643143
doi:
Substances chimiques
Actins
0
NES protein, human
0
Nes protein, mouse
0
Nestin
0
Vimentin
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1546-1556Déclaration de conflit d'intérêts
Competing Interests: The authors have declared that no competing interest exists.
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