The concerted action of SEPT9 and EPLIN modulates the adhesion and migration of human fibroblasts.
Humans
Septins
/ metabolism
Cell Movement
/ genetics
Cell Adhesion
Fibroblasts
/ metabolism
LIM Domain Proteins
/ metabolism
Focal Adhesions
/ metabolism
Cytoskeletal Proteins
/ metabolism
Pseudopodia
/ metabolism
Actin Cytoskeleton
/ metabolism
Cell Line
Actins
/ metabolism
Stress Fibers
/ metabolism
Journal
Life science alliance
ISSN: 2575-1077
Titre abrégé: Life Sci Alliance
Pays: United States
ID NLM: 101728869
Informations de publication
Date de publication:
Jul 2024
Jul 2024
Historique:
received:
23
08
2022
revised:
29
04
2024
accepted:
29
04
2024
medline:
9
5
2024
pubmed:
9
5
2024
entrez:
8
5
2024
Statut:
epublish
Résumé
Septins are cytoskeletal proteins that participate in cell adhesion, migration, and polarity establishment. The septin subunit SEPT9 directly interacts with the single LIM domain of epithelial protein lost in neoplasm (EPLIN), an actin-bundling protein. Using a human SEPT9 KO fibroblast cell line, we show that cell adhesion and migration are regulated by the interplay between both proteins. The low motility of SEPT9-depleted cells could be partly rescued by increased levels of EPLIN. The normal organization of actin-related filopodia and stress fibers was directly dependent on the expression level of SEPT9 and EPLIN. Increased levels of SEPT9 and EPLIN enhanced the size of focal adhesions in cell protrusions, correlating with stabilization of actin bundles. Conversely, decreased levels had the opposite effect. Our work thus establishes the interaction between SEPT9 and EPLIN as an important link between the septin and the actin cytoskeleton, influencing cell adhesion, motility, and migration.
Identifiants
pubmed: 38719752
pii: 7/7/e202201686
doi: 10.26508/lsa.202201686
pii:
doi:
Substances chimiques
Septins
EC 3.6.1.-
SEPTIN9 protein, human
EC 3.6.1.-
LIMA1 protein, human
0
LIM Domain Proteins
0
Cytoskeletal Proteins
0
Actins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© 2024 Hecht et al.