The concerted action of SEPT9 and EPLIN modulates the adhesion and migration of human fibroblasts
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Date
2024-05-07
Authors
Hecht, Matthias
Alber, Nane
Marhoffer, Pia
Johnsson, Nils
Gronemeyer, Thomas
Journal Title
Journal ISSN
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Publication Type
Wissenschaftlicher Artikel
Published in
Life Science Alliance, 2024
Abstract
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.
Description
Faculties
Fakultät für Naturwissenschaften
Institutions
Institut für Molekulare Genetik und Zellbiologie
Citation
DFG Project uulm
EU Project THU
Other projects THU
International PhD Programme in Molecular Medicine / IGradU, Universität Ulm
License
CC BY 4.0 International
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DOI external
DOI external
10.26508/lsa.202201686
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DFG Project THU
item.page.thu.projectEU
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Keywords
Cell Biology