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LSP1‐myosin1e bimolecular complex regulates focal adhesion dynamics and cell migration
Author(s) -
Schäringer Katja,
Maxeiner Sebastian,
Schalla Carmen,
Rütten Stephan,
Zenke Martin,
Sechi Antonio
Publication year - 2021
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fj.202000740rr
Subject(s) - lamellipodium , focal adhesion , microbiology and biotechnology , cytoskeleton , actin cytoskeleton , cell migration , actin remodeling , cell adhesion , adhesion , actin , chemistry , biology , cell , signal transduction , biochemistry , organic chemistry
Several cytoskeleton‐associated proteins and signaling pathways work in concert to regulate actin cytoskeleton remodeling, cell adhesion, and migration. Although the leukocyte‐specific protein 1 (LSP1) has been shown to interact with the actin cytoskeleton, its function in the regulation of actin cytoskeleton dynamics is, as yet, not fully understood. We have recently demonstrated that the bimolecular complex between LSP1 and myosin1e controls actin cytoskeleton remodeling during phagocytosis. In this study, we show that LSP1 downregulation severely impairs cell migration, lamellipodia formation, and focal adhesion dynamics in macrophages. Inhibition of the interaction between LSP1 and myosin1e also impairs these processes resulting in poorly motile cells, which are characterized by few and small lamellipodia. Furthermore, cells in which LSP1‐myosin1e interaction is inhibited are typically associated with inefficient focal adhesion turnover. Collectively, our findings show that the LSP1‐myosin1e bimolecular complex plays a pivotal role in the regulation of actin cytoskeleton remodeling and focal adhesion dynamics required for cell migration.