ArticleMolecular biology of the cell2015
Flightless I interacts with NMMIIA to promote cell extension formation, which enables collagen remodeling.
Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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The trial behind it
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- Biallelic variants in FLII cause pediatric cardiomyopathy by disrupting cardiomyocyte cell adhesion and myofibril organization.JCI insight · 2023Article
- Wound Healing from an Actin Cytoskeletal Perspective.Cold Spring Harbor perspectives in biology · 2022Review
- Flightless anchors IQGAP1 and R-ras to mediate cell extension formation and matrix remodeling.Molecular biology of the cell · 2020Article
- The scaffold-protein IQGAP1 enhances and spatially restricts the actin-nucleating activity of Diaphanous-related formin 1 (DIAPH1).The Journal of biological chemistry · 2020Article
- The Activities of the Gelsolin Homology Domains of Flightless-I in Actin Dynamics.Frontiers in molecular biosciences · 2020Article
- Multifunctional Roles of the Actin-Binding Protein Flightless I in Inflammation, Cancer and Wound Healing.Frontiers in cell and developmental biology · 2020Review
- Mammalian nonmuscle myosin II comes in three flavors.Biochemical and biophysical research communications · 2018Review
- The leucine-rich region of Flightless I interacts with R-ras to regulate cell extension formation.Molecular biology of the cell · 2018Article
- GEFs: Dual regulation of Rac1 signaling.Small GTPases · 2017Review
- Differential Rac1 signalling by guanine nucleotide exchange factors implicates FLII in regulating Rac1-driven cell migration.Nature communications · 2016Article
- Cytoskeletal protein Flightless I inhibits apoptosis, enhances tumor cell invasion and promotes cutaneous squamous cell carcinoma progression.Oncotarget · 2015Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
We examined the role of the actin-capping protein flightless I (FliI) in collagen remodeling by mouse fibroblasts. FliI-overexpressing cells exhibited reduced spreading on collagen but formed elongated protrusions that stained for myosin10 and fascin and penetrated pores of collagen-coated membranes. Inhibition of Cdc42 blocked formation of cell protrusions. In FliI-knockdown cells, transfection with constitutively active Cdc42 did not enable protrusion formation. FliI-overexpressing cells displayed increased uptake and degradation of exogenous collagen and strongly compacted collagen fibrils, which was blocked by blebbistatin. Mass spectrometry analysis of FliI immunoprecipitates showed that FliI associated with nonmuscle myosin IIA (NMMIIA), which was confirmed by immunoprecipitation. GFP-FliI colocalized with NMMIIA at cell protrusions. Purified FliI containing gelsolin-like domains (GLDs) 1-6 capped actin filaments efficiently, whereas FliI GLD 2-6 did not. Binding assays showed strong interaction of purified FliI protein (GLD 1-6) with the rod domain of NMMIIA (kD = 0.146 μM), whereas FliI GLD 2-6 showed lower binding affinity (kD = 0.8584 μM). Cells expressing FliI GLD 2-6 exhibited fewer cell extensions, did not colocalize with NMMIIA, and showed reduced collagen uptake compared with cells expressing FliI GLD 1-6. We conclude that FliI interacts with NMMIIA to promote cell extension formation, which enables collagen remodeling in fibroblasts.
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Registered trials
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