ArticleMolecular biology of the cell2018
The leucine-rich region of Flightless I interacts with R-ras to regulate cell extension formation.
Article in Molecular biology of the cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 8 citations in OpenAlex.
- Loss of the actin remodeling protein Flightless-1 impairs CD8 and regulatory T cell function.Journal of immunology (Baltimore, Md. : 1950) · 2026Article
- Quantification of the Actin-Binding Protein Flightless-I in Human Serum by Automated Western Blot System and Investigation of Its Diagnostic Potential in Sepsis.Biomedicines · 2025Article
- Inhibition of ADAM9 promotes the selective degradation of KRAS and sensitizes pancreatic cancers to chemotherapy.Nature cancer · 2024Article
- The Role of R-Ras Proteins in Normal and Pathologic Migration and Morphologic Change.The American journal of pathology · 2021Review
- Flightless anchors IQGAP1 and R-ras to mediate cell extension formation and matrix remodeling.Molecular biology of the cell · 2020Article
- Multifunctional Roles of the Actin-Binding Protein Flightless I in Inflammation, Cancer and Wound Healing.Frontiers in cell and developmental biology · 2020Review
- Quantitative Proteomics Analysis Indicates That Upregulation of lncRNA HULC Promotes Pathogenesis of Glioblastoma Cells.OncoTargets and therapy · 2020Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Flightless I (FliI) is a calcium-dependent, actin severing and capping protein that localizes to cell matrix adhesions, contributes to the generation of cell extensions, and colocalizes with Ras. Currently, the mechanism by which FliI interacts with Ras to enable assembly of actin-based cell protrusions is not defined. R-Ras, but not K-ras, H-ras, or N-ras, associated with the leucine-rich region (LRR) of FliI. Mutations of the proline-rich region of R-ras (P202A, P203A) prevented this association. Knockdown of Ras GTPase-activating SH3 domain-binding protein (G3BP1) or Rasgap
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Registered trials
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