Flightless I: an actin-remodelling protein and an important negative regulator of wound repair
- PMID: 17526423
- DOI: 10.1016/j.biocel.2007.04.011
Flightless I: an actin-remodelling protein and an important negative regulator of wound repair
Abstract
Flightless I (FliI) is a member of the gelsolin family of actin-remodelling proteins, and has been identified as having two functional protein family domains: a leucine rich repeat (LRR) domain and a gelsolin-like domain. This unique structure allows FliI to act as an actin-remodelling protein as well as a nuclear receptor co-activator with ability to interact with various other proteins important in cellular signaling. The actin cytoskeleton is an integral component of all cells and the effect of FliI protein on actin remodelling is a vital part of cellular motility, contraction and adhesion. The product of the FliI gene is expected to provide a vital link between the molecules of yet unidentified signal transduction pathways and the actin cytoskeleton. Exact signaling pathways and mechanisms underpinning FliI effects in wound healing are yet to be fully identified however strong research evidence clearly identifies this molecule as a possible new therapeutic target whose manipulation may greatly improve wound healing and could lead to potential innovative medical applications.
Similar articles
-
Flightless I deficiency enhances wound repair by increasing cell migration and proliferation.J Pathol. 2007 Apr;211(5):572-581. doi: 10.1002/path.2143. J Pathol. 2007. PMID: 17326236
-
Flightless I regulates hemidesmosome formation and integrin-mediated cellular adhesion and migration during wound repair.J Invest Dermatol. 2009 Aug;129(8):2031-45. doi: 10.1038/jid.2008.461. Epub 2009 Feb 12. J Invest Dermatol. 2009. PMID: 19212345
-
Decreased expression of Flightless I, a gelsolin family member and developmental regulator, in early-gestation fetal wounds improves healing.Mamm Genome. 2011 Jun;22(5-6):341-52. doi: 10.1007/s00335-011-9320-z. Epub 2011 Mar 13. Mamm Genome. 2011. PMID: 21400204
-
The flightless I protein and the gelsolin family in nuclear hormone receptor-mediated signalling.Biochem Soc Trans. 2004 Dec;32(Pt 6):940-2. doi: 10.1042/BST0320940. Biochem Soc Trans. 2004. PMID: 15506930 Review.
-
Multifunctional Roles of the Actin-Binding Protein Flightless I in Inflammation, Cancer and Wound Healing.Front Cell Dev Biol. 2020 Nov 24;8:603508. doi: 10.3389/fcell.2020.603508. eCollection 2020. Front Cell Dev Biol. 2020. PMID: 33330501 Free PMC article. Review.
Cited by
-
Amotl2 interacts with LL5β, localizes to podosomes and regulates postsynaptic differentiation in muscle.J Cell Sci. 2013 May 15;126(Pt 10):2225-35. doi: 10.1242/jcs.121327. Epub 2013 Mar 22. J Cell Sci. 2013. PMID: 23525008 Free PMC article.
-
A Review of Acquired Autoimmune Blistering Diseases in Inherited Epidermolysis Bullosa: Implications for the Future of Gene Therapy.Antibodies (Basel). 2021 May 17;10(2):19. doi: 10.3390/antib10020019. Antibodies (Basel). 2021. PMID: 34067512 Free PMC article. Review.
-
FLII Modulates the Myogenic Differentiation of Progenitor Cells via Actin Remodeling-Mediated YAP1 Regulation.Int J Mol Sci. 2023 Sep 20;24(18):14335. doi: 10.3390/ijms241814335. Int J Mol Sci. 2023. PMID: 37762638 Free PMC article.
-
Porous Alumina Membrane-Based Electrochemical Biosensor for Protein Biomarker Detection in Chronic Wounds.Front Chem. 2020 Mar 6;8:155. doi: 10.3389/fchem.2020.00155. eCollection 2020. Front Chem. 2020. PMID: 32211379 Free PMC article.
-
Slit2N Inhibits Transmission of HIV-1 from Dendritic Cells to T-cells by Modulating Novel Cytoskeletal Elements.Sci Rep. 2015 Nov 19;5:16833. doi: 10.1038/srep16833. Sci Rep. 2015. PMID: 26582347 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials