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|Title:||Flightless I: An actin-remodelling protein and an important negative regulator of wound repair|
|Citation:||International Journal of Biochemistry & Cell Biology, 2008; 40(8):1415-1419|
|Publisher:||Pergamon-Elsevier Science Ltd|
|Z. Kopecki and A.J. Cowin|
|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.|
|Keywords:||Animals; Humans; Microfilament Proteins; Actins; Gelsolin; Drosophila Proteins; Receptors, Cytoplasmic and Nuclear; Wound Healing|
|Appears in Collections:||Paediatrics publications|
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