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FLASH GENE
Symbol FLII contributors: mct - updated : 10-12-2015
HGNC name flightless I homolog (Drosophila)
HGNC id 3750
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • sixteen N terminal, leucine-rich repeat motifs (LRR), with LXXLL motif within the LRR domain of FLII interacting directly with the DNA-binding domain of PPARG
  • five C terminal gelsolin-like domains, involved in capping and severing actin filaments
  • HOMOLOGY
    interspecies homolog to Drosophila flightless (fli) 1
    homolog to murine Fliih
    Homologene
    FAMILY
  • gelsolin superfamily of actin-remodeling proteins
  • CATEGORY motor/contractile
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm,cytosolic
    intracellular,cytoplasm,cytoskeleton
    intracellular,nucleus,nucleoplasm
    text
  • distributed throughout the cytosol and in focal adhesions
  • basic FUNCTION
  • playing a key role in embryonic cellularization by interacting with both the cytoskeleton and other cellular components
  • actin-remodeling protein that influences diverse processes including cell migration and gene transcription and links signal transduction with cytoskeletal regulation 0)
  • regulates cell migration through its localization to focal adhesions and its ability to cap actin filaments, which collectively affect focal adhesion maturation
  • may contribute to the inhibitory effect of chronic wound fluid on fibroblast function
  • is a component of the MLXIPL transcriptional complex and negatively regulates MLXIPL function in cancer cells
  • important role for FLII in the development and regulation of the epidermal barrier, which may contribute to the impaired healing and skin fragility of epidermolysis bullosa (EB) patients
  • functions in PPARG activation as a molecular switch to repress transcriptional activity by interrupting formation of the PPARG/RXRA complex
  • is a negative regulator of wound healing
  • actin remodeling protein that affects cellular processes including adhesion, proliferation and migration
  • enhances cutaneous squamous cell carcinoma tumor progression by decreasing apoptosis and enhancing tumor cell invasion
  • CELLULAR PROCESS cell organization/biogenesis
    PHYSIOLOGICAL PROCESS
    text muscle contraction
    PATHWAY
    metabolism
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule
    protein
  • is a substrate of SGK3 that functions downstream of PI 3-kinase and SGK3 can associate with FLII and phosphorylate FLII at residues Ser(436) and Thr(818)
  • FLII can bind directly to both ESR1 and ACTL6A, an actin-related component of the SWI/SNF complex, suggesting that FLII may recruit SWI/SNF to ESR1 target genes via interaction with ACTL6A
  • FLII is a novel NXN-binding partner (binds to NXN and other related proteins, such as Rod-derived cone viability factor (NXNL1)
  • with FLAp (linking FLII to the actin cytoskeleton)
  • three regulators of the actin cytoskeleton--AMOTL2, SPATA13 and FLII--interact with PHLDB2
  • LRRFIP2 enhances the interaction between FLII and CASP1, facilitating the inhibitory effect of FLII on CASP1 activation
  • FLII binds directly to and suppresses the transcriptional activity of PPARG
  • FLII interacts with MYH9 to promote cell extension formation, which enables collagen remodeling in fibroblasts
  • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional   deletion    
    constantly, in Smith-Magenis syndrome (SMCR)
    constitutional     --over  
    increased in the blistered skin of patients with epidermolysis bullosa (EB)
    tumoral     --over  
    negatively regulated MLXIPL mediated transcription in cancer cells
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    SystemTypeDisorderPubmed
    cancerskin 
    targeting FLII may be a potential strategy for reducing the severity of cutaneous squamous cell carcinoma
    obesity  
    FLII may serve as a novel therapeutic target in the treatment of adiposity-related metabolic syndromes
    ANIMAL & CELL MODELS