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FLASH GENE
Symbol INF2 contributors: mct/npt/pgu - updated : 01-02-2017
HGNC name inverted formin, FH2 and WH2 domain containing
HGNC id 23791
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • an N-terminal diaphanous inhibitory domain (DID), and this DID-containing N terminus of INF2 does not directly bind the Rho GTPase CDC42
  • an FH1 domain and a dimeric formin homology 2 (FH2) domain that binds filament barbed ends and is critical for polymerization and depolymerization activities , and the (FH2) domain accelerates actin filament assembly and remains at the barbed end, modulating elongation
  • a C-terminal diaphanous autoregulatory domain (DAD)/ WASP homology-2 (WH2) domain, actin monomer-binding, required for depolymerization activity, and also serves as a diaphanous autoregulatory domain (DAD), which binds to the N-terminal diaphanous inhibitory domain (DID) , but do not display barbed end binding abilities , and WH2 domain of INF2 might aid in actin nucleation, in a manner perhaps similar to FMNL3 and other formins
  • HOMOLOGY
    Homologene
    FAMILY
  • diaphanous formin family
  • CATEGORY unknown/unspecified
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm,organelle,endoplasmic reticulum
    basic FUNCTION
  • formin protein with the unique biochemical ability to accelerate actin filament depolymerization
  • physiologically, INF2 acts in the secretory pathway
  • INF2 and stable, detyrosinated microtubules are central players in centrosome reorientation in T cells
  • upon TCR triggering the INF2 formin, together with the formins DIAPH1 and FMNL1, promotes the formation of a specialized array of stable detyrosinated MT that breaks the symmetrical organization of the T-cell microtubule (MT) cytoskeleton
  • unusual formin protein in that it accelerates both actin polymerization and depolymerization, the latter through an actin filament-severing activity
  • important role for the formin INF2 in specifying the function of fibrillar focal adhesions (FAs) through its ability to generate dorsal stress fibers (SFs)
  • in addition to the common formin ability to accelerate actin nucleation and elongation, INF2 can also sever filaments and accelerate their depolymerization
  • FHOD1 and INF2 are novel components and additional actin-based regulators of podosomes in primary human macrophages
  • FHOD1 and INF2 are novel regulators of inter- and intra-structural contractility of podosomes
  • encoding a diaphanous formin family protein that regulates actin cytoskeleton dynamics, and cause human focal segmental glomerulosclerosis (FSGS)
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule
    protein
  • interacts with the Rho-GTPase CDC42 and myelin and lymphocyte protein (MAL) that are implicated in essential steps of myelination and myelin maintenance
  • INF2-induced actin filaments may drive initial mitochondrial constriction, which allows DNM1L-driven secondary constriction
  • formin protein with unique biochemical effects on actin
  • SPIRE1 cooperates with INF2 to regulate actin assembly at ER-mitochondrial contacts
  • SPOP recognizes a Ser/Thr (S/T)-rich motif in the C-terminal region of INF2 and triggers atypical polyubiquitination of INF2
  • INF2 is important for SPOP inactivation-induced prostate cancer cell migration and invasion
  • interacts with INF2
  • cell & other
    REGULATION
    Other post-translationally modified by a C-terminal farnesyl group, and this modification is required for ER interaction
    ASSOCIATED DISORDERS
    corresponding disease(s) FSGS5 , CMTDIE
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS
  • in mice, normal Inf2 function is not required for glomerular development but normal Inf2 is required for regulation of the actin-based behaviors necessary for response to and/or recovery from injury