Inverted formin-2 belongs to the formin homology family. In mice, it interacts with profilin and actin at the FH1 and FH2 domains respectively. It severs actin filaments and accelerates their polymerisation and depolymerisation [].
DIAPH2 belongs to the formin homology family, Diaphanous subfamily (also known as the Diaphanous-related formins, Drfs). In addition to the FH1 and FH2 domains, Drfs contain an N-terminal GTPase-binding domain (mDiaN) and a C-terminal Diaphanous-autoregulatory domain (DAD).DIAPH2 may be involved in oogenesis and in the regulation of endosome dynamics. In humans, DIAPH2 has three isoforms produced by alternative splicing. Its isoform3, DIA2C, together with CSK are sequentially activated by GTPase RhoD to regulate the motility of early endosomes through interactions with the actin cytoskeleton [].
Protein diaphanous homologue 3 (DIAPH3) belongs to the formin homology family, Diaphanous subfamily (also known as the Diaphanous-related formins, Drfs). In addition to the FH1 and FH2 domains, Drfs contain an N-terminal GTPase-binding domain (mDiaN) and a C-terminal Diaphanous-autoregulatory domain (DAD).DIAPH3 (also known as mDia2, which can be confusing) acts in a Rho-dependent manner to recruit profilin to the membrane, where it promotes actin polymerisation. It is required for cytokinesis, stress fibre formation, and transcriptional activation of the serum response factor []. It couples Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics [].
Formins (formin homology proteins) proteins play a crucial role in the reorganisation of the actin cytoskeleton and associate with the fast-growing end (barbed end) of actin filaments [, ]. This entry represents the formin homologues from plants. Seed plants have two formin clades with numerous paralogues []. They can be classified as class I and class II formins. Class I formins includes a N-terminal membrane insertion signal, a predicted extracytoplasmic Pro-rich stretch, a transmembrane region, and C-terminal FH1 and FH2 domains []. Though class II formins usually contain a N-terminal PTEN domain related to the human PTEN protein (implied in pathogenesis of the Parkinson disease) [], the N-termini of type-II plant formins do not contain any recognisable domain that can provide a clue to their biological function.
Protein diaphanous homologue 1 (Dia1) belongs to the formin homology family, Diaphanous subfamily (also known as the Diaphanous-related formins, Drfs). In addition to the FH1 and FH2 domains, Drfs contain an N-terminal GTPase-binding domain (mDiaN) and a C-terminal Diaphanous-autoregulatory domain (DAD).Dia1 contains the N-terminal RhoA-binding domain (RBD) followed by a four armadillo-repeats containing Diaphanous inhibitory domain (DID) that binds the C-terminal Diaphanous autoregulatory domain (DAD) [, ]. Dia1 nucleates actin filaments and regulate actin polymerisation and depolymerisation. The activities of Dia1 is regulated by an autoinhibitory interaction between DAD domain and the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments []. Dia1 couples Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics [].
Formin homology (FH) proteins play a crucial role in the reorganisation of the actin cytoskeleton, which mediates various functions of the cell cortex including motility, adhesion, and cytokinesis []. Formins are multidomain proteins that interact with diverse signalling molecules and cytoskeletal proteins, although some formins have been assigned functions within the nucleus. Formins are characterised by the presence of three FH domains (FH1, FH2 and FH3), although members of the formin family do not necessarily contain all three domains []. The proline-rich FH1 domain mediates interactions with a variety of proteins, including the actin-binding protein profilin, SH3 (Src homology 3) domain proteins, and WW domain proteins. The FH2 domain () is required to inhibit actin polymerisation. The FH3 domain is less well conserved and is required for directing formins to the correct intracellular location, such the mitotic spindle [], or the projection tip during conjugation []. In addition, some formins can contain a GTPase-binding domain (GBD) () required for binding to Rho small GTPases, and a C-terminal conserved Dia-autoregulatory domain (DAD).This entry represents the FH3 domain.
Formin homology (FH) proteins play a crucial role in the reorganisation of the actin cytoskeleton, which mediates various functions of the cell cortex including motility, adhesion, and cytokinesis []. Formins are multidomain proteins that interact with diverse signalling molecules and cytoskeletal proteins, although some formins have been assigned functions within the nucleus. Formins are characterised by the presence of three FH domains (FH1, FH2 and FH3), although members of the formin family do not necessarily contain all three domains []. The proline-rich FH1 domain mediates interactions with a variety of proteins, including the actin-binding protein profilin, SH3 (Src homology 3) domain proteins, and WW domain proteins. The FH2 domain is required for the self-association of formin proteins through the ability of FH2 domains to directly bind each other [], and may also act to inhibit actin polymerisation []. The FH3 domain () is less well conserved and may be important for determining intracellular localisation of formin family proteins. In addition, some formins can contain a GTPase-binding domain (GBD) () required for binding to Rho small GTPases, and a C-terminal conserved Dia-autoregulatory domain (DAD).This superfamily represents the FH2 domain, which was shown by X-ray crystallography to have an elongated, crescent shape containing three helical subdomains [].
Formin homology (FH) proteins play a crucial role in the reorganisation of the actin cytoskeleton, which mediates various functions of thecell cortex including motility, adhesion, and cytokinesis []. Formins are multidomain proteins that interact with diverse signalling molecules and cytoskeletal proteins, although some formins have been assigned functions within the nucleus. Formins are characterised by the presence of three FH domains (FH1, FH2 and FH3), although members of the formin family do not necessarily contain all three domains []. The proline-rich FH1 domain mediates interactions with a variety of proteins, including the actin-binding protein profilin, SH3 (Src homology 3) domain proteins, and WW domain proteins. The FH2 domain is required for the self-association of formin proteins through the ability of FH2 domains to directly bind each other [], and may also act to inhibit actin polymerisation []. The FH3 domain () is less well conserved and may be important for determining intracellular localisation of formin family proteins. In addition, some formins can contain a GTPase-binding domain (GBD) () required for binding to Rho small GTPases, and a C-terminal conserved Dia-autoregulatory domain (DAD).This entry represents the FH2 domain, which was shown by X-ray crystallography to have an elongated, crescent shape containing three helical subdomains [].
Formins (formin homology proteins) proteins play a crucial role in the reorganisation of the actin cytoskeleton and associate with the fast-growing end (barbed end) of actin filaments [, ]. This entry represents the formin homologues from animals (and some fungi), including protein cappuccino from Drosophila melanogaster and formins from human and mouse. Protein cappuccino acts as an actin nucleation factor and promotes assembly of actin filaments together with spir. It may play a role in intracellular vesicle transport along actin fibres, providing a novel link between actin cytoskeleton dynamics and intracellular transport []. Formins are characterised by the presence of three FH domains (FH1, FH2 and FH3), although members of the formin family do not necessarily contain all three domains []. The proline-rich FH1 domain mediates interactions with a variety of proteins, including the actin-binding protein profilin, SH3 (Src homology 3) domain proteins, and WW domain proteins. The FH2 domain is required for the self-association of formin proteins through the ability of FH2 domains to directly bind each other [], and may also act to inhibit actin polymerisation []. The FH3 domain () is less well conserved and may be important for determining intracellular localisation of formin family proteins. In addition, some formins can contain a GTPase-binding domain (GBD) () required for binding to Rho small GTPases, and a C-terminal conserved Dia-autoregulatory domain (DAD).
