Formins

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Proteins

title: "Formins" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public tags: ["protein-domains", "cell-biology", "proteins", "cellular-processes"] description: "Proteins" topic_path: "science/biology" source: "https://en.wikipedia.org/wiki/Formins" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Proteins ::

::data[format=table title="infobox protein"]

FieldValue
Nameformin 1
HGNCid3768
SymbolFMN1
AltSymbolsLD, FMN
EntrezGene342184
OMIM136535
RefSeqNM_001103184
UniProtQ68DA7
Chromosome15
Armq
Band13
LocusSupplementaryData-q14
::

|Name=formin 1 |caption= |image= |width= |HGNCid=3768 |Symbol=FMN1 |AltSymbols=LD, FMN |EntrezGene=342184 |OMIM=136535 |RefSeq=NM_001103184 |UniProt= Q68DA7 |PDB= |ECnumber= |Chromosome=15 |Arm=q |Band=13 |LocusSupplementaryData=-q14 | Symbol = Drf_FH1 | Name = Formin Homology Region 1 | image = | width = | caption = | Pfam = PF06346 | Pfam_clan = | InterPro = IPR009408 | SMART = | PROSITE = | MEROPS = | SCOP = | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = ::figure[src="https://upload.wikimedia.org/wikipedia/commons/0/03/Formin_proteins.png" caption="doi = 10.1093/molbev/msn215 }}"] ::

| Symbol = FH2 | Name = Formin Homology 2 Domain | image = PDB 1ux4 EBI.jpg | width = | caption = crystal structures of a formin homology-2 domain reveal a tethered-dimer architecture | Pfam = PF02181 | Pfam_clan = | InterPro = IPR015425 | SMART = FH2 | PROSITE = | MEROPS = | SCOP = 1ux5 | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = | Symbol = Drf_FH3 | Name = Diaphanous FH3 Domain | image = PDB 1z2c EBI.jpg | width = | caption = crystal structure of mdia1 gbd-fh3 in complex with rhoc-gmppnp | Pfam = PF06367 | Pfam_clan = CL0020 | InterPro = IPR010472 | SMART = | PROSITE = | MEROPS = | SCOP = | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = | Symbol = Drf_DAD | Name = DRF Autoregulatory Domain | image = PDB 2bap EBI.jpg | width = | caption = crystal structure of the n-terminal mdia1 armadillo repeat region and dimerisation domain in complex with the mdia1 autoregulatory domain (dad) | Pfam = PF06345 | Pfam_clan = | InterPro = IPR010465 | SMART = | PROSITE = | MEROPS = | SCOP = | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = | Symbol = Drf_GBD | Name = Diaphanous GTPase-binding Domain | image = PDB 1z2c EBI.jpg | width = | caption = crystal structure of mdia1 gbd-fh3 in complex with rhoc-gmppnp | Pfam = PF06371 | Pfam_clan = CL0020 | InterPro = IPR010473 | SMART = | PROSITE = | MEROPS = | SCOP = | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = Formins (formin homology proteins) are a group of proteins that are involved in the polymerization of actin and associate with the fast-growing end (barbed end) of actin filaments. Most formins are Rho-GTPase effector proteins. Formins regulate the actin and microtubule cytoskeleton and are involved in various cellular functions such as cell polarity, cytokinesis, cell migration and SRF transcriptional activity. Formins are multidomain proteins that interact with diverse signalling molecules and cytoskeletal proteins, although some formins have been assigned functions within the nucleus.

Diversity

Formins have been found in all eukaryotes studied. In humans, 15 different formin proteins are present that have been classified in 7 subgroups. By contrast, yeasts contain only 2-3 formins.

Structure and interactions

Formins are characterized by the presence of three formin homology (FH) domains (FH1, FH2 and FH3), although members of the formin family do not necessarily contain all three domains. In addition, other domains are usually present, such as PDZ, DAD, WH2, or FHA 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 actin nucleation-promoting activity of S. cerevisiae formins has been localized to the FH2 domain. 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 polymerization. The FH3 domain is less well conserved and is required for directing formins to the correct intracellular location, such as the mitotic spindle, or the projection tip during cellular 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). The GBD is a bifunctional autoinhibitory domain that interacts with and is regulated by activated Rho family members. Mammalian Drf3 contains a CRIB-like motif within its GBD for binding to Cdc42, which is required for Cdc42 to activate and guide Drf3 towards the cell cortex where it remodels the actin skeleton. The DAD binds the N-terminal GBD; this link is broken when GTP-bound Rho binds to the GBD and activates the protein. The addition of the DAD to mammalian cells induces actin filament formation, stabilizes microtubules, and activates SRF mediated transcription. Another commonly found domain is an armadillo repeat region (ARR) located in the FH3 domain.

The FH2 domain, has been shown by X-ray crystallography to have an elongated, crescent shape containing three helical subdomains.

Formins also directly bind to microtubules via their FH2 domain. This interaction is important in promoting the capture and stabilization of a subset of microtubules oriented towards the leading edge of migrating cells. Formins also promote the capture of microtubules by the kinetochore during mitosis and for aligning microtubules along actin filaments.

References

References

  1. (December 2008). "Origins and evolution of the formin multigene family that is involved in the formation of actin filaments". Molecular Biology and Evolution.
  2. (July 2003). "Formins: signaling effectors for assembly and polarization of actin filaments". Journal of Cell Science.
  3. (June 2015). "The evolution of compositionally and functionally distinct actin filaments". Journal of Cell Science.
  4. (2007). "Mechanism and function of formins in the control of actin assembly". Annual Review of Biochemistry.
  5. (June 2006). "Staying in shape with formins". Developmental Cell.
  6. (January 2005). "Phylogenetic analysis of the formin homology 2 domain". Molecular Biology of the Cell.
  7. (July 2010). "SnapShot: Formins". Cell.
  8. (February 2003). "ForC, a novel type of formin family protein lacking an FH1 domain, is involved in multicellular development in Dictyostelium discoideum". Journal of Cell Science.
  9. (August 2003). "The formins: active scaffolds that remodel the cytoskeleton". Trends in Cell Biology.
  10. Uetz, Peter. (1997). "Biochemische Studien am limb deformity-Protein der Vertebraten: Inaugural-Dissertation zur Erlangung der Doktorwürde der Naturwissenschaftlich-Mathematischen Gesamtfakultät der Ruprecht-Karls-Universität Heidelberg". European Molecular Biology Laboratory.
  11. (December 1996). "Molecular interaction between limb deformity proteins (formins) and Src family kinases". The Journal of Biological Chemistry.
  12. (November 2003). "Fhos, a mammalian formin, directly binds to F-actin via a region N-terminal to the FH1 domain and forms a homotypic complex via the FH2 domain to promote actin fiber formation". Journal of Cell Science.
  13. (February 2004). "The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization". Molecular Cell.
  14. (February 2001). "Localization of a mammalian homolog of diaphanous, mDia1, to the mitotic spindle in HeLa cells". Journal of Cell Science.
  15. (June 1998). "FH3, a domain found in formins, targets the fission yeast formin Fus1 to the projection tip during conjugation". The Journal of Cell Biology.
  16. (April 2003). "Disruption of the Diaphanous-related formin Drf1 gene encoding mDia1 reveals a role for Drf3 as an effector for Cdc42". Current Biology.
  17. (March 2004). "Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture". Cell.
  18. (January 2013). "FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation". Nature Structural & Molecular Biology.
  19. (August 2001). "mDia mediates Rho-regulated formation and orientation of stable microtubules". Nature Cell Biology.
  20. (February 2010). "Formins and microtubules". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research.

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