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. 2021 Sep 27;10(10):2554. doi: 10.3390/cells10102554

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© 2021 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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The human formin family. (A) Tree of human formins. The FH2 domain sequence of the formins was aligned with BLAST and the alignment was used to construct the tree [103]. The UniProt accession numbers of the corresponding sequences were: DIAPH1 (O60610), DIAPH2 (O60879), DIAPH3 (Q9NSV4), DAAM1 (Q9Y4D1), DAAM2 (Q86T65), FMNL1 (O95466), FMNL2 (Q96PY5), FMNL3 (Q8IVF7), FHOD1 (Q9Y613), FHOD3 (Q2V2M9), FMN1 (Q68DA7), FMN2 (Q9NZ56), INF2 (Q27J81), FHDC1 (Q9C0D6) and Delphilin (A4D2P6). (B) Structure and regulation of Diaphanous-related formins. The interaction of the DID and the DAD maintains the formin in a closed, inactive conformation. The binding of a specific GTP-loaded Rho GTPase to the N-terminal region of the formin opens the molecule, rendering it in its active form. The FH1 domain recruits profilin, which feeds the FH2 domain with G-actin to form the actin filaments. The illustrated molecules are not drawn to scale.