Formins include several families of proteins that regulate actin cytoskeletal dynamics via two conserved formin homology domains, FH1 and FH2. Through cooperation of FH1 and FH2, formins construct actin-based structures comprising linear, unbranched filaments that are used in stress fibers, actin cables, microspikes, and contractile rings. A subgroup of the formins is the diaphanous (Dia) family, which includes mDia1 (Diap1), mDia2 (Diap3), and mDia3 (Diap2). The mDia2 protein has been implicated in cell migration and cytokinesis. This Dia protein can nucleate actin polymerization and stabilize microtubules. mDia2 may also function in the nucleus as the protein continually shuttles between the cytoplasm and nucleus. Regulation of mDia2 activity may occur through ROCK phosphorylation of Thr-1061 and Ser-1070. This phosphorylation disrupts inhibitory interactions between the DAD and DID domains leading to enhanced mDia2 activation of RhoA.
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*For more information, see UniProt Accession Q9Z207
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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