phospho-FHOD1 (Thr-1141) Peptide

Formins include several families of proteins that regulate actin cytoskeletal dynamics via two conserved formin homology domains, FH1 and FH2. The FH1 region contains poly-proline stretches that promote interactions with profilin. The FH2 domain, located C-terminally to the FH1 domain, is highly conserved in formin proteins and possesses actin nucleation and polymerization activities. 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. Several mammalian formins, including mDia1, FRL, and formin homology domain protein 1 (FHOD1) are inhibited through an intramolecular interaction between the C-terminal Dia autoregulatory domain (DAD) and its recognition region at the N-terminus. In FHOD1, this autoinhibitory interaction is disrupted through phosphorylation of Ser-1131, Ser-1137, and Thr-1141 by ROCK. Subsequent FHOD1 activation leads to stress fiber formation. In endothelial cells, thrombin activates this ROCK pathway, leading to FHOD1-mediated stress fiber formation.

References

*For more information, see UniProt Accession Q9Y613

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