Formin homology 2 domain-containing protein 1 (FHOD1)

Formin homology 2 domain-containing protein 1 (FHOD1) is a member of the diaphanous-related formin (DRF) family of cytoskeletal regulatory proteins. It contains formin homology (FH1 and FH2) domains, a GTPase-binding domain, coiled-coil, and auto-inhibitory regions typical for DRFs. FHOD1 acts as an actin-bundling and barbed-end capping protein, driving the stabilization and organization of actin filaments into stress fibers and arcs, rather than nucleating new actin filaments[1][2][3]. FHOD1 has key roles in regulating cell migration, spreading, and adhesion, and participates in nuclear positioning by linking actin cables to the nuclear envelope[1]. It is tightly regulated by phosphorylation (notably via ROCK kinase) and is a mediator of the effects of upstream GTPase signaling pathways. FHOD1 is overexpressed in certain cancers—such as triple-negative breast cancer and glioma—where it enhances cell migration, invasion, and contributes to tumor immunosuppression by affecting immune cell infiltration and PDL1 expression[4]. Although FHOD1 is a driver of cytoskeletal rearrangement and cancer cell behavior, it is not currently considered a direct druggable target, but its expression is associated with disease aggressiveness and may serve as a potential biomarker in cancer[1][4].

Other names

FHOSFHOS1Formin homolog overexpressed in spleen 1FH1/FH2 domain-containing protein 1Formin homology 2 domain containing protein 1

Not applicable for direct drug targeting. Inhibiting FHOD1 (hypothetically) would affect actin bundling and cellular migration, but such mechanisms are not exploited by current drugs[1][4].