FRY microtubule binding protein (FRY)

FRY microtubule binding protein (FRY) is a large and highly conserved scaffolding protein, originally named for its ortholog in fruit flies (“furry”) and now classified as a microtubule-binding protein in mammals[1][5][4][6]. It plays a critical role in mitotic spindle assembly and maintenance through the promotion of PLK1 activity and structural organization of centrosomes during cell division[5]. FRY may also serve as a scaffold for the interaction between the kinases AURKA and PLK1, facilitating proper phosphorylation and mitotic progression. Beyond cell division, FRY is involved in cell morphogenesis, polarization, and may modulate signal transduction, particularly in the Hippo/YAP pathway that regulates cell growth and proliferation[1][3]. Disruption of FRY function alters cell morphology, suppresses proliferation of specific cancer cell lines (breast cancer), and its deficiency is associated with defects in development and morphogenesis. There is evidence linking its aberrant function to cancer (as a tumor suppressor modulator), as well as to rare neurodevelopmental diseases via its paralog FRYL[1][2][5]. Given its size, complexity, and scaffolding function, FRY is not currently considered a traditional drug target such as a receptor, enzyme, or transporter, and there are no known drugs that interact with it[5][1][4].

Other names

Protein furry homologC13orf14bA37E23.113CDNA73CG003bA207N4.2214K23.2WUGSC:H_2G3A.1furry homologFRY microtubule binding protein

No drugs or small molecules targeting FRY are described; mechanism relates to biological role as a scaffold and regulator of mitotic kinases and cell structure.