ANLN Gene: Function, Expression, Mutations, and Disease Associations

The ANLN gene encodes anillin, a highly conserved actin-binding protein that plays a critical role in cytokinesis, the final stage of cell division. Anillin functions as a scaffold protein, coordinating the assembly and contractility of the actomyosin ring at the cleavage furrow. It interacts with multiple structural and regulatory proteins, including F-actin, myosin II, septins, and RhoA, to ensure proper cell division. Beyond its role in cytokinesis, anillin is involved in cell migration, cell adhesion, and tissue morphogenesis. Its expression is tightly regulated during the cell cycle, peaking in G2/M phase. Dysregulation of ANLN expression and function has been implicated in various human diseases, most notably cancer, where it is frequently overexpressed and associated with poor prognosis, and in a rare form of focal segmental glomerulosclerosis (FSGS).

Tissue Expression

Cell Line Expression

Hotspot Mutations

Mutation functional classification

• Cytokinesis

• Actin Cytoskeleton Regulation

• Rho GTPase signaling

• Cell Cycle

Anillin is a 1249-amino acid protein with a molecular weight of approximately 140 kDa. It is a multi-domain scaffold protein that localizes to the cleavage furrow during cytokinesis. Its key structural features include an N-terminal actin-binding domain, a central myosin II binding region, and a C-terminal PH domain that binds to the plasma membrane. Anillin is essential for the proper assembly and constriction of the actomyosin contractile ring. It acts as a hub, linking the actin cytoskeleton to the plasma membrane and to regulatory proteins like RhoA and septins. This coordination is critical for the successful separation of daughter cells. In addition to its role in cytokinesis, anillin is involved in interphase processes such as cell migration and adhesion. Its expression is cell-cycle regulated, and its dysregulation is a hallmark of many aggressive cancers.