Anillin
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Anillin is a protein that plays a crucial role in cell division, particularly during the process of cytokinesis. It is encoded by the ANLN gene in humans. Anillin is highly conserved across species, indicating its essential function in cellular processes.
Function[edit | edit source]
Anillin is a multifunctional protein that interacts with various components of the cytoskeleton, including actin, myosin, and septins. During cytokinesis, anillin localizes to the contractile ring, a structure composed of actin and myosin that constricts to divide the cell into two daughter cells. Anillin helps to stabilize the contractile ring and ensures proper cell division.
Structure[edit | edit source]
Anillin contains several domains that facilitate its interactions with other proteins and the cytoskeleton. These include an actin-binding domain, a myosin-binding domain, and a pleckstrin homology (PH) domain. The PH domain is particularly important for anillin's localization to the plasma membrane during cytokinesis.
Clinical Significance[edit | edit source]
Mutations or dysregulation of anillin can lead to defects in cell division, which may contribute to various diseases, including cancer. Overexpression of anillin has been observed in several types of cancer, suggesting that it may play a role in tumorigenesis.
Research[edit | edit source]
Ongoing research is focused on understanding the precise mechanisms by which anillin regulates cytokinesis and its potential as a therapeutic target in cancer treatment.
See also[edit | edit source]
References[edit | edit source]
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Contributors: Prab R. Tumpati, MD