CEP170

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CEP170 is a protein that in humans is encoded by the CEP170 gene. This protein is a component of the centrosome, an organelle important for the process of microtubule nucleation and anchoring. The centrosome plays a pivotal role in the organization of the microtubule network within the cell and is crucial for the process of cell division and the maintenance of cell shape and size.

Function[edit | edit source]

CEP170 is involved in the organization and stability of the microtubule network. It is a centrosomal protein that plays a significant role in the formation and function of the mitotic spindle, a structure required for the segregation of chromosomes during cell division. CEP170 interacts with other centrosomal proteins to anchor microtubules to the centrosome, facilitating their organization and stabilization. This protein is also implicated in the regulation of microtubule dynamics, affecting cell shape, motility, and polarity.

Gene[edit | edit source]

The CEP170 gene is located on human chromosome 1. It encodes a protein that is essential for centrosome function and integrity. Mutations in this gene have been associated with various cellular and developmental abnormalities, highlighting its importance in cell division and structure.

Clinical Significance[edit | edit source]

Although direct links between mutations in the CEP170 gene and specific human diseases are still under investigation, the critical role of CEP170 in cell division and its potential implications in cancer biology are of significant interest. Abnormalities in centrosome number and function are a hallmark of many cancer cells, and as a centrosomal protein, CEP170 may play a role in tumorigenesis. Further research is needed to elucidate the exact mechanisms by which CEP170 contributes to disease.

Interactions[edit | edit source]

CEP170 is known to interact with several other proteins involved in centrosome function and microtubule dynamics, including Pericentrin and Ninein. These interactions are crucial for the proper organization of the microtubule network and for the fidelity of cell division.

See Also[edit | edit source]

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Contributors: Prab R. Tumpati, MD