Villin 1

Villin 1 is a protein that in humans is encoded by the VIL1 gene. It is a member of the villin/gelsolin superfamily of actin regulatory proteins. Villin 1 is an enzyme that is involved in the cytoskeleton organization in epithelial cells and has been implicated in various cellular functions such as cell migration, cell adhesion, wound healing, and cell morphology.

Structure

Villin 1 is a 92.5 kDa protein composed of 827 amino acids. The protein is organized into six Gelsolin homology domains (G1-G6) and a headpiece domain. The headpiece domain is responsible for the high-affinity actin-binding activity of villin 1.

Function

Villin 1 is primarily found in the microvilli of epithelial cells, where it plays a crucial role in the organization and maintenance of the actin cytoskeleton. It has the ability to bundle and sever actin filaments, which is essential for the dynamic remodeling of the cytoskeleton.

In addition to its role in the cytoskeleton, villin 1 has been found to interact with other proteins such as E-cadherin and Integrin, which are involved in cell adhesion and cell-cell interactions. This suggests that villin 1 may also play a role in these processes.

Clinical significance

Alterations in the expression of villin 1 have been associated with various diseases. For example, increased expression of villin 1 has been observed in certain types of cancer, including colorectal cancer and gastric cancer. This suggests that villin 1 may serve as a potential biomarker for these cancers.

See also

• Villin
• Gelsolin
• Actin
• Microvilli

References

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