p120cateniini

P120Catennins are a family of proteins that play a crucial role in the regulation of cell adhesion and cytoskeleton dynamics. They are characterized by their ability to bind to the catenin family of proteins, which includes p120, p190, and β-catenin. This binding is mediated by the catenin-binding domain (CBD) present in p120Catennins.

There are several isoforms of p120Catennins, which are generated through alternative splicing from a single gene. These isoforms have distinct expression patterns and functional properties, suggesting that they may play specialized roles in different cell types. The most widely studied member of this family is p120 itself, which is known to modulate the activity of Rho GTPases and the cytoskeletal-network dynamics.

p120Catennins have been implicated in a range of physiological processes, including cell migration, wound healing, and tumorigenesis. They are thought to exert their effects by regulating the turnover of cadherin-catenin complexes, which control cell-cell adhesion and communication. Aberrant expression of p120Catennins has been observed in various carcinomas and melanomas, suggesting that they may contribute to cancer progression. However, the mechanistic details of their involvement in disease remain the subject of ongoing investigation.

p120Catennins have been studied in detail in several organisms, including humans, mice, and Drosophila. Work in these model systems has shed light on the molecular mechanisms underlying their function and highlighted the importance of these proteins in maintaining tissue structure and function. Further research is needed to elucidate the full range of their cellular roles and to explore their potential as therapeutic targets.