Destrin

Destrin

Illustration of the Destrin protein structure

Destrin, also known as actin-depolymerizing factor (ADF), is a protein that plays a crucial role in the regulation of the actin cytoskeleton in eukaryotic cells. It is involved in the disassembly of actin filaments, which is essential for various cellular processes such as cell motility, cytokinesis, and cellular morphogenesis.

Structure

Destrin is a member of the ADF/cofilin family of proteins, which are characterized by their ability to bind to actin and modulate its dynamics. The protein consists of a single polypeptide chain that folds into a compact structure, allowing it to interact with actin filaments. The structure of destrin includes several key regions that are responsible for its actin-binding and depolymerizing activities.

Function

Destrin functions primarily by binding to ADP-bound actin filaments, promoting their disassembly. This activity is crucial for the turnover and remodeling of the actin cytoskeleton, which is necessary for cell movement and shape changes. Destrin's ability to sever actin filaments and increase the rate of actin monomer dissociation is vital for maintaining the dynamic nature of the cytoskeleton.

Regulation

The activity of destrin is regulated by several factors, including phosphorylation and interactions with other proteins. Phosphorylation of destrin can inhibit its actin-depolymerizing activity, thereby stabilizing actin filaments. Additionally, destrin can be regulated by phosphoinositides and other signaling molecules that modulate its interaction with actin.

Clinical Significance

Alterations in destrin function or expression have been implicated in various diseases. For example, dysregulation of actin dynamics due to abnormal destrin activity can contribute to cancer cell metastasis, as well as neurodegenerative diseases. Understanding the role of destrin in these conditions may provide insights into potential therapeutic targets.

Related Pages

• Actin
• Cytoskeleton
• Cell motility
• Cytokinesis
• Phosphorylation