DNM2

DNM2 protein

DNM2

File:DNM2 structure.png

Crystal structure of DNM2

Dynamin-2 (DNM2) is a protein-coding gene that plays a crucial role in cellular processes such as endocytosis and membrane trafficking. It is a member of the dynamin family of GTPases and is primarily involved in the scission of vesicles from the plasma membrane during endocytosis.

Structure

DNM2 consists of several domains, including a GTPase domain, a middle domain, a pleckstrin homology (PH) domain, a GTPase effector domain (GED), and a proline-rich domain. These domains work together to facilitate the formation and fission of vesicles.

Function

The primary function of DNM2 is to regulate the process of endocytosis, which involves the internalization of extracellular molecules into the cell. DNM2 plays a key role in the formation of clathrin-coated vesicles that transport cargo molecules into the cell.

Clinical Significance

Mutations in the DNM2 gene have been associated with various human diseases, including centronuclear myopathy and Charcot-Marie-Tooth disease. These conditions are characterized by muscle weakness and degeneration due to impaired vesicle trafficking and membrane dynamics.

Interactions

DNM2 interacts with a variety of proteins involved in endocytosis and vesicle trafficking, including clathrin, amphiphysin, and endophilin. These interactions are essential for the proper functioning of the endocytic machinery.

Regulation

The activity of DNM2 is tightly regulated by post-translational modifications such as phosphorylation and ubiquitination. These modifications modulate the GTPase activity of DNM2 and its ability to scission vesicles from the membrane.