Dynamin

Dynamins (EC 3.6.5.5) are multi-domain, high molecular weight GTPases, which play a key role in receptor-mediated endocytosis, synaptic vesicle recycling, focal adhesion assembly, cytoskeletal changes, motility of cancer cells and spermatogenesis. The dynamin family also includes dynamin-like proteins.

In mammals, there are three classical dynamins, each coded by a different gene, with varying expression patterns. Dynamin I is predominantly expressed in neurons and mediates synaptic vesicle recycling. Dynamin II is ubiquitously expressed and is involved in receptor mediated endocytosis, including uptake of viral and bacterial pathogens. The highest levels of dynamin III are found in the lung, testes and post-synaptic neurons and has been implicated in post-synaptic AMPA receptor recycling.

Dynamin proteins have various domains associated with different functions: the N-terminal GTPase domain to binds and hydrolyzes GTP; pleckstrin homology (PH) domains, which bind acidic membrane phospholipids; and C-terminal proline rich (PR) domains that mediate protein-protein interactions. Dynamin-like proteins, which assist in recruiting classical dynamins to cleave vesicles from the cell membrane, lack PH and PR domains.

Dynamins are associated with a range of disorders including, but not limited to, Alzheimer's disease, cancer metastasis, epilepsy, Huntington's disease and Parkinson's disease. Mutations in the dynamin II gene have been linked to two neuromuscular diseases; Centronuclear myopathy, and intermediate and axonal forms of Charcot-Marie Tooth disease.

External sources of pharmacological information for Dynamin :

• BJP Guide

Dynamin Gene Data