Dynamins represent one of the subfamilies of GTP-binding proteins. These proteins share considerable sequence similarity over the N-terminal portion of the molecule, which contains the GTPase domain. Dynamins are associated with microtubules. They have been implicated in cell processes such as endocytosis and cell motility, and in alterations of the membrane that accompany certain activities such as bone resorption by osteoclasts. Dynamins bind many proteins that bind actin and other cytoskeletal proteins. Dynamins can also self-assemble, a process that stimulates GTPase activity. Five alternatively spliced transcripts encoding different proteins have been described. Additional alternatively spliced transcripts may exist, but their full-length nature has not been determined. [provided by RefSeq, Jun 2010]
Forensic Context
A study in mice demonstrated that the DNM2 is part of a common cosplicing network of glutamatergic synapse genes in brain reward circuitry, specifically identified in the ventral midbrain, prefrontal cortex, and nucleus accumbens of animals selectively bred for differential methamphetamine intake risk [Hitzemann et al. DOI:10.3390/brainsci9070155].