GTPases of the dynamin family are key players regulating membrane trafficking. Scientists identify a brain-specific dynamin family GTPase, neurolastin (RNF112/Znf179), with closest homology to atlastin.
They demonstrate that neurolastin has functional GTPase and RING domains, making it a unique protein identified with this multi-enzymatic domain organization.
They also show that neurolastin is a peripheral membrane protein that localizes to endosomes and affects endosomal membrane dynamics via its RING domain.
In addition, neurolastin knockout mice have fewer dendritic spines, and rescue of the wild-type phenotype requires both the GTPase and RING domains. Furthermore, they find fewer functional synapses and reduced paired pulse facilitation in neurolastin knockout mice.
Thus, researchers identify neurolastin as a dynamin family GTPase that affects endosome size and spine density.