Membrane trafficking and spinogenesis contribute significantly to changes in synaptic strength during development and in various paradigms of synaptic plasticity. 
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.
http://www.cell.com/cell-reports/abstract/S2211-1247(15)00702-0