This entry includes senescence/dehydration-associated proteins from plants and Spartin from animals. This group of proteins share the C-terminal AAA ATPase domain [].Besides its C-terminal AAA ATPase domain, Spartin contains an N-terminal MIT (contained within microtubule-interacting and transport molecules) domain and a -P-P-x-Y- motif. Spastin monomers assemble into hexameric, ring-shaped ATPases that sever microtubules along their lengths [, ]. In flies, Spartin has been shown to regulates both synaptic development and neuronal survival by controlling microtubule stability via the BMP-dFMRP-Futsch pathway []. In humans, Spartin (also known as SPG20) has been linked to Troyer syndrome, characterised by spastic dysarthria, cognitive impairment, short stature, and distal muscle wasting in addition to lower extremity spastic weakness []. SPG20 has been shown to be recruited to the midbodyand participates in cytokinesis [].In plants, this group of proteins have been linked to senescence and dehydration [, ]. Different from their animal homologues, they don't have the MIT domain. In Hemerocallis, petals have a genetically based program that leads to senescence and cell death approximately 24 hours after the, flower opens, and it is believed that senescence proteins produced around that time have a role in this program [].
