Organisational and signalling cues in membranes Recently a new class of membrane shapers termed N Ank proteins (Wolf et al. 2019) were defined by their ability to bind sense and shape the membrane via their N Ank module which consists of an amino(N) terminal amphipathic helix and ankyrin repeats. N Ank family of membrane shapers is phylogenetically classified into two sub families and Ankyrin repeat domain containing protein (Ankrd) 24 an uncharacterised protein was suggested to be in their smaller sub family. Thus this study unveiled that Ankrd24 isoform 6 (Ankrd24x6) is one of the expressed isoforms in brains of 8 week old mice. Investigation of the N Ank properties of Ankrd24x6 using in vitro reconstitution assays with liposomes showed that it is an N Ank protein but with distinct characteristics. The N Ank module of Ankrd24x6 binds and shape the membrane and displayed that the presence of the putative amphipathic helix is quintessential for its binding. The predicted seven ankyrin repeats in Ankrd24x6 displayed lack of binding to the liposomes irrespective of their curvature. This property of Ankrd24x6 is distinct compared to the other members of the N Ank superfamily which showed that the ankyrin repeats alone preferred higher curvature liposomes. Ankrd24x6 is also capable of oligomerising as it demonstrated self association which was mediated by the predicted coiled coil domains. Another interesting feature of Ankrd24x6 is the presence of a proline rich motif via which it showed binding to the syndapin I protein. Syndapin I is involved in diverse crucial biological processes like synaptic vesicle recycling cytoskeletal remodelling dendritogenesis and ciliogenesis because it is capable of binding and shaping the membranes and can additionally interact with various proteins. ...