Abstract:
:Cells of multicellular organisms need to adopt specific morphologies. However, the molecular mechanisms bringing about membrane topology changes are far from understood-mainly because knowledge of membrane-shaping proteins that can promote local membrane curvatures is still limited. Our analyses unveiled that several members of a large, previously unrecognised protein family, which we termed N-Ank proteins, use a combination of their ankyrin repeat array and an amino (N)-terminal amphipathic helix to bind and shape membranes. Consistently, functional analyses revealed that the N-Ank protein ankycorbin (NORPEG/RAI14), which was exemplarily characterised further, plays an important, ankyrin repeat-based and N-terminal amphipathic helix-dependent role in early morphogenesis of neurons. This function furthermore required coiled coil-mediated self-assembly and manifested as ankycorbin nanodomains marked by protrusive membrane topologies. In summary, here, we unveil a class of powerful membrane shapers and thereby assign mechanistic and cell biological functions to the N-Ank protein superfamily.
journal_name
Nat Cell Bioljournal_title
Nature cell biologyauthors
Wolf D,Hofbrucker-MacKenzie SA,Izadi M,Seemann E,Steiniger F,Schwintzer L,Koch D,Kessels MM,Qualmann Bdoi
10.1038/s41556-019-0381-7subject
Has Abstractpub_date
2019-10-01 00:00:00pages
1191-1205issue
10eissn
1465-7392issn
1476-4679pii
10.1038/s41556-019-0381-7journal_volume
21pub_type
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