Premium
The PX‐BAR membrane‐remodeling unit of sorting nexin 9
Author(s) -
Pylypenko Olena,
Lundmark Richard,
Rasmuson Erika,
Carlsson Sven R,
Rak Alexey
Publication year - 2007
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7601889
Subject(s) - sorting nexin , biology , sorting , bar (unit) , unit (ring theory) , microbiology and biotechnology , physics , computer science , mathematics , endosome , intracellular , mathematics education , meteorology , programming language
Sorting nexins (SNXs) form a family of proteins known to interact with components in the endosomal system and to regulate various steps of vesicle transport. Sorting nexin 9 (SNX9) is involved in the late stages of clathrin‐mediated endocytosis in non‐neuronal cells, where together with the GTPase dynamin, it participates in the formation and scission of the vesicle neck. We report here crystal structures of the functional membrane‐remodeling unit of SNX9 and show that it efficiently tubulates lipid membranes in vivo and in vitro . Elucidation of the protein superdomain structure, together with mutational analysis and biochemical and cell biological experiments, demonstrated how the SNX9 PX and BAR domains work in concert in targeting and tubulation of phosphoinositide‐containing membranes. The study provides insights into the SNX9‐induced membrane modulation mechanism.