Do different SNX-BAR proteins define distinct tubular elements of the tubulovesicular early endosome?
All of the mammalian SNX-BAR proteins contain, in addition to the SNX-PX domain, a membrane-binding carboxy-terminal BAR (Bin/amphiphysin/Rvs) domain. This is a dimerisation motif that forms a rigid curved structure, the concave face of which constitutes a membrane binding surface which preferentially interacts with membranes of positive curvature, as found on small vesicles or narrow diameter membrane tubules. In some instances, for example SNX1, BAR domain-containing proteins can induce the formation of high curvature membrane tubules through the formation of a polymerised helical coat. Indeed, the mammalian retromer SNX-BAR coat complex generates and defines the ETC tubular sub-domain of the early endosome. The ability of SNX-BARs to drive tubule formation is of particular interest given that tubular elements of the early endocytic network are known to constitute sorting platforms, for example ETCs and the TSE/TEN.
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