Retromer oligomerization drives SNX-BAR coat assembly and membrane constriction

ABSTRACT: Proteins exit from endosomes through tubular carriers coated by retromer, a complex that impacts cellular signaling, lysosomal biogenesis, and numerous diseases. The coat must overcome membrane tension to form tubules. We explored the dynamics and driving force of this process by reconstituting coat formation with yeast retromer and the BAR-domain sorting nexins Vps5 and Vps17 on oriented synthetic lipid tubules. This coat oligomerizes bidirectionally, forming a static tubular structure that does not exchange subunits. High concentrations of sorting nexins alone constrict membrane tubes to an invariant radius of 19 nm. At lower concentrations, oligomers of retromer must bind and interconnect the sorting nexins to drive constriction. Constricting less curved membranes into tubes, which re

SUBMITTER: Prof. Andreas Mayer 

PROVIDER: S-SCDT-10_15252-EMBJ_2022112287 | biostudies-other |

REPOSITORIES: biostudies-other