Abstract
Significance Coat proteins play a central role in the intracellular transport pathways by coupling two main functions: bending the membrane to generate transport carriers and binding to cargoes for their sorting into these carriers. Studies thus far have mostly solved the structure of coat proteins in solution, but their functional form requires assembly on the membrane into protein complexes. Here, we have pursued cryo-EM to reveal in molecular detail how SNX1 assembles on the membrane to deform the membrane. When compared to a previously solved retromer-SNX complex, our elucidation also suggests how retromer affects SNX in this complex as well as the intermediary stages of this coat assembly.
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