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-Structure paper
Title | Architecture of the ESCPE-1 membrane coat. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 30, Issue 7, Page 958-969, Year 2023 |
Publish date | Jun 15, 2023 |
![]() | Carlos Lopez-Robles / Stefano Scaramuzza / Elsa N Astorga-Simon / Morié Ishida / Chad D Williamson / Soledad Baños-Mateos / David Gil-Carton / Miguel Romero-Durana / Ander Vidaurrazaga / Juan Fernandez-Recio / Adriana L Rojas / Juan S Bonifacino / Daniel Castaño-Díez / Aitor Hierro / ![]() ![]() ![]() |
PubMed Abstract | Recycling of membrane proteins enables the reuse of receptors, ion channels and transporters. A key component of the recycling machinery is the endosomal sorting complex for promoting exit 1 (ESCPE-1) ...Recycling of membrane proteins enables the reuse of receptors, ion channels and transporters. A key component of the recycling machinery is the endosomal sorting complex for promoting exit 1 (ESCPE-1), which rescues transmembrane proteins from the endolysosomal pathway for transport to the trans-Golgi network and the plasma membrane. This rescue entails the formation of recycling tubules through ESCPE-1 recruitment, cargo capture, coat assembly and membrane sculpting by mechanisms that remain largely unknown. Herein, we show that ESCPE-1 has a single-layer coat organization and suggest how synergistic interactions between ESCPE-1 protomers, phosphoinositides and cargo molecules result in a global arrangement of amphipathic helices to drive tubule formation. Our results thus define a key process of tubule-based endosomal sorting. |
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Methods | EM (subtomogram averaging) / X-ray diffraction |
Resolution | 2.5 - 10.0 Å |
Structure data | EMDB-15413, PDB-8afz: ![]() PDB-8a1g: ![]() PDB-8abq: |
Chemicals | ![]() ChemComp-POL: ![]() ChemComp-HOH: ![]() ChemComp-PT: |
Source |
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![]() | PROTEIN TRANSPORT / SNX / Membrane trafficking. / TRANSPORT PROTEIN / Membrane trafficking / sorting nexins / PX domain / BAR domain / endosomes / retrograde transport / endocytic recycling / cargo recognition / protein coat / membrane recruitment / membrane deformation / membrane tubules. |