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Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex.

Im YJ, Hurley JH
Dev Cell 14 902-13 (2008)
Cited: 65 times
EuropePMC logo PMID: 18539118

Abstract

ESCRT-II plays a pivotal role in receptor downregulation and multivesicular body biogenesis and is conserved from yeast to humans. The crystal structures of two human ESCRT-II complex structures have been determined at 2.6 and 2.9 A resolution, respectively. The complex has three lobes and contains one copy each of VPS22 and VPS36 and two copies of VPS25. The structure reveals a dynamic helical domain to which both the VPS22 and VPS36 subunits contribute that connects the GLUE domain to the rest of the ESCRT-II core. Hydrodynamic analysis shows that intact ESCRT-II has a compact, closed conformation. ESCRT-II binds to the ESCRT-I VPS28 C-terminal domain subunit through a helix immediately C-terminal to the VPS36-GLUE domain. ESCRT-II is targeted to endosomal membranes by the lipid-binding activities of both the Vps36 GLUE domain and the first helix of Vps22. These data provide a unifying structural and functional framework for the ESCRT-II complex.

Reviews - 2zme mentioned but not cited (2)

  1. Membrane fission reactions of the mammalian ESCRT pathway. McCullough J, Colf LA, Sundquist WI. Annu Rev Biochem 82 663-692 (2013)
  2. Evolution: On a bender--BARs, ESCRTs, COPs, and finally getting your coat. Field MC, Sali A, Rout MP. J Cell Biol 193 963-972 (2011)

Articles - 2zme mentioned but not cited (2)

  1. Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex. Im YJ, Hurley JH. Dev Cell 14 902-913 (2008)
  2. Prediction of the tetramer protein complex interaction based on CNN and SVM. Lyu Y, He R, Hu J, Wang C, Gong X. Front Genet 14 1076904 (2023)


Reviews citing this publication (27)

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Articles citing this publication (34)

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