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Midbody Targeting of the ESCRT Machinery by a Noncanonical Coiled Coil in CEP55

Open access
Lee, Hyung Ho, Elia, Natalie, Ghirlando, Rodolfo, Lippincott-Schwartz, Jennifer, Hurley, James H.·2008·Science

Abstract

The ESCRT (endosomal sorting complex required for transport) machinery is required for the scission of membrane necks in processes including the budding of HIV-1 and cytokinesis. An essential step in cytokinesis is recruitment of the ESCRT-I complex and the ESCRT-associated protein ALIX to the midbody (the structure that tethers two daughter cells) by the protein CEP55. Biochemical experiments show that peptides from ALIX and the ESCRT-I subunit TSG101 compete for binding to the ESCRT and ALIX-binding region (EABR) of CEP55. We solved the crystal structure of EABR bound to an ALIX peptide at a resolution of 2.0 angstroms. The structure shows that EABR forms an aberrant dimeric parallel coiled coil. Bulky and charged residues at the interface of the two central heptad repeats create asymmetry and a single binding site for an ALIX or TSG101 peptide. Both ALIX and ESCRT-I are required for cytokinesis, which suggests that multiple CEP55 dimers are required for function.

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Metadata

Authors
Lee, H. H., Elia, N., Ghirlando, R., Lippincott-Schwartz, J., & Hurley, J. H.
Venue
Science
Published
2008-10-24
Volume
322
Issue
5901
Pages
576-580
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2065164168
Cited by
260
References
6
FWCI
6.44
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Midbody Targeting of the ESCRT Machinery by a Noncanonical Coiled Coil in CEP55. https://app.cochat.ai/papers/10.1126/science.1162042
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Lee, H. H., Elia, N., Ghirlando, R., Lippincott-Schwartz, J., & Hurley, J. H. (2008). Midbody Targeting of the ESCRT Machinery by a Noncanonical Coiled Coil in CEP55. Science. https://doi.org/10.1126/science.1162042

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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.