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Science 24 October 2008:
Vol. 322. no. 5901, pp. 576 - 580
DOI: 10.1126/science.1162042
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Reports

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

Hyung Ho Lee,1 Natalie Elia,2 Rodolfo Ghirlando,1 Jennifer Lippincott-Schwartz,2 James H. Hurley1*

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.

1 Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892, USA.
2 Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892, USA.

* To whom correspondence should be addressed. E-mail: hurley{at}helix.nih.gov

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
The ESCRT machinery at a glance.
T. Wollert, D. Yang, X. Ren, H. H. Lee, Y. J. Im, and J. H. Hurley (2009)
J. Cell Sci. 122, 2163-2166
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No strings attached: the ESCRT machinery in viral budding and cytokinesis.
B. McDonald and J. Martin-Serrano (2009)
J. Cell Sci. 122, 2167-2177
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