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Cited by 256

The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.

Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B

Open access
Yang, Dong, Rismanchi, Neggy, Renvoisé, Benoît, Lippincott-Schwartz, Jennifer, Blackstone, Craig, Hurley, James H·2008·Nature Structural & Molecular Biology
DOI 10.1038/nsmb.1512
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Abstract

The endosomal sorting complex required for transport (ESCRT) machinery, including ESCRT-III, localizes to the midbody and participates in the membrane-abscission step of cytokinesis. The ESCRT-III protein charged multivesicular body protein 1B (CHMP1B) is required for recruitment of the MIT domain–containing protein spastin, a microtubule-severing enzyme, to the midbody. The 2.5-Å structure of the C-terminal tail of CHMP1B with the MIT domain of spastin reveals a specific, high-affinity complex involving a noncanonical binding site between the first and third helices of the MIT domain. The structural interface is twice as large as that of the MIT domain of the VPS4–CHMP complex, consistent with the high affinity of the interaction. A series of unique hydrogen-bonding interactions and close packing of small side chains discriminate against the other ten human ESCRT-III subunits. Point mutants in the CHMP1B binding site of spastin block recruitment of spastin to the midbody and impair cytokinesis.

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Metadata

Authors
Yang, D., Rismanchi, N., Renvoisé, B., Lippincott-Schwartz, J., Blackstone, C., & Hurley, J. H.
Venue
Nature Structural & Molecular Biology
Publisher
Springer Science and Business Media LLC
Published
2008-11-09
Volume
15
Issue
12
Pages
1278-1286
ISSN
  • 1545-9985 (ISSN-L)
  • 1545-9993
DOI
10.1038/nsmb.1512
OpenAlex
W2006463246
Cited by
256
References
4
FWCI
6.44
Type
journal article
Language
en
Open access
green

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