Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 13, Issue 11, Pages 1029-1030Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1160
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Funding
- NIAID NIH HHS [AI51174, R01 AI051174] Funding Source: Medline
- NIGMS NIH HHS [P01 GM066521, GM66521] Funding Source: Medline
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The ESCRT-I and ESCRT-II complexes help sort ubiquitinated proteins into vesicles that accumulate within multivesicular bodies (MVBs). Crystallographic and biochemical analyses reveal that the GLUE domain of the human ESCRT-II EAP45 (also called VPS36) subunit is a split pleckstrin-homology domain that binds ubiquitin along one edge of the b-sandwich. The structure suggests how human ESCRT-II can couple recognition of ubiquitinated cargoes and endosomal phospholipids during MVB protein sorting.
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