Structural highlights
Function
[MB12B_HUMAN] Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies.
Publication Abstract from PubMed
MVB12-associated beta-prism (MABP) domains are predicted to occur in a diverse set of membrane-associated bacterial and eukaryotic proteins, but their existence, structure, and biochemical properties have not been characterized experimentally. Here, we find that the MABP domains of the MVB12A and B subunits of ESCRT-I are functional modules that bind in vitro to liposomes containing acidic lipids depending on negative charge density. The MABP domain is capable of autonomously localizing to subcellular puncta and to the plasma membrane. The 1.3-A atomic resolution crystal structure of the MVB12B MABP domain reveals a beta-prism fold, a hydrophobic membrane-anchoring loop, and an electropositive phosphoinositide-binding patch. The basic patch is open, which explains how it senses negative charge density but lacks stereoselectivity. These observations show how ESCRT-I could act as a coincidence detector for acidic phospholipids and protein ligands, enabling it to function both in protein transport at endosomes and in cytokinesis and viral budding at the plasma membrane.
Structural basis for membrane targeting by the MVB12-associated beta-prism domain of the human ESCRT-I MVB12 subunit.,Boura E, Hurley JH Proc Natl Acad Sci U S A. 2012 Feb 7;109(6):1901-6. Epub 2012 Jan 9. PMID:22232651[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Boura E, Hurley JH. Structural basis for membrane targeting by the MVB12-associated beta-prism domain of the human ESCRT-I MVB12 subunit. Proc Natl Acad Sci U S A. 2012 Feb 7;109(6):1901-6. Epub 2012 Jan 9. PMID:22232651 doi:http://dx.doi.org/10.1073/pnas.1117597109
