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dc.contributor.authorKnoblich, Konstantin
dc.contributor.authorPark, Soohyung
dc.contributor.authorCall, Matthew E.
dc.contributor.authorCall, Melissa J.
dc.contributor.authorIm, Wonpil
dc.date.accessioned2016-11-14T18:47:03Z
dc.date.available2016-11-14T18:47:03Z
dc.date.issued2015-05-26
dc.identifier.citationKnoblich, K., Park, S., Lutfi, M., van’t Hag, L., Conn, C. E., Seabrook, S. A., ... & Call, M. J. (2015). Transmembrane complexes of DAP12 crystallized in lipid membranes provide insights into control of oligomerization in immunoreceptor assembly. Cell reports, 11(8), 1184-1192.en_US
dc.identifier.urihttp://hdl.handle.net/1808/21957
dc.description.abstractThe membrane-spanning α helices of single-pass receptors play crucial roles in stabilizing oligomeric structures and transducing biochemical signals across the membrane. Probing intermolecular transmembrane interactions in single-pass receptors presents unique challenges, reflected in a gross underrepresentation of their membrane-embedded domains in structural databases. Here, we present two high-resolution structures of transmembrane assemblies from a eukaryotic single-pass protein crystallized in a lipidic membrane environment. Trimeric and tetrameric structures of the immunoreceptor signaling module DAP12, determined to 1.77-Å and 2.14-Å resolution, respectively, are organized by the same polar surfaces that govern intramembrane assembly with client receptors. We demonstrate that, in addition to the well-studied dimeric form, these trimeric and tetrameric structures are made in cells, and their formation is competitive with receptor association in the ER. The polar transmembrane sequences therefore act as primary determinants of oligomerization specificity through interplay between charge shielding and sequestration of polar surfaces within helix interfaces.en_US
dc.publisherElsevieren_US
dc.rightsCopyright © 2015 The Authorsen_US
dc.titleTransmembrane Complexes of DAP12 Crystallized in Lipid Membranes Provide Insights into Control of Oligomerization in Immunoreceptor Assemblyen_US
dc.typeArticleen_US
kusw.kuauthorIm, Wonpil
kusw.kudepartmentMolecular Biosciencesen_US
dc.identifier.doi10.1016/j.celrep.2015.04.045en_US
dc.identifier.orcidhttps://orcid.org/0000-0002-4883-3031
kusw.oaversionScholarly/refereed, publisher versionen_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US
dc.rights.accessrightsopenAccess


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