Structural basis for membrane insertion by the human ER membrane protein complex | Zendy

Tino Pleiner | Zendy; Giovani Pinton Tomaleri | Zendy; Kurt Januszyk | Zendy; Alison J. Inglis | Zendy; Masami Hazu | Zendy; Rebecca M. Voorhees | Zendy

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Structural basis for membrane insertion by the human ER membrane protein complex

Author(s) -

Tino Pleiner,

Giovani Pinton Tomaleri,

Kurt Januszyk,

Alison J. Inglis,

Masami Hazu,

Rebecca M. Voorhees

Publication year - 2020

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.abb5008

Subject(s) - membrane protein , integral membrane protein , endoplasmic reticulum , microbiology and biotechnology , membrane contact site , biogenesis , peripheral membrane protein , vesicle associated membrane protein 8 , protein targeting , lipid bilayer , biology , chemistry , membrane , biochemistry , gene

A defining step in the biogenesis of amembrane protein is the insertion of itshydrophobic transmembrane helices into the lipidbilayer. The nine-subunit endoplasmic reticulum(ER) membrane protein complex (EMC) is a conservedco- and posttranslational insertase at the ER. Wedetermined the structure of the human EMC in alipid nanodisc to an overall resolution of 3.4angstroms by cryo–electron microscopy, permittingbuilding of a nearly complete atomic model. Weused structure-guided mutagenesis to demonstratethat substrate insertion requires amethionine-rich cytosolic loop and occurs via anenclosed hydrophilic vestibule within the membraneformed by the subunits EMC3 and EMC6. We proposethat the EMC uses local membrane thinning and apositively charged patch to decrease the energeticbarrier for insertion into the bilayer.

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