Abstract
Ribosomes translating secretory and membrane proteins are targeted to the endoplasmic reticulum membrane and attach to the protein-conducting channel and ribosome-associated membrane proteins (RAMPs). Recently, a new RAMP, ERj1p, has been identified that recruits BiP to ribosomes and regulates translational activity. Here we present the cryo-EM structure of a ribosome-ERj1p complex, revealing how ERj1p coordinates the ribosome at the membrane and how allosteric effects may mediate ERj1p's regulatory activity.
Publication types
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Comparative Study
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Cryoelectron Microscopy
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Endoplasmic Reticulum / metabolism*
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Endoplasmic Reticulum Chaperone BiP
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Gene Expression Regulation / genetics*
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HSP40 Heat-Shock Proteins / metabolism*
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Heat-Shock Proteins / metabolism
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Membrane Proteins / chemistry*
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Membrane Proteins / metabolism
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Membrane Proteins / ultrastructure
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Mice
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Models, Molecular*
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Molecular Chaperones / metabolism
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Neoplasm Proteins / metabolism*
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Ribosomes / chemistry*
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Ribosomes / metabolism
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Ribosomes / ultrastructure
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Structure-Activity Relationship
Substances
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Dnajc1 protein, mouse
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Endoplasmic Reticulum Chaperone BiP
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HSP40 Heat-Shock Proteins
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Heat-Shock Proteins
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Membrane Proteins
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Molecular Chaperones
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Neoplasm Proteins