Abstract
Almost all secreted proteins pass through the endoplasmic reticulum (ER), an organelle that is equipped to tolerate and/or degrade misfolded proteins. We report here that yeast expressing the cystic fibrosis transmembrane conductance regulator (CFTR) concentrate the protein at defined sites in the ER membrane that are not necessarily enriched for the ER molecular chaperone BiP. We propose that these sites are Russell bodies, an ER subcompartment in which misfolded proteins are stored and can be targeted for degradation.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Carrier Proteins / metabolism*
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Cystic Fibrosis Transmembrane Conductance Regulator / metabolism*
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Endoplasmic Reticulum / metabolism*
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Endoplasmic Reticulum / ultrastructure
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Endoplasmic Reticulum Chaperone BiP
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Heat-Shock Proteins*
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Microscopy, Immunoelectron
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Molecular Chaperones / metabolism*
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Yeasts / metabolism*
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Yeasts / ultrastructure
Substances
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Carrier Proteins
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Endoplasmic Reticulum Chaperone BiP
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Heat-Shock Proteins
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Molecular Chaperones
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Cystic Fibrosis Transmembrane Conductance Regulator