ArticleThe Journal of cell biology2009
The structural and functional coupling of two molecular machines, the ribosome and the translocon.
Article in The Journal of cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Viral Infections and Their Ability to Modulate Endoplasmic Reticulum Stress Response Pathways.Viruses · 2024Review
- Pharmacologic Approaches for Adapting Proteostasis in the Secretory Pathway to Ameliorate Protein Conformational Diseases.Cold Spring Harbor perspectives in biology · 2020Review
- Cotranslational folding inhibits translocation from within the ribosome-Sec61 translocon complex.Nature structural & molecular biology · 2014Article
- Membrane protein TM segments are retained at the translocon during integration until the nascent chain cues FRET-detected release into bulk lipid.Molecular cell · 2012Article
- Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis.Cold Spring Harbor perspectives in biology · 2011Review
- Polytopic membrane protein folding at L17 in the ribosome tunnel initiates cyclical changes at the translocon.The Journal of cell biology · 2011Article
- Transmembrane segments of nascent polytopic membrane proteins control cytosol/ER targeting during membrane integration.The Journal of cell biology · 2011Article
- The liposoluble proteome of Mycoplasma agalactiae: an insight into the minimal protein complement of a bacterial membrane.BMC microbiology · 2010Article
- J domain co-chaperone specificity defines the role of BiP during protein translocation.The Journal of biological chemistry · 2010Article
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1 author.
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Abstract
Ribosomes synthesizing secretory and membrane proteins are bound to translocons at the membrane of the endoplasmic reticulum (ER). Both the ribosome and translocon are complex macromolecular machines whose structural and functional interactions are poorly understood. A new study by Pool (Pool, M.R. 2009. J. Cell Biol. 185:889-902) has now shown that the structure of the translocon is dictated by the identity of the protein being synthesized by the ribosome, thereby demonstrating that the two macromolecular machines are structurally coupled for functional purposes. The study also identifies an unexpected component in the apparent molecular linkage that connects the two machines, a discovery that shows the current view of translocon structure is oversimplified.
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