ArticleMolecular biology of the cell2006
Ribosome binding to and dissociation from translocation sites of the endoplasmic reticulum membrane.
Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Cytosolic and ER-associated ribosomes share rRNA 2'-O-methylation landscapes across human cell types.RNA (New York, N.Y.) · 2026Article
- The Epstein-Barr virus deubiquitinase BPLF1 regulates stress-induced ribosome UFMylation and reticulophagy.Autophagy · 2025Article
- RPL26/uL24 UFMylation is essential for ribosome-associated quality control at the endoplasmic reticulum.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- RPL26/uL24 UFMylation is essential for ribosome-associated quality control at the endoplasmic reticulum.bioRxiv : the preprint server for biology · 2023Article
- Heterogeneous translational landscape of the endoplasmic reticulum revealed by ribosome proximity labeling and transcriptome analysis.The Journal of biological chemistry · 2019Article
- Mammalian SRP receptor switches the Sec61 translocase from Sec62 to SRP-dependent translocation.Nature communications · 2015Article
- Article
- Diversity and selectivity in mRNA translation on the endoplasmic reticulum.Nature reviews. Molecular cell biology · 2015Review
- Dynamic interaction of the sec translocon with the chaperone PpiD.The Journal of biological chemistry · 2014Article
- The bacterial translocon SecYEG opens upon ribosome binding.The Journal of biological chemistry · 2013Article
- Bacterial protein translocation requires only one copy of the SecY complex in vivo.The Journal of cell biology · 2012Article
- p180 promotes the ribosome-independent localization of a subset of mRNA to the endoplasmic reticulum.PLoS biology · 2012Article
- Ribosome distribution in HeLa cells during the cell cycle.PloS one · 2012Article
- Signal sequence-independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle.Molecular biology of the cell · 2011Article
- Interaction of calmodulin with Sec61α limits Ca2+ leakage from the endoplasmic reticulum.The EMBO journal · 2011Article
- Environmental transition of signal-anchor sequences during membrane insertion via the endoplasmic reticulum translocon.Molecular biology of the cell · 2010Article
- Regulation of the protein-conducting channel by a bound ribosome.Structure (London, England : 1993) · 2009Article
- Visualization of distinct entities of the SecYEG translocon during translocation and integration of bacterial proteins.Molecular biology of the cell · 2009Article
- Constitutive, translation-independent opening of the protein-conducting channel in the endoplasmic reticulum.Pflugers Archiv : European journal of physiology · 2009Article
- Sequence-specific retention and regulated integration of a nascent membrane protein by the endoplasmic reticulum Sec61 translocon.Molecular biology of the cell · 2009Article
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2 authors.
Funding
Abstract
We have addressed how ribosome-nascent chain complexes (RNCs), associated with the signal recognition particle (SRP), can be targeted to Sec61 translocation channels of the endoplasmic reticulum (ER) membrane when all binding sites are occupied by nontranslating ribosomes. These competing ribosomes are known to be bound with high affinity to tetramers of the Sec61 complex. We found that the membrane binding of RNC-SRP complexes does not require or cause the dissociation of prebound nontranslating ribosomes, a process that is extremely slow. SRP and its receptor target RNCs to a free population of Sec61 complex, which associates with nontranslating ribosomes only weakly and is conformationally different from the population of ribosome-bound Sec61 complex. Taking into account recent structural data, we propose a model in which SRP and its receptor target RNCs to a Sec61 subpopulation of monomeric or dimeric state. This could explain how RNC-SRP complexes can overcome the competition by nontranslating ribosomes.
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