ArticlePflugers Archiv : European journal of physiology2009
Constitutive, translation-independent opening of the protein-conducting channel in the endoplasmic reticulum.
Article in Pflugers Archiv : European journal of physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- Review
- Sec61 complex/translocon: The role of an atypical ER CaFrontiers in physiology · 2022Review
- Voltage Sensing in Bacterial Protein Translocation.Biomolecules · 2020Article
- Aberrant expression of Sec61α in esophageal cancers.Journal of cancer research and clinical oncology · 2019Article
- Driving Forces of Translocation Through Bacterial Translocon SecYEG.The Journal of membrane biology · 2018Article
- Structure of the native Sec61 protein-conducting channel.Nature communications · 2015Article
- The bacterial translocon SecYEG opens upon ribosome binding.The Journal of biological chemistry · 2013Article
- Reconciling the roles of kinetic and thermodynamic factors in membrane-protein insertion.Journal of the American Chemical Society · 2013Article
- Applications of the molecular dynamics flexible fitting method.Journal of structural biology · 2011Article
- Interaction of calmodulin with Sec61α limits Ca2+ leakage from the endoplasmic reticulum.The EMBO journal · 2011Article
- The SecY complex forms a channel capable of ionic discrimination.EMBO reports · 2009Article
- Let's talk about Secs: Sec61, Sec62 and Sec63 in signal transduction, oncology and personalized medicine.Signal transduction and targeted therapyReview
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Secretory and membrane proteins are translocated into the endoplasmic reticulum (ER) through a translocon assembled as a tetramer of Sec61 protein-conducting channels (PCC). How the opening of the PCCs in the tetramer is regulated through the protein translocation cycle is poorly understood. In this study, the permeability of PCCs in native ER membranes to small molecules was measured using fluorescence and electrophysiological techniques. Although the PCCs were closed at 4 degrees C, they were constitutively open at physiological temperatures in the absence of protein translation or a bound ribosome. The open PCCs occurred in clusters that are likely to correspond to the simultaneous opening of three or four PCCs in a translocon. The binding of 60S subunits to a ribosome-free membrane increased the number of open PCCs but did not increase the single-channel conductance. The translation-independent, constitutive opening of Sec61 PCCs provides new insight into the role of the translocon in the transport of small molecules across the ER membrane.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.