ArticleBMC cell biology2009
Functional characterization of the trans-membrane domain interactions of the Sec61 protein translocation complex beta-subunit.
Article in BMC cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- Comprehensive analysis of 1,771 transcriptomes from 7 tissues enhance genetic and biological interpretations of maize complex traits.G3 (Bethesda, Md.) · 2025Article
- Cancer associated mutations in Sec61γ alter the permeability of the ER translocase.PLoS genetics · 2021Article
- Article
- Disruption of vacuolar protein sorting components of the HOPS complex leads to enhanced secretion of recombinant proteins in Pichia pastoris.Microbial cell factories · 2019Article
- Membrane phospholipid alteration causes chronic ER stress through early degradation of homeostatic ER-resident proteins.Scientific reports · 2019Article
- Article
- The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron.The Journal of cell biology · 2015Article
- Direct association of the reticulon protein RTN1A with the ryanodine receptor 2 in neurons.Biochimica et biophysica acta · 2013Article
- A component of the Sec61 ER protein transporting pore is required for plant susceptibility to powdery mildew.Frontiers in plant science · 2013Article
- Sec61β controls sensitivity to platinum-containing chemotherapeutic agents through modulation of the copper-transporting ATPase ATP7A.Molecular pharmacology · 2012Article
- RTN/Nogo in forming Alzheimer's neuritic plaques.Neuroscience and biobehavioral reviews · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundIn eukaryotic cells co- and post-translational protein translocation is mediated by the trimeric Sec61 complex. Currently, the role of the Sec61 complex beta-subunit in protein translocation is poorly understood. We have shown previously that in Saccharomyces cerevisiae the trans-membrane domain alone is sufficient for the function of the beta-subunit Sbh1p in co-translational protein translocation. In addition, Sbh1p co-purifies not only with the protein translocation channel subunits Sec61p and Sss1p, but also with the reticulon family protein Rtn1p.
resultsWe used random mutagenesis to generate novel Sbh1p mutants in order to functionally map the Sbh1p trans-membrane domain. These mutants were analyzed for their interactions with Sec61p and how they support co-translational protein translocation. The distribution of mutations identifies one side of the Sbh1p trans-membrane domain alpha-helix that is involved in interactions with Sec61p and that is important for Sbh1p function in protein translocation. At the same time, these mutations do not affect Sbh1p interaction with Rtn1p. Furthermore we show that Sbh1p is found in protein complexes containing not only Rtn1p, but also the two other reticulon-like proteins Rtn2p and Yop1p.
conclusionOur results identify functionally important amino acids in the Sbh1p trans-membrane domain. In addition, our results provide additional support for the involvement of Sec61beta in processes unlinked to protein translocation.
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