ArticleThe Journal of biological chemistry2010
Sss1p is required to complete protein translocon activation.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Cancer associated mutations in Sec61γ alter the permeability of the ER translocase.PLoS genetics · 2021Article
- The conserved C-terminus of Sss1p is required to maintain the endoplasmic reticulum permeability barrier.The Journal of biological chemistry · 2020Article
- Stability and function of the Sec61 translocation complex depends on the Sss1p tail-anchor sequence.The Biochemical journal · 2011Article
- Article
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Authors and funding
4 authors.
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Abstract
Protein translocation across the endoplasmic reticulum membrane occurs at the Sec61 translocon. This has two essential subunits, the channel-forming multispanning membrane protein Sec61p/Sec61α and the tail-anchored Sss1p/Sec61γ, which has been proposed to "clamp" the channel. We have analyzed the function of Sss1p using a series of domain mutants and found that both the cytosolic and transmembrane clamp domains of Sss1p are essential for protein translocation. Our data reveal that the cytosolic domain is required for Sec61p interaction but that the transmembrane clamp domain is required to complete activation of the translocon after precursor targeting to Sec61p.
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