ArticleMolecular biology of the cell2013
Fingerloop activates cargo delivery and unloading during cotranslational protein targeting.
Article in Molecular biology of the cell, 2013. 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, 13 citations in OpenAlex.
- Take Me Home, Protein Roads: Structural Insights into Signal Peptide Interactions during ER Translocation.International journal of molecular sciences · 2021Review
- Molecular mechanism of cargo recognition and handover by the mammalian signal recognition particle.Cell reports · 2021Article
- Cotranslational protein targeting to the membrane: Nascent-chain transfer in a quaternary complex formed at the translocon.Scientific reports · 2018Article
- Article
- Domain Organization in the 54-kDa Subunit of the Chloroplast Signal Recognition Particle.Biophysical journal · 2016Article
- Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon.Nature communications · 2016Article
- Ribosome-SRP-FtsY cotranslational targeting complex in the closed state.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Allosteric response and substrate sensitivity in peptide binding of the signal recognition particle.The Journal of biological chemistry · 2014Article
- Co-translational protein targeting to the bacterial membrane.Biochimica et biophysica acta · 2014Review
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
During cotranslational protein targeting by the signal recognition particle (SRP), information about signal sequence binding in the SRP's M domain must be effectively communicated to its GTPase domain to turn on its interaction with the SRP receptor (SR) and thus deliver the cargo proteins to the membrane. A universally conserved "fingerloop" lines the signal sequence-binding groove of SRP; the precise role of this fingerloop in protein targeting has remained elusive. In this study, we show that the fingerloop plays important roles in SRP function by helping to induce the SRP into a more active conformation that facilitates multiple steps in the pathway, including efficient recruitment of SR, GTPase activation in the SRP•SR complex, and most significantly, the unloading of cargo onto the target membrane. On the basis of these results and recent structural work, we propose that the fingerloop is the first structural element to detect signal sequence binding; this information is relayed to the linker connecting the SRP's M and G domains and thus activates the SRP and SR for carrying out downstream steps in the pathway.
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Registered trials
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