ArticleThe Journal of cell biology2007
Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocation.
Article in The Journal of cell biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
What it found
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Who cites it
46 citing papers in PubMed, 72 citations in OpenAlex.
- GTPase cycle and ER membrane regulate cargo handover during cotranslational protein targeting.Science advances · 2026Article
- Temporal Regulation of Signal Recognition Particle During Translation.Journal of molecular biology · 2025Article
- SRPassing Co-translational Targeting: The Role of the Signal Recognition Particle in Protein Targeting and mRNA Protection.International journal of molecular sciences · 2021Review
- Receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER.Science advances · 2021Article
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- A ribosome-associated chaperone enables substrate triage in a cotranslational protein targeting complex.Nature communications · 2020Article
- The SRP signal sequence of KdpD.Scientific reports · 2019Article
- GTP hydrolysis promotes disassembly of the atlastin crossover dimer during ER fusion.The Journal of cell biology · 2018Article
- Sequential activation of human signal recognition particle by the ribosome and signal sequence drives efficient protein targeting.Proceedings of the National Academy of Sciences of the United States of America · 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
- Regulation by a chaperone improves substrate selectivity during cotranslational protein targeting.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Co-translational protein targeting to the bacterial membrane.Biochimica et biophysica acta · 2014Review
- Inefficient translocation of preproinsulin contributes to pancreatic β cell failure and late-onset diabetes.The Journal of biological chemistry · 2014Article
- YlxM is a newly identified accessory protein that influences the function of signal recognition particle pathway components in Streptococcus mutans.Journal of bacteriology · 2014Article
- Fidelity of cotranslational protein targeting by the signal recognition particle.Annual review of biophysics · 2014Review
- The structural basis of FtsY recruitment and GTPase activation by SRP RNA.Molecular cell · 2013Article
- Structural basis of signal sequence surveillance and selection by the SRP-FtsY complex.Nature structural & molecular biology · 2013Article
- SecYEG activates GTPases to drive the completion of cotranslational protein targeting.The Journal of cell biology · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
During cotranslational protein targeting, two guanosine triphosphatase (GTPase) in the signal recognition particle (SRP) and its receptor (SR) form a unique complex in which hydrolyses of both guanosine triphosphates (GTP) are activated in a shared active site. It was thought that GTP hydrolysis drives the recycling of SRP and SR, but is not crucial for protein targeting. Here, we examined the translocation efficiency of mutant GTPases that block the interaction between SRP and SR at specific stages. Surprisingly, mutants that allow SRP-SR complex assembly but block GTPase activation severely compromise protein translocation. These mutations map to the highly conserved insertion box domain loops that rearrange upon complex formation to form multiple catalytic interactions with the two GTPs. Thus, although GTP hydrolysis is not required, the molecular rearrangements that lead to GTPase activation are essential for protein targeting. Most importantly, our results show that an elaborate rearrangement within the SRP-SR GTPase complex is required to drive the unloading and initiate translocation of cargo proteins.
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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.