ArticleMolecular and cellular biology2016
Cotranslational Intersection between the SRP and GET Targeting Pathways to the Endoplasmic Reticulum of Saccharomyces cerevisiae.
Article in Molecular and cellular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- The cotranslational cycle of the ribosome-bound Hsp70 homolog Ssb.Nature communications · 2026Article
- Characterisation of guided entry of tail-anchored proteins in Magnaporthe oryzae.PLoS pathogens · 2025Article
- The formation of chaperone-rich GET bodies depends on the tetratricopeptide repeat region of Sgt2 and is reversed by NADH.Journal of cell science · 2025Article
- Stalled disomes marked by Hel2-dependent ubiquitin chains undergo Ubp2/Ubp3-mediated deubiquitination upon translational run-off.Communications biology · 2025Article
- A conserved guided entry of tail-anchored pathway is involved in the trafficking of a subset of membrane proteins in Plasmodium falciparum.PLoS pathogens · 2021Article
- Capture and delivery of tail-anchored proteins to the endoplasmic reticulum.The Journal of cell biology · 2021Review
- Article
- Ribosome-bound Get4/5 facilitates the capture of tail-anchored proteins by Sgt2 in yeast.Nature communications · 2021Article
- Posttranslational insertion of small membrane proteins by the bacterial signal recognition particle.PLoS biology · 2020Article
- SGTA associates with nascent membrane protein precursors.EMBO reports · 2020Article
- A structural perspective on tail-anchored protein biogenesis by the GET pathway.Current opinion in structural biology · 2018Review
- Hsp90-downregulation influences the heat-shock response, innate immune response and onset of oocyte development in nematodes.PloS one · 2017Article
- Interaction of the cotranslational Hsp70 Ssb with ribosomal proteins and rRNA depends on its lid domain.Nature communications · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Targeting of transmembrane proteins to the endoplasmic reticulum (ER) proceeds via either the signal recognition particle (SRP) or the guided entry of tail-anchored proteins (GET) pathway, consisting of Get1 to -5 and Sgt2. While SRP cotranslationally targets membrane proteins containing one or multiple transmembrane domains, the GET pathway posttranslationally targets proteins containing a single C-terminal transmembrane domain termed the tail anchor. Here, we dissect the roles of the SRP and GET pathways in the sorting of homologous, two-membrane-spanning K(+) channel proteins termed Kcv, Kesv, and Kesv-VV. We show that Kcv is targeted to the ER cotranslationally via its N-terminal transmembrane domain, while Kesv-VV is targeted posttranslationally via its C-terminal transmembrane domain, which recruits Get4-5/Sgt2 and Get3. Unexpectedly, nascent Kcv recruited not only SRP but also the Get4-5 module of the GET pathway to ribosomes. Ribosome binding of Get4-5 was independent of Sgt2 and was strongly outcompeted by SRP. The combined data indicate a previously unrecognized cotranslational interplay between the SRP and GET pathways.
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