ArticleThe Journal of biological chemistry2016
Tail-anchored Protein Insertion in Mammals: FUNCTION AND RECIPROCAL INTERACTIONS OF THE TWO SUBUNITS OF THE TRC40 RECEPTOR.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 38 citations in OpenAlex.
- ASNA1 is essential for cardiac development and function by regulating tail-anchored protein stability and vesicular transport in cardiomyocytes.PLoS genetics · 2025Article
- Proteogenomic signature of Alzheimer's disease and related dementia risk in individuals with major depressive disorder.Nature. Mental health · 2025Article
- Characterisation of guided entry of tail-anchored proteins in Magnaporthe oryzae.PLoS pathogens · 2025Article
- Identification of C. elegans ASNA-1 domains and tissue requirements that differentially influence platinum sensitivity and growth control.PLoS genetics · 2022Article
- Proteomics Identifies Substrates and a Novel Component in hSnd2-Dependent ER Protein Targeting.Cells · 2022Article
- The Molecular Biodiversity of Protein Targeting and Protein Transport Related to the Endoplasmic Reticulum.International journal of molecular sciences · 2021Review
- Inhibitors of the Sec61 Complex and Novel High Throughput Screening Strategies to Target the Protein Translocation Pathway.International journal of molecular sciences · 2021Review
- 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
- Alternative redox forms of ASNA-1 separate insulin signaling from tail-anchored protein targeting and cisplatin resistance in C. elegans.Scientific reports · 2021Article
- Endoplasmic reticulum membrane receptors of the GET pathway are conserved throughout eukaryotes.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- Differential Modes of Orphan Subunit Recognition for the WRB/CAML Complex.Cell reports · 2020Article
- The WRB Subunit of the Get3 Receptor is Required for the Correct Integration of its Partner CAML into the ER.Scientific reports · 2019Article
- The Ways of Tails: the GET Pathway and more.The protein journal · 2019Review
- The peroxisome biogenesis factors posttranslationally target reticulon homology domain-containing proteins to the endoplasmic reticulum membrane.Scientific reports · 2018Article
- Mechanisms of Tail-Anchored Membrane Protein Targeting and Insertion.Annual review of cell and developmental biology · 2017Review
- Yet another hump for CAML: support of cell survival independent of tail-anchored protein insertion.Cell death & disease · 2017Article
- CAML mediates survival of Myc-induced lymphoma cells independent of tail-anchored protein insertion.Cell death discovery · 2017Article
- Mice lacking WRB reveal differential biogenesis requirements of tail-anchored proteins in vivo.Scientific reports · 2016Article
Corrections and comments
- Erratum issued
Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The GET (guided entry of tail-anchored proteins)/TRC (transmembrane recognition complex) pathway for tail-anchored protein targeting to the endoplasmic reticulum (ER) has been characterized in detail in yeast and is thought to function similarly in mammals, where the orthologue of the central ATPase, Get3, is known as TRC40 or Asna1. Get3/TRC40 function requires an ER receptor, which in yeast consists of the Get1/Get2 heterotetramer and in mammals of the WRB protein (tryptophan-rich basic protein), homologous to yeast Get1, in combination with CAML (calcium-modulating cyclophilin ligand), which is not homologous to Get2. To better characterize the mammalian receptor, we investigated the role of endogenous WRB and CAML in tail-anchored protein insertion as well as their association, concentration, and stoichiometry in rat liver microsomes and cultured cells. Functional proteoliposomes, reconstituted from a microsomal detergent extract, lost their activity when made with an extract depleted of TRC40-associated proteins or of CAML itself, whereas in vitro synthesized CAML and WRB together were sufficient to confer insertion competence to liposomes. CAML was found to be in ∼5-fold excess over WRB, and alteration of this ratio did not inhibit insertion. Depletion of each subunit affected the levels of the other one; in the case of CAML silencing, this effect was attributable to destabilization of the WRB transcript and not of WRB protein itself. These results reveal unanticipated complexity in the mutual regulation of the TRC40 receptor subunits and raise the question as to the role of the excess CAML in the mammalian ER.
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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.