ReviewThe Journal of cell biology2021
Capture and delivery of tail-anchored proteins to the endoplasmic reticulum.
Review in The Journal of cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 46 citations in OpenAlex.
- C-terminal tail of MAVS dictates organelle targeting and innate immune response.Cell communication and signaling : CCS · 2026Article
- ASNA1 is essential for cardiac development and function by regulating tail-anchored protein stability and vesicular transport in cardiomyocytes.PLoS genetics · 2025Article
- Navigating lipid droplet proteins - part I: ER targeting routes of lipid droplet-destined membrane proteins.Biochemical Society transactions · 2025Review
- Remote on-off switching of protein activity by intrinsically disordered region.Nature structural & molecular biology · 2025Article
- Genome-wide identification of modulators of Chlamydia trachomatis parasitophorous vacuole stability highlights an important role for sphingolipid supply.PLoS biology · 2025Article
- 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
- The DNase TREX1 is a substrate of the intramembrane protease SPP with implications for disease pathogenesis.Cellular and molecular life sciences : CMLS · 2025Article
- Article
- Identification of SLC35A1 as an essential host factor for the transduction of multi-serotype recombinant adeno-associated virus (AAV) vectors.bioRxiv : the preprint server for biology · 2024Article
- Cytoprotective Role of Autophagy in CDIP1 Expression-Induced Apoptosis in MCF-7 Breast Cancer Cells.International journal of molecular sciences · 2024Article
- SMA20/PMIS2 Is a Rapidly Evolving Sperm Membrane Alloantigen with Possible Species-Divergent Function in Fertilization.International journal of molecular sciences · 2024Article
- Article
- The GET insertase exhibits conformational plasticity and induces membrane thinning.Nature communications · 2023Article
- CRI-SPA: a high-throughput method for systematic genetic editing of yeast libraries.Nucleic acids research · 2023Article
- Article
- Identifying novel genes for amyotrophic lateral sclerosis by integrating human brain proteomes with genome-wide association data.Journal of neurology · 2023Article
- Article
- Review
- Protein Tyrosine Phosphatases: Mighty oaks from little acorns grow.IUBMB life · 2023Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tail-anchored (TA) proteins fulfill diverse cellular functions within different organellar membranes. Their characteristic C-terminal transmembrane segment renders TA proteins inherently prone to aggregation and necessitates their posttranslational targeting. The guided entry of TA proteins (GET in yeast)/transmembrane recognition complex (TRC in humans) pathway represents a major route for TA proteins to the endoplasmic reticulum (ER). Here, we review important new insights into the capture of nascent TA proteins at the ribosome by the GET pathway pretargeting complex and the mechanism of their delivery into the ER membrane by the GET receptor insertase. Interestingly, several alternative routes by which TA proteins can be targeted to the ER have emerged, raising intriguing questions about how selectivity is achieved during TA protein capture. Furthermore, mistargeting of TA proteins is a fundamental cellular problem, and we discuss the recently discovered quality control machineries in the ER and outer mitochondrial membrane for displacing mislocalized TA 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.