ArticleThe Journal of biological chemistry2019
Transmembrane insertases and
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed, 46 citations in OpenAlex.
- Pairwise transmembrane domain insertion during multipass protein biogenesis.Molecular cell · 2026Article
- MicroRNA-223-3p is a determinant of platelet procoagulant activity.Blood advances · 2026Article
- Article
- Rules of Engagement for Components of Membrane Protein Biogenesis at the Human Endoplasmic Reticulum.International journal of molecular sciences · 2025Review
- MGAT1-Guided complex N-Glycans on CD73 regulate immune evasion in triple-negative breast cancer.Nature communications · 2025Article
- Electrosome assembly: Structural insights from high voltage-activated calcium channel (CaV)-chaperone interactions.Biochemical Society transactions · 2025Review
- Identification of a factor that accelerates substrate release from the signal recognition particle.Science (New York, N.Y.) · 2024Article
- Article
- Review
- The odyssey of the TR(i)P journey to the cellular membrane.Frontiers in cell and developmental biology · 2024Review
- Human Transient Receptor Potential Ankyrin 1 Channel: Structure, Function, and Physiology.Sub-cellular biochemistry · 2024Review
- Quantitative Mass Spectrometry Characterizes Client Spectra of Components for Targeting of Membrane Proteins to and Their Insertion into the Membrane of the Human ER.International journal of molecular sciences · 2023Review
- EMC chaperone-CaNature · 2023Article
- The Biogenesis of Multipass Membrane Proteins.Cold Spring Harbor perspectives in biology · 2023Review
- Transient receptor potential canonical type 6 (TRPC6) O-GlcNAcylation at Threonine-221 plays potent role in channel regulation.iScience · 2023Article
- Apolipoprotein L1 (APOL1) cation current in HEK-293 cells and in human podocytes.Pflugers Archiv : European journal of physiology · 2023Article
- Ion channels and channelopathies in glomeruli.Physiological reviews · 2023Review
- Article
- Proteomics Identifies Substrates and a Novel Component in hSnd2-Dependent ER Protein Targeting.Cells · 2022Article
- The mechanisms of integral membrane protein biogenesis.Nature reviews. Molecular cell biology · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Transient receptor potential cation channel subfamily C member 6 (TRPC6) is a widely expressed ion channel. Gain-of-function mutations in the human TRPC6 channel cause autosomal-dominant focal segmental glomerulosclerosis, but the molecular components involved in disease development remain unclear. Here, we found that overexpression of gain-of-function TRPC6 channel variants is cytotoxic in cultured cells. Exploiting this phenotype in a genome-wide CRISPR/Cas screen for genes whose inactivation rescues cells from TRPC6-associated cytotoxicity, we identified several proteins essential for TRPC6 protein expression, including the endoplasmic reticulum (ER) membrane protein complex transmembrane insertase. We also identified transmembrane protein 208 (TMEM208), a putative component of a signal recognition particle-independent (SND) ER protein-targeting pathway, as being necessary for expression of TRPC6 and several other ion channels and transporters. TRPC6 expression was also diminished by loss of the previously uncharacterized WD repeat domain 83 opposite strand (WDR83OS), which interacted with both TRPC6 and TMEM208. Additionally enriched among the screen hits were genes involved in
Indexed as
Identifiers
What OpenQuestion holds
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.