ArticleiScience2026
Variant-specific interaction of kinectin 1 with the multi-tRNA synthetase complex regulates ER sheet organization.
Article in iScience, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
- The ER anchoring and abundance of the EEF1B complex is affected by tissue-specific alternative EEF1D splicing.Life science alliance · 2026Article
- Inferring translational efficiency from transcriptomes improves noncanonical neoantigen prioritization and cancer patient stratification.NPJ precision oncology · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Kinectin 1 (KTN1) is an integral endoplasmic reticulum (ER) sheet protein involved in ER organization and translation elongation. Alternative splicing introduces sequence diversity into the cytosolic region of KTN1; however, the functional significance of these variants has remained unclear. Here, we show that the multi-tRNA synthetase complex (MSC), composed of eight aminoacyl-tRNA synthetases and three nonenzymatic proteins, specifically interacts with KTN1 in a manner dependent on the alternative exon V2 and glutamine-tRNA synthetase (QARS). Using V2 exon-specific knockout cells and KTN1 knockout cells with variant-specific rescue, we found that the V2 exon is required for KTN1-mediated recruitment of the MSC to the ER, where it facilitates the formation of rough ER stacks. These findings define a variant-specific role for KTN1 in anchoring the MSC to the ER and suggest that this interaction underlies a noncanonical function of the MSC in regulating ER sheet organization.
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.