ArticleThe Journal of cell biology2012
Arginylation-dependent regulation of a proteolytic product of talin is essential for cell-cell adhesion.
Article in The Journal of cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 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
41 citing papers in PubMed, 63 citations in OpenAlex.
- Trypsin exhibits exopeptidase-like activity toward N-terminal arginine that biases proteomic analyses.bioRxiv : the preprint server for biology · 2026Article
- Review
- Methods to Study Arginylation of Tubulin.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Arginylation of ⍺-tubulin at E77 regulates microtubule dynamics via MAP1S.The Journal of cell biology · 2025Article
- Arginyltransferase 1 modulates p62-driven autophagy via mTORC1/AMPk signaling.Cell communication and signaling : CCS · 2024Article
- Protein Arginylation: Milestones of Discovery.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Arginylation Regulates Cytoskeleton Organization and Cell Division and Affects Mitochondria in Fission Yeast.Molecular and cellular biology · 2022Article
- The mechanical cell - the role of force dependencies in synchronising protein interaction networks.Journal of cell science · 2022Review
- Functional Interplay between Arginyl-tRNA Synthetases and Arginyltransferase.International journal of molecular sciences · 2022Article
- The evolutionarily conserved arginyltransferase 1 mediates a pVHL-independent oxygen-sensing pathway in mammalian cells.Developmental cell · 2022Article
- Article
- Heat stress induced arginylation of HuR promotes alternative polyadenylation of Hsp70.3 by regulating HuR stability and RNA binding.Cell death and differentiation · 2021Article
- Manipulation of Focal Adhesion Signaling by Pathogenic Microbes.International journal of molecular sciences · 2021Review
- Fourier Multiplexed Fluorescence Lifetime Imaging.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Posttranslational Arginylation Enzyme Arginyltransferase1 Shows Genetic Interactions With Specific Cellular PathwaysFrontiers in physiology · 2020Article
- Regulation of Mitochondrial Respiratory Chain Complex Levels, Organization, and Function by Arginyltransferase 1.Frontiers in cell and developmental biology · 2020Article
- Ate1-mediated posttranslational arginylation affects substrate adhesion and cell migration in Dictyostelium discoideum.Molecular biology of the cell · 2019Article
- Reduced Arginyltransferase 1 is a driver and a potential prognostic indicator of prostate cancer metastasis.Oncogene · 2019Article
- Adhesions Assemble!-Autoinhibition as a Major Regulatory Mechanism of Integrin-Mediated Adhesion.Frontiers in molecular biosciences · 2019Review
- Posttranscriptional and Posttranslational Regulation of Actin.Anatomical record (Hoboken, N.J. : 2007) · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Talin is a large scaffolding molecule that plays a major role in integrin-dependent cell-matrix adhesion. A role for talin in cell-cell attachment through cadherin has never been demonstrated, however. Here, we identify a novel calpain-dependent proteolytic cleavage of talin that results in the release of a 70-kD C-terminal fragment, which serves as a substrate of posttranslational arginylation. The intracellular levels of this fragment closely correlated with the formation of cell-cell adhesions, and this fragment localized to cadherin-containing cell-cell contacts. Moreover, reintroduction of this fragment rescued the cell-cell adhesion defects in arginyltransferase (Ate1) knockout cells, which normally have a very low level of this fragment. Arginylation of this fragment further enhanced its ability to rescue cell-cell adhesion formation. In addition, arginylation facilitated its turnover, suggesting a dual role of arginylation in its intracellular regulation. Thus, our work identifies a novel proteolytic product of talin that is regulated by arginylation and a new role of talin in cadherin-dependent cell-cell adhesion.
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.