ArticleThe Journal of biological chemistry2020
DHHC7-mediated palmitoylation of the accessory protein barttin critically regulates the functions of ClC-K chloride channels.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Description of the novel variant c.784delG;p. (Ala262Profs*68) atBiomedical reports · 2026Article
- Palmitoylation in Renal Physiology and Pathology.Biomolecules · 2026Review
- Post-translational protein S-palmitoylation in renal tubular injury: mechanisms and therapeutic implications.Frontiers in cell and developmental biology · 2026Review
- Global analysis of membrane protein S-acylation in the model plantbioRxiv : the preprint server for biology · 2025Article
- Palmitoylation of Voltage-Gated Ion Channels.International journal of molecular sciences · 2022Review
- RFCM-PALM: In-Silico Prediction of S-Palmitoylation Sites in the Synaptic Proteins for Male/Female Mouse Data.International journal of molecular sciences · 2021Article
- S-Palmitoylation of Synaptic Proteins as a Novel Mechanism Underlying Sex-Dependent Differences in Neuronal Plasticity.International journal of molecular sciences · 2021Article
- Bartter's syndrome: clinical findings, genetic causes and therapeutic approach.World journal of pediatrics : WJP · 2021Review
- Proteasomal and lysosomal degradation for specific and durable suppression of immunotherapeutic targets.Cancer biology & medicine · 2020Review
Corrections and comments
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Authors and funding
20 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Barttin is the accessory subunit of the human ClC-K chloride channels, which are expressed in both the kidney and inner ear. Barttin promotes trafficking of the complex it forms with ClC-K to the plasma membrane and is involved in activating this channel. Barttin undergoes post-translational palmitoylation that is essential for its functions, but the enzyme(s) catalyzing this post-translational modification is unknown. Here, we identified zinc finger DHHC-type containing 7 (DHHC7) protein as an important barttin palmitoyl acyltransferase, whose depletion affected barttin palmitoylation and ClC-K-barttin channel activation. We investigated the functional role of barttin palmitoylation
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