NAA10 and BTRC drive CREBRF degradation in endoplasmic reticulum stress and renal tubular injury
Sitian Fang, Jing Ning, Jinjing Huang, Yanxia Chen · 2026
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Description
Fang and co-authors unravel, in 2026, how the protective protein CREBRF gets destroyed in diabetic kidney disease, worsening stress inside kidney tubule cells. CREBRF normally restrains endoplasmic reticulum stress, the protein-folding overload that injures tubules under high glucose. Working in HK-2 tubule cells exposed to high glucose and in streptozotocin-diabetic mice, injected at 50 milligrams per kilogram, they traced CREBRF's regulation upward.
CREBRF was downregulated in the disease models, and restoring it calmed endoplasmic reticulum stress and reduced tubule injury. The acetylation enzyme NAA10 tags CREBRF with an acetyl group, and that tag invites the ubiquitin ligase BTRC to mark CREBRF for degradation, a disposal signal. Blocking the chain preserved CREBRF and its protection. Diabetic status in the mice was confirmed at blood glucose of 250 milligrams per deciliter or higher. The authors name the NAA10-BTRC-CREBRF axis as a candidate intervention point in diabetic kidney disease.
Catalog record
| CREATOR | Sitian Fang, Jing Ning, Jinjing Huang, Yanxia Chen |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 38 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |