P5A-ATPases constitute a distinct branch of the P-type ATPase superfamily implicated in endoplasmic reticulum (ER) quality control through the removal or reorientation of transmembrane segments. Although genetic and structural studies have suggested a role for these enzymes in transmembrane-helix handling, biochemical evidence linking substrate interaction to catalytic activity has remained limited....
✦ Clinical Takeaway ✦
No actionable change — this is a basic biochemistry study with no audiology relevance.
✦ Why It Matters ✦
This article has no meaningful relevance to audiology; it is a molecular biology study of protein-enzyme interactions in cellular quality control.
✦ Key Points ✦
- 01Examines how tail-anchored protein C-terminal domains activate the P5A-ATPase enzyme Spf1p.
- 02Relevant to basic cell biology and endoplasmic reticulum (ER) quality control research.
- 03Published in Journal of Biological Chemistry (2026).
- 04No clinical or hearing-related application identified.
- 05Findings are at the molecular/biochemical level only.
✦ Research metadata ✦
- PMID
- 42208892
- DOI
- 10.1016/j.jbc.2026.113205.
- Journal
- Journal of Biological Chemistry
- Publication type
- research_article
- Evidence level
- na
- Population
- In vitro / molecular biology (yeast/cell model)
- Intervention
- Tail-anchored protein C-terminal domain stimulation of Spf1p ATPase
Primary outcomes
ATP hydrolysis rate by P5A-ATPase Spf1p; Characterization of tail-anchored protein interactions