ArticleInternational journal of molecular sciences2021
C-Terminal Domain of Aquaporin-5 Is Required to Pass Its Protein Quality Control and Ensure Its Trafficking to Plasma Membrane.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 8 papers.
What it found
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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
8 citing papers in PubMed, 12 citations in OpenAlex.
- Correction: Muroi, S.-i.; Isohama, Y. C-Terminal Domain of Aquaporin-5 Is Required to Pass Its Protein Quality Control and Ensure Its Trafficking to Plasma Membrane.International journal of molecular sciences · 2025Article
- CLIP2: a novel functional player in AQP5 trafficking dynamics and implications for Sjögren's disease.Cell communication and signaling : CCS · 2025Article
- AQP5 trafficking is regulated by its C-terminal tail and interaction with prolactin-inducible protein.Biology direct · 2025Article
- Role of aquaporins in brain water transport and edema.Frontiers in neuroscience · 2025Review
- Aquaporin-5 Dynamic Regulation.International journal of molecular sciences · 2023Review
- Protein Structure and Modification of Aquaporins.Advances in experimental medicine and biology · 2023Article
- Article
- Differentially Aquaporin 5 Expression in Submandibular Glands and Cerebral Cortex in Alzheimer's Disease.Biomedicines · 2022Article
Corrections and comments
- Erratum issued
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aquaporin-5 (AQP5) is selectively expressed in the apical membrane of exocrine glands, such as salivary, lacrimal, and submucosal glands. It is important for the secretory function of exocrine glands because mice with the knockout of AQP5 exhibit a significant reduction in secretion from these glands. Previous reports indicated that the AQP5 C-terminal domain is crucial for the localization of AQP5 at the plasma membrane, but it remains unclear which motif or amino acid residues in the C-terminal domain are essential for this. In this study, we examined the effects of various AQP5 C-terminal deletions or mutations on the expression of AQP5 on the cell surface. AQP5 C-terminal domain mutants did not localize on the plasma membrane, and Leu
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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.