ArticleAmerican journal of physiology. Cell physiology2018
Identification of UT-A1- and AQP2-interacting proteins in rat inner medullary collecting duct.
Article in American journal of physiology. Cell physiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed, 18 citations in OpenAlex.
- Physiological Functions of Urea Transporters.Sub-cellular biochemistry · 2025Review
- Exploring the Functionality of the Krüppel-like Factors in Kidney Development, Metabolism, and Diseases.Life (Basel, Switzerland) · 2024Review
- Bayesian mapping of protein kinases to vasopressin-regulated phosphorylation sites in renal collecting duct.American journal of physiology. Renal physiology · 2024Article
- Proteomics and AQP2 regulation.The Journal of physiology · 2024Review
- Aldosterone Contributes to Vasopressin Escape through Changes in Water and Urea Transport.Biomedicines · 2023Article
- Phosphatases Decrease Water and Urea Permeability in Rat Inner Medullary Collecting Ducts.International journal of molecular sciences · 2023Article
- Insight into the Mammalian Aquaporin Interactome.International journal of molecular sciences · 2022Review
- LRBA is essential for urinary concentration and body water homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Surface proteomics and label-free quantification of Leptospira interrogans serovar Pomona.PLoS neglected tropical diseases · 2021Article
- Review
- THBS1/CD47 Modulates the Interaction of γ-Catenin With E-Cadherin and Participates in Epithelial-Mesenchymal Transformation in Lipid Nephrotoxicity.Frontiers in cell and developmental biology · 2020Article
- Phosphoproteomic identification of vasopressin V2 receptor-dependent signaling in the renal collecting duct.American journal of physiology. Renal physiology · 2019Article
- Mammalian urine concentration: a review of renal medullary architecture and membrane transporters.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2018Review
- From Molecules to Mechanisms: Functional Proteomics and Its Application to Renal Tubule Physiology.Physiological reviews · 2018Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
The urea channel UT-A1 and the water channel aquaporin-2 (AQP2) mediate vasopressin-regulated transport in the renal inner medullary collecting duct (IMCD). To identify the proteins that interact with UT-A1 and AQP2 in native rat IMCD cells, we carried out chemical cross-linking followed by detergent solubilization, immunoprecipitation, and LC-MS/MS analysis of the immunoprecipitated material. The analyses revealed 133 UT-A1-interacting proteins and 139 AQP2-interacting proteins, each identified in multiple replicates. Fifty-three proteins that were present in both the UT-A1 and the AQP2 interactomes can be considered as mediators of housekeeping interactions, likely common to all plasma membrane proteins. Among proteins unique to the UT-A1 list were those involved in posttranslational modifications: phosphorylation (protein kinases Cdc42bpb, Phkb, Camk2d, and Mtor), ubiquitylation/deubiquitylation (Uba1, Usp9x), and neddylation (Nae1 and Uba3). Among the proteins unique to the AQP2 list were several Rab proteins (Rab1a, Rab2a, Rab5b, Rab5c, Rab7a, Rab11a, Rab11b, Rab14, Rab17) involved in membrane trafficking. UT-A1 was found to interact with UT-A3, although quantitative proteomics revealed that most UT-A1 molecules in the cell are not bound to UT-A3. In vitro incubation of UT-A1 peptides with the protein kinases identified in the UT-A1 interactome revealed that all except Mtor were capable of phosphorylating known sites in UT-A1. Overall, the UT-A1 and AQP2 interactomes provide a snapshot of a dynamic process in which UT-A1 and AQP2 are produced in the rough endoplasmic reticulum, processed through the Golgi apparatus, delivered to endosomes that move into and out of the plasma membrane, and are regulated in the plasma membrane.
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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.