AQP5 trafficking is regulated by its C-terminal tail and interaction with prolactin-inducible protein

In summary, this study advances our understanding of AQP5 trafficking dynamics and provides critical insights into the regulatory roles of the C-terminal tail and its interaction with PIP. The innovative methodology to assess AQP5 translocation to the plasma membrane sets the stage for future investigations to identify the role of individual amino acids and phosphorylation sites within the distal AQP5 C-terminus in the trafficking mechanism and protein-protein interaction, and to explore the dynamic of the process by high resolution live cell imaging. Further research in this area is warranted to uncover critical insights into the regulation of AQP5, offering opportunities for the development of innovative therapeutic strategies.

Authors

Institutions

Publication Details

Journal
Biology Direct
Published
2025-04-16
DOI
https://doi.org/10.1186/s13062-025-00647-6
Citations
2
Primary Topic
Ion Transport and Channel Regulation
Type
article
Field-Weighted Citation Impact
1.61

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

AQP5 trafficking is regulated by its C-terminal tail and interaction with prolactin-inducible protein

Françoise Grégoire, Jason Perret, Nargis Bolaky, Susanna Törnroth‐Horsefield et al.
2 citations
Biology Direct
Ion Transport and Channel Regulation
1.61
article

AQP5 trafficking is regulated by its C-terminal tail and interaction with prolactin-inducible protein

Françoise Grégoire, Jason Perret, Nargis Bolaky, Susanna Törnroth‐Horsefield, Christine Delporte, Egor Zindy, Louise Conrard, Claudia D’Agostino, Amel Takkal
article en
2 citations

Abstract

In summary, this study advances our understanding of AQP5 trafficking dynamics and provides critical insights into the regulatory roles of the C-terminal tail and its interaction with PIP. The innovative methodology to assess AQP5 translocation to the plasma membrane sets the stage for future investigations to identify the role of individual amino acids and phosphorylation sites within the distal AQP5 C-terminus in the trafficking mechanism and protein-protein interaction, and to explore the dynamic of the process by high resolution live cell imaging. Further research in this area is warranted to uncover critical insights into the regulation of AQP5, offering opportunities for the development of innovative therapeutic strategies.

Biology DirectVol. 20(1)
Université Libre de Bruxelles (BE), Lund University (SE)
Fonds De La Recherche Scientifique - FNRS, University of Tokushima
Openalex Percentile: Top 18%
Ion Transport and Channel Regulation
1.61
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.

AQP5 trafficking is regulated by its C-terminal tail and interaction with prolactin-inducible protein — Françoise Grégoire, Jason Perret, et al. · Biology Direct (2025) | TGRS Research Map | TGRS