Neuropeptide Regulation of Aquaporin Intracellular Trafficking in Marine Teleost Rectal Enterocytes
- 1Institute of Marine Sciences, Spanish National Research Council (CSIC), 08003 Barcelona, Spain
- 2Institute of Biotechnology and Biomedicine (IBB), Universitat Autònoma de Barcelona, Bellaterra, 08193 Cerdanyola del Vallès, Spain
- 3Department of Biological Sciences, University of Bergen, 5006 Bergen, Norway
Abstract
In marine teleosts, the neuroendocrine regulation of aquaporin intracellular trafficking in osmoregulatory organs such as the intestinal rectum remains underexplored. By using paralog-specific antibodies, here we determined the subcellular localization of seven aquaporin and aquaglyceroporin paralogs in the rectal enterocytes of the marine teleost gilthead seabream (Sparus aurata) and investigated the neuropeptinergic effects of arginine vasopressin (Avp) and oxytocin (Oxt) on channel trafficking. The data reveal that Aqp1aa, -1ab2 and -3a are mainly localized in the cytoplasm and basolateral membranes of the enterocytes, while Aqp1ab1, -10bb and -14 are cytoplasmatic and also present in the apical plasma membrane microvilli. In contrast, Aqp0a localizes in the enterocyte subapical cytoplasm. Treatment of rectal explants with Avp in vitro increases the targeting of Aqp1ab1, -1ab2, -10bb and -14, but not of Aqp0a, -1aa and -3a, to the enterocyte apical microvilli, which involves protein kinase A (PKA)-mediated phosphorylation of the channel subdomains. In addition, we find that the differential interaction of the Aqp1ab-type paralogs with teleost-specific 14-3-3ζ-like binding proteins is associated with the trafficking of the channels to the apical microvilli membranes. Conversely, Oxt treatment does not affect the subcellular distribution of any of the investigated aquaporins, except Aqp14, which is internalized in response to the neuropeptide by a partially independent protein kinase C pathway. These data suggest that Avp-PKA signaling controls plasma membrane trafficking of several seabream rectal aquaporins, possibly to facilitate water and solute fluxes across the enterocyte membrane.
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BibTeX
@article{chauvigne2026neuropeptide,
title = {{Neuropeptide Regulation of Aquaporin Intracellular Trafficking in Marine Teleost Rectal Enterocytes}},
author = {François Chauvigné and Daniel Toala-Franco and Àngel Rey-Alfonso and Marc Catalán-García and Roderick Nigel Finn and Joan Cerdà},
journal = {International Journal of Molecular Sciences},
year = {2026},
month = oct,
doi = {10.3390/ijms27219427},
url = {https://www.mdpi.com/1422-0067/27/21/9427},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Neuropeptide Regulation of Aquaporin Intracellular Trafficking in Marine Teleost Rectal Enterocytes
AU - François Chauvigné
AU - Daniel Toala-Franco
AU - Àngel Rey-Alfonso
AU - Marc Catalán-García
AU - Roderick Nigel Finn
AU - Joan Cerdà
PY - 2026
DA - 2026/10/22
JO - International Journal of Molecular Sciences
DO - 10.3390/ijms27219427
UR - https://www.mdpi.com/1422-0067/27/21/9427
AB - In marine teleosts, the neuroendocrine regulation of aquaporin intracellular trafficking in osmoregulatory organs such as the intestinal rectum remains underexplored. By using paralog-specific antibodies, here we determined the subcellular localization of seven aquaporin and aquaglyceroporin paralogs in the rectal enterocytes of the marine teleost gilthead seabream (Sparus aurata) and investigated the neuropeptinergic effects of arginine vasopressin (Avp) and oxytocin (Oxt) on channel trafficking. The data reveal that Aqp1aa, -1ab2 and -3a are mainly localized in the cytoplasm and basolateral membranes of the enterocytes, while Aqp1ab1, -10bb and -14 are cytoplasmatic and also present in the apical plasma membrane microvilli. In contrast, Aqp0a localizes in the enterocyte subapical cytoplasm. Treatment of rectal explants with Avp in vitro increases the targeting of Aqp1ab1, -1ab2, -10bb and -14, but not of Aqp0a, -1aa and -3a, to the enterocyte apical microvilli, which involves protein kinase A (PKA)-mediated phosphorylation of the channel subdomains. In addition, we find that the differential interaction of the Aqp1ab-type paralogs with teleost-specific 14-3-3ζ-like binding proteins is associated with the trafficking of the channels to the apical microvilli membranes. Conversely, Oxt treatment does not affect the subcellular distribution of any of the investigated aquaporins, except Aqp14, which is internalized in response to the neuropeptide by a partially independent protein kinase C pathway. These data suggest that Avp-PKA signaling controls plasma membrane trafficking of several seabream rectal aquaporins, possibly to facilitate water and solute fluxes across the enterocyte membrane.
SN - 1422-0067
ER -