PUBLICATION

Pacsin2 is required for endocytosis in the zebrafish pronephric tubule

Authors
Morgan, J., Yarwood, R., Starborg, T., Yan, G., Lowe, M.
ID
ZDB-PUB-220527-7
Date
2022
Source
Biology Open   11(6): (Journal)
Registered Authors
Lowe, Martin
Keywords
Endocytosis, Megalin, Proximal tubule, Zebrafish, pacsin2
MeSH Terms
  • Animals
  • Biological Transport
  • Endocytosis/physiology
  • Kidney Tubules, Proximal/metabolism
  • Low Density Lipoprotein Receptor-Related Protein-2*/genetics
  • Low Density Lipoprotein Receptor-Related Protein-2*/metabolism
  • Mammals/metabolism
  • Zebrafish*/metabolism
PubMed
35616009 Full text @ Biol. Open
Abstract
Endocytosis mediates the cellular uptake of numerous molecules from the extracellular space and is a fundamentally important process. In the renal proximal tubule, the scavenger receptor megalin and its co-receptor cubilin mediate endocytosis of low molecular weight proteins from the renal filtrate. However, the extent to which megalin endocytosis relies on different components of the trafficking machinery remains relatively poorly defined in vivo. In this study, we identify a functional requirement for the F-BAR protein pacsin2 in endocytosis in the renal proximal tubule of zebrafish larvae. Pacsin2 is expressed throughout development and in all zebrafish tissues, similar to the mammalian orthologue. Within renal tubular epithelial cells, pacsin2 is enriched at the apical pole where it is localised to endocytic structures. Loss of pacsin2 results in reduced endocytosis within the proximal tubule, which is accompanied by a reduction in the abundance of megalin and endocytic organelles. Our results indicate that pacsin2 is required for efficient endocytosis in the proximal tubule, where it likely cooperates with other trafficking machinery to maintain endocytic uptake and recycling of megalin.
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