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. 2021 May 11;11:83. doi: 10.1186/s13578-021-00595-4

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© The Author(s) 2021

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 4 — Clathrin accessory proteins for assembly (Lap) and disassembly (Aux; Hsc70-4) are required for endocytosis of slit diaphragm protein Pyd. Immunofluorescence labeling for Pyd (red), with DAPI (blue) nuclear stain of adult fly nephrocytes, visualized by confocal microscopy. Scale bar: 1 μm. a–a″ In wild type (Control) nephrocytes, Pyd was localized to the cell membrane (a) and exhibited a uniform and smoothly distributed fingerprint-like pattern on the cell surface (a′–a″). b–b″ Silencing of lap resulted in intracellular aggregation of Pyd proteins with partial disruption of Pyd cell surface localization. Note the fingerprint-like pattern remained largely intact, however gaps between adjacent Pyd-positive ridges appeared increased. c–d Silencing of aux (c–c″) and Hsc70-4 (d–d″) resulted in severe disruption of Pyd cell surface localization. Revealing intracellular localization of aggregate-like structures, and cell-surface distribution marked by high-density aggregation areas