Light-dependent inhibition of clathrin-mediated endocytosis in yeast unveils conserved functions of the AP2 complex
File(s)
Published version
Author(s)
Type
Journal Article
Abstract
Clathrin-mediated endocytosis (CME) is an essential cellular process, conserved among eukaryotes. Yeast constitutes a powerful genetic model to dissect the complex endocytic machinery, yet there is a lack of specific pharmacological agents to interfere with CME in these organisms. TL2 is a light-regulated peptide inhibitor targeting the AP2-β-adaptin/β-arrestin interaction and that can photocontrol CME with high spatiotemporal precision in mammalian cells. Here, we study endocytic protein dynamics by live-cell imaging of the fluorescently tagged coat-associated protein Sla1-GFP, demonstrating that TL2 retains its inhibitory activity in S. cerevisiae spheroplasts. This is despite the β-adaptin/β-arrestin interaction not being conserved in yeast. Our data indicate that the AP2 α-adaptin is the functional target of activated TL2. We identified as interacting partners for the α-appendage, the Eps15 and epsin homologues Ede1 and Ent1. This demonstrates that endocytic cargo loading and sensing can be executed by conserved molecular interfaces, regardless of the proteins involved.
Date Issued
2023-10-20
Date Acceptance
2023-09-08
Citation
iScience, 2023, 26 (10)
ISSN
2589-0042
Publisher
Elsevier
Journal / Book Title
iScience
Volume
26
Issue
10
Copyright Statement
© 2023 The Author(s).
This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
Identifier
https://www.sciencedirect.com/science/article/pii/S2589004223019764?via%3Dihub
Subjects
ACTIN POLYMERIZATION
ADAPTERS
ALPHA-APPENDAGE
AZOBENZENE
CROSS-LINKER
MECHANISM
Multidisciplinary Sciences
PEPTIDES
PROTEINS
RECEPTOR
Science & Technology
Science & Technology - Other Topics
TRAFFICKING
Publication Status
Published
Article Number
ARTN 107899
Date Publish Online
2023-09-12