Evolutionarily diverged on-switch for actin assembly in fungal endocytosis

Clathrin-mediated endocytosis is a conserved eukaryotic trafficking process where an Arp2/3 complex-nucleated branched actin network provides force for vesicle formation. The mechanisms that initiate endocytic actin assembly are incompletely understood. In the fission yeast, Schizosaccharomyces pombe, actin assembly is initiated by Dip1, an Arp2/3 complex activator. In the budding yeast, Saccharomyces cerevisiae, the initiation of actin assembly has remained a mystery. Here, we show that S. cerevisiae Ldb17, the homolog of Dip1, functions as an on-switch for endocytic actin assembly. Unexpectedly, the regulation of Ldb17 is more complicated than that of constitutively active Dip1. Ldb17 is controlled by a coat protein, Sla1, via separate recruitment and activation steps. This regulation was likely lost in the S. pombe lineage, and this simplification may be related to other changes in actin assembly between these species. Our findings add a key missing piece in the understanding of endocytosis in S. cerevisiae and reveal an intriguing evolutionary tinkering of the actin on-switch.

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Publication Details

Journal
The Journal of Cell Biology
Published
2026-10-28
DOI
https://doi.org/10.1083/jcb.202506135
Primary Topic
Cellular transport and secretion
Type
article
Field-Weighted Citation Impact
0.00

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article

Evolutionarily diverged on-switch for actin assembly in fungal endocytosis

Nicolas Carvalho, Andrea Picco, Alphée Michelot, Markku Hakala et al.
1 links
The Journal of Cell Biology
Cellular transport and secretion
article

Evolutionarily diverged on-switch for actin assembly in fungal endocytosis

Nicolas Carvalho, Andrea Picco, Alphée Michelot, Markku Hakala, Anne-Sophie Rivier-Cordey, Marko Kaksonen, Christopher P. Toret, Bagyashree VT, Juliette Sebellin, Fabina Binth Kandiyoth
article en

Abstract

Clathrin-mediated endocytosis is a conserved eukaryotic trafficking process where an Arp2/3 complex-nucleated branched actin network provides force for vesicle formation. The mechanisms that initiate endocytic actin assembly are incompletely understood. In the fission yeast, Schizosaccharomyces pombe, actin assembly is initiated by Dip1, an Arp2/3 complex activator. In the budding yeast, Saccharomyces cerevisiae, the initiation of actin assembly has remained a mystery. Here, we show that S. cerevisiae Ldb17, the homolog of Dip1, functions as an on-switch for endocytic actin assembly. Unexpectedly, the regulation of Ldb17 is more complicated than that of constitutively active Dip1. Ldb17 is controlled by a coat protein, Sla1, via separate recruitment and activation steps. This regulation was likely lost in the S. pombe lineage, and this simplification may be related to other changes in actin assembly between these species. Our findings add a key missing piece in the understanding of endocytosis in S. cerevisiae and reveal an intriguing evolutionary tinkering of the actin on-switch.

The Journal of Cell BiologyVol. 226(1)
University of Geneva (CH), Centre National de la Recherche Scientifique (FR), National University of Singapore (SG), Aix-Marseille Université (FR), Institut de Biologie du Développement Marseille (FR), Mechanobiology Institute (SG), Bridging Mechanobiology and Medicine (SG)
National Research Foundation, National University of Singapore, National Research Foundation Singapore, Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung, Université de Genève, Mechanobiology Institute, Singapore
Openalex Percentile: Top 17%
Cellular transport and secretion
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