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Peer-reviewedCC BYThe Journal of cell biology

Evolutionarily diverged on-switch for actin assembly in fungal endocytosis.

  • Juliette Sebellin1
  • Fabina Binth Kandiyoth2
  • V T Bagyashree1
  • Andrea Picco1,3
  • Nicolas Carvalho1
  • Markku Hakala1
  • Anne-Sophie Rivier-Cordey1
  • Alphée Michelot2,4
  • Christopher P Toret1
  • Marko Kaksonen1
4 affiliations
  1. 1Department of Biochemistry, University of Geneva, Geneva, Switzerland.
  2. 2Aix Marseille University, CNRS, IBDM, Turing Centre for Living Systems , Marseille, France.
  3. 3MIDA.science , Geneva, Switzerland.
  4. 4CNRS International Research Laboratory Bridging Mechanobiology and Medicine (IRL 3639 BMC), Mechanobiology Institute, National University of Singapore (NUS), Singapore.
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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.

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Cite

BibTeXRIS
BibTeX
@article{sebellin2026evolutionarily,
  title = {{Evolutionarily diverged on-switch for actin assembly in fungal endocytosis.}},
  author = {Juliette Sebellin and Fabina Binth Kandiyoth and V T Bagyashree and Andrea Picco and Nicolas Carvalho and Markku Hakala and Anne-Sophie Rivier-Cordey and Alphée Michelot and Christopher P Toret and Marko Kaksonen},
  journal = {The Journal of cell biology},
  year = {2026},
  month = oct,
  doi = {10.1083/jcb.202506135},
  url = {https://europepmc.org/article/MED/42949641},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - Evolutionarily diverged on-switch for actin assembly in fungal endocytosis.
AU  - Juliette Sebellin
AU  - Fabina Binth Kandiyoth
AU  - V T Bagyashree
AU  - Andrea Picco
AU  - Nicolas Carvalho
AU  - Markku Hakala
AU  - Anne-Sophie Rivier-Cordey
AU  - Alphée Michelot
AU  - Christopher P Toret
AU  - Marko Kaksonen
PY  - 2026
DA  - 2026/10/28
JO  - The Journal of cell biology
DO  - 10.1083/jcb.202506135
UR  - https://europepmc.org/article/MED/42949641
AB  - 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.
SN  - 0021-9525
SN  - 1540-8140
ER  -