Dynamin1 long- and short-tail isoforms exploit distinct recruitment and spatial patterns to form endocytic nanoclusters

Anmin Jiang, Kye Kudo, Rachel S. Gormal, Sevannah Ellis, Sikao Guo, Tristan P. Wallis, Shanley F. Longfield, Phillip J. Robinson, Margaret E. Johnson, Merja Joensuu () and Frédéric A. Meunier ()
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Anmin Jiang: The University of Queensland
Kye Kudo: The University of Queensland
Rachel S. Gormal: The University of Queensland
Sevannah Ellis: The University of Queensland
Sikao Guo: Johns Hopkins University
Tristan P. Wallis: The University of Queensland
Shanley F. Longfield: The University of Queensland
Phillip J. Robinson: The University of Sydney
Margaret E. Johnson: Johns Hopkins University
Merja Joensuu: The University of Queensland
Frédéric A. Meunier: The University of Queensland

Nature Communications, 2024, vol. 15, issue 1, 1-21

Abstract: Abstract Endocytosis requires a coordinated framework of molecular interactions that ultimately lead to the fission of nascent endocytic structures. How cytosolic proteins such as dynamin concentrate at discrete sites that are sparsely distributed across the plasma membrane remains poorly understood. Two dynamin-1 major splice variants differ by the length of their C-terminal proline-rich region (short-tail and long-tail). Using sptPALM in PC12 cells, neurons and MEF cells, we demonstrate that short-tail dynamin-1 isoforms ab and bb display an activity-dependent recruitment to the membrane, promptly followed by their concentration into nanoclusters. These nanoclusters are sensitive to both Calcineurin and dynamin GTPase inhibitors, and are larger, denser, and more numerous than that of long-tail isoform aa. Spatiotemporal modelling confirms that dynamin-1 isoforms perform distinct search patterns and undergo dimensional reduction to generate endocytic nanoclusters, with short-tail isoforms more robustly exploiting lateral trapping in the generation of nanoclusters compared to the long-tail isoform.

Date: 2024
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DOI: 10.1038/s41467-024-47677-8

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