Actomyosin organelle functions of SPIRE actin nucleators precede animal evolution

Kollmar, Martin and Welz, Tobias and Ravi, Aishwarya and Kaufmann, Thomas and Alzahofi, Noura and Hatje, Klas and Alghamdi, Asmahan and Kim, Jiyu and Briggs, Deborah A. and Samol-Wolf, Annette and Pylypenko, Olena and Hume, Alistair N. and Burkhardt, Pawel and Faix, Jan and Kerkhoff, Eugen (2024) Actomyosin organelle functions of SPIRE actin nucleators precede animal evolution. COMMUNICATIONS BIOLOGY, 7 (1): 832. ISSN , 2399-3642

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Abstract

An important question in cell biology is how cytoskeletal proteins evolved and drove the development of novel structures and functions. Here we address the origin of SPIRE actin nucleators. Mammalian SPIREs work with RAB GTPases, formin (FMN)-subgroup actin assembly proteins and class-5 myosin (MYO5) motors to transport organelles along actin filaments towards the cell membrane. However, the origin and extent of functional conservation of SPIRE among species is unknown. Our sequence searches show that SPIRE exist throughout holozoans (animals and their closest single-celled relatives), but not other eukaryotes. SPIRE from unicellular holozoans (choanoflagellate), interacts with RAB, FMN and MYO5 proteins, nucleates actin filaments and complements mammalian SPIRE function in organelle transport. Meanwhile SPIRE and MYO5 proteins colocalise to organelles in Salpingoeca rosetta choanoflagellates. Based on these observations we propose that SPIRE originated in unicellular ancestors of animals providing an actin-myosin driven exocytic transport mechanism that may have contributed to the evolution of complex multicellular animals. Genome analysis and molecular cell biology studies indicate that SPIRE actin nucleators originated in unicellular ancestors of animals, providing an actin-myosin driven exocytic transport mechanism that may have contributed to animal evolution.

Item Type: Article
Uncontrolled Keywords: MULTIPLE SEQUENCE ALIGNMENT; WEB SERVER; MELANOSOME TRANSPORT; STRUCTURAL BASIS; RAB GTPASES; WH2 DOMAIN; PROTEIN; FORMIN; ORIGIN; COMPLEX;
Subjects: 600 Technology > 610 Medical sciences Medicine
Divisions: Medicine > Lehrstuhl für Neurologie
Depositing User: Dr. Gernot Deinzer
Date Deposited: 04 Nov 2025 09:22
Last Modified: 04 Nov 2025 09:22
URI: https://pred.uni-regensburg.de/id/eprint/64902

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