A1 Refereed original research article in a scientific journal
Myosin-X recruits lamellipodin to filopodia tips
Authors: Popovíc Ana, Miihkinen Mitro, Ghimire Sujan, Saup Rafael, Grönloh Max L.B., Ball Neil J., Goult Benjamin T., Ivaska Johanna, Jacquemet Guillaume
Publisher: COMPANY BIOLOGISTS LTD
Publication year: 2023
Journal: Journal of Cell Science
Journal name in source: JOURNAL OF CELL SCIENCE
Journal acronym: J CELL SCI
Article number: jcs260574
Volume: 136
Issue: 5
Number of pages: 12
ISSN: 0021-9533
eISSN: 1477-9137
DOI: https://doi.org/10.1242/jcs.260574
Web address : https://doi.org/10.1242/jcs.260574
Self-archived copy’s web address: https://research.utu.fi/converis/portal/detail/Publication/179320189
Myosin-X (MYO10), a molecular motor localizing to filopodia, is thought to transport various cargo to filopodia tips, modulating filopodia function. However, only a few MYO10 cargoes have been described. Here, using GFP-Trap and BioID approaches combined with mass spectrometry, we identified lamellipodin (RAPH1) as a novel MYO10 cargo. We report that the FERM domain of MYO10 is required for RAPH1 localization and accumulation at filopodia tips. Previous studies have mapped the RAPH1 interaction domain for adhesome components to its talin-binding and Ras-association domains. Surprisingly, we find that the RAPH1 MYO10-binding site is not within these domains. Instead, it comprises a conserved helix located just after the RAPH1 pleckstrin homology domain with previously unknown functions. Functionally, RAPH1 supports MYO10 filopodia formation and stability but is not required to activate integrins at filopodia tips. Taken together, our data indicate a feed-forward mechanism whereby MYO10 filopodia are positively regulated by MYO10-mediated transport of RAPH1 to the filopodium tip.
Downloadable publication This is an electronic reprint of the original article. |  |
