Myosin-X recruits lamellipodin to filopodia tips

Ana Popović, Mitro Miihkinen, Sujan Ghimire, Rafael Saup, Max L B Grönloh, Neil J Ball, Benjamin T Goult, Johanna Ivaska, Guillaume Jacquemet*

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

2 Citations (Scopus)
36 Downloads (Pure)


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.

Original languageEnglish
Article numberjcs260574
JournalJournal of Cell Science
Issue number5
Publication statusPublished - 1 Mar 2023
MoE publication typeA1 Journal article-refereed


  • Pseudopodia
  • Binding Sites
  • Integrins
  • Mass Spectrometry
  • Myosins/genetics


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