Myosin-X recruits lamellipodin to filopodia tips



Miihkinen, Mitro, Popović, Ana, Ghimire, Sujan, Saup, Rafael, Grönloh, Max LB, Ball, Neil, Goult, Benjamin ORCID: 0000-0002-3438-2807, Ivaska, Johanna ORCID: 0000-0002-6295-6556 and Jacquemet, Guillaume ORCID: 0000-0002-9286-920X
(2022) Myosin-X recruits lamellipodin to filopodia tips. [Preprint]

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Abstract

Myosin-X (MYO10), a molecular motor localizing to filopodia, is thought to transport various cargo to filopodia tips, modulating filopodia function. Yet, 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 RAPH1 interaction with adhesome components to its talinbinding and Ras-association domains. Surprisingly, we find that the RAPH1 MYO10-binding site is not within these domains. Instead, it comprises an area with previously unknown functions. Functionally, RAPH1 supports MYO10 filopodia formation and stability but is not involved in regulating integrin activity in 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.

Item Type: Preprint
Uncontrolled Keywords: 3101 Biochemistry and Cell Biology, 31 Biological Sciences, 1.1 Normal biological development and functioning, Generic health relevance
Divisions: Faculty of Health and Life Sciences
Faculty of Health and Life Sciences > Institute of Systems, Molecular and Integrative Biology
Depositing User: Symplectic Admin
Date Deposited: 13 Mar 2024 10:01
Last Modified: 19 Jul 2024 16:56
DOI: 10.1101/2022.08.17.504298
Open Access URL: https://doi.org/10.1101/2022.08.17.504298
Related URLs:
URI: https://livrepository.liverpool.ac.uk/id/eprint/3179302