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Myosin-X and talin modulate integrin activity at filopodia tips

Miihkinen, Mitro, Grönloh, Max L.B., Popović, Ana, Vihinen, Helena, Jokitalo, Eija, Goult, Benjamin T., Ivaska, Johanna, Jacquemet, Guillaume (2021) Myosin-X and talin modulate integrin activity at filopodia tips. Cell Reports, 36 (11). Article Number 109716. ISSN 2211-1247. (doi:10.1016/j.celrep.2021.109716) (KAR id:81141)

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Filopodia assemble unique integrin-adhesion complexes to sense the extracellular matrix. However, the mechanisms of integrin localization and regulation in filopodia are poorly defined. Here, we observed that active integrins accumulate at the tip of myosin-X(MYO10)-positive filopodia while inactive integrins are uniformly distributed. RNAi depletion of 10 integrin activity modulators identified talin as the principal integrin activator in filopodia. Deletion of the MYO10-FERM domain, or mutation of the β1-integrin-binding residues within, revealed MYO10 as facilitating integrin activation but not transport in filopodia. However, MYO10-FERM alone could not activate integrins, potentially due to dual binding to both α- and β-integrin tails. As swapping MYO10-FERM with talin-FERM enabled integrin activation in filopodia, our data indicate that an integrin-binding FERM domain coupled to a myosin motor is a core requirement for integrin activation in filopodia. Therefore, we propose a two-step integrin activation model in filopodia: receptor tethering by MYO10 followed by talin-mediated integrin activation.

Item Type: Article
DOI/Identification number: 10.1016/j.celrep.2021.109716
Uncontrolled keywords: Filopodia, integrin activity, adhesion, MYO10, talin
Subjects: Q Science > QH Natural history > QH581.2 Cell Biology
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Ben Goult
Date Deposited: 06 May 2020 20:03 UTC
Last Modified: 19 Nov 2021 10:08 UTC
Resource URI: (The current URI for this page, for reference purposes)
Goult, Benjamin T.:
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