A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Myosin-X recruits lamellipodin to filopodia tips
Tekijät: Popovíc Ana, Miihkinen Mitro, Ghimire Sujan, Saup Rafael, Grönloh Max L.B., Ball Neil J., Goult Benjamin T., Ivaska Johanna, Jacquemet Guillaume
Kustantaja: COMPANY BIOLOGISTS LTD
Julkaisuvuosi: 2023
Journal: Journal of Cell Science
Tietokannassa oleva lehden nimi: JOURNAL OF CELL SCIENCE
Lehden akronyymi: J CELL SCI
Artikkelin numero: jcs260574
Vuosikerta: 136
Numero: 5
Sivujen määrä: 12
ISSN: 0021-9533
eISSN: 1477-9137
DOI: https://doi.org/10.1242/jcs.260574
Verkko-osoite: https://doi.org/10.1242/jcs.260574
Rinnakkaistallenteen osoite: 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.
Ladattava julkaisu This is an electronic reprint of the original article. |  |
