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Filopodome Mapping Identifies p130Cas as a Mechanosensitive Regulator of Filopodia Stability




TekijätGuillaume Jacquemet, Aki Stubb, Rafael Saup, Mitro Miihkinen, Elena Kremneva, Hellyeh Hamidi, Johanna Ivaska

Julkaisuvuosi2019

JournalCurrent Biology

Tietokannassa oleva lehden nimiCurrent biology : CB

Lehden akronyymiCurr Biol

Vuosikerta29

Numero2

Aloitussivu202

Lopetussivu216

Sivujen määrä22

ISSN0960-9822

eISSN1879-0445

DOIhttps://doi.org/10.1016/j.cub.2018.11.053

Rinnakkaistallenteen osoitehttps://research.utu.fi/converis/portal/detail/Publication/37838958


Tiivistelmä
in filopodia tips, predicts critical roles for PIs in regulating filopodia ultra-structure and function. Our mapping further reveals that filopodia adhesions consist of a unique set of proteins, the filopodome, that are distinct from classical nascent adhesions, focal adhesions, and fibrillar adhesions. Using live imaging, we observe that filopodia adhesions can give rise to nascent adhesions, which, in turn, form focal adhesions. We demonstrate that p130Cas (BCAR1) is recruited to filopodia tips via its C-terminal Cas family homology domain (CCHD) and acts as a mechanosensitive regulator of filopodia stability. Finally, we demonstrate that our map based on myosin-X-induced filopodia can be translated to endogenous filopodia and fascin- and IRSp53-mediated filopodia.

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