Filopodome Mapping Identifies p130Cas as a Mechanosensitive Regulator of Filopodia Stability.

A1 Originalartikel i en vetenskaplig tidskrift (referentgranskad)

Interna författare/redaktörer

Publikationens författare: Jacquemet, Stubb, Saup, Miihkinen, Kremneva, Hamidi, Ivaska
Publiceringsår: 2019
Tidskrift: Current Biology
Tidskriftsakronym: Curr Biol
Volym: 29
Nummer: 2
Artikelns första sida, sidnummer: 202
Artikelns sista sida, sidnummer: 216.e7
ISSN: 1879-0445


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.

Senast uppdaterad 2020-01-10 vid 04:58