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

A1 Journal article (refereed)


Internal Authors/Editors


Publication Details

List of Authors: Jacquemet, Stubb, Saup, Miihkinen, Kremneva, Hamidi, Ivaska
Publication year: 2019
Journal: Current Biology
Journal acronym: Curr Biol
Volume number: 29
Issue number: 2
Start page: 202
End page: 216.e7
ISSN: 1879-0445


Abstract

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.

Last updated on 2019-10-12 at 03:20