TY - JOUR
T1 - Filopodome Mapping Identifies p130Cas as a Mechanosensitive Regulator of Filopodia Stability.
AU - Jacquemet, Guillaume
AU - Stubb, null
AU - Saup, null
AU - Miihkinen, null
AU - Kremneva, null
AU - Hamidi, null
AU - Ivaska, null
PY - 2019
Y1 - 2019
N2 - 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.
AB - 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.
U2 - 10.1016/j.cub.2018.11.053
DO - 10.1016/j.cub.2018.11.053
M3 - Artikel
SN - 0960-9822
VL - 29
SP - 202–216.e7
JO - Current Biology
JF - Current Biology
IS - 2
ER -