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

Guillaume Jacquemet; null Stubb; null Saup; null Miihkinen; null Kremneva; null Hamidi; null Ivaska

doi:10.1016/j.cub.2018.11.053

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

Guillaume Jacquemet, Stubb, Saup, Miihkinen, Kremneva, Hamidi, Ivaska

Research output: Contribution to journal › Article › Scientific › peer-review

75 Citations (Scopus)

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.

Original language	Undefined/Unknown
Pages (from-to)	202–216.e7
Journal	Current Biology
Volume	29
Issue number	2
DOIs	https://doi.org/10.1016/j.cub.2018.11.053
Publication status	Published - 2019
MoE publication type	A1 Journal article-refereed

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10.1016/j.cub.2018.11.053

Cite this

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title = "Filopodome Mapping Identifies p130Cas as a Mechanosensitive Regulator of Filopodia Stability.",

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.",

author = "Guillaume Jacquemet and Stubb and Saup and Miihkinen and Kremneva and Hamidi and Ivaska",

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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

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