FAK structure from single particle analysis of 2D crystals
Ontology highlight
ABSTRACT:
SUBMITTER: Ricardo Righetto
PROVIDER: EMPIAR-10347 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structural basis of Focal Adhesion Kinase activation on lipid membranes.
Acebrón Iván I Righetto Ricardo D RD Schoenherr Christina C de Buhr Svenja S Redondo Pilar P Culley Jayne J Rodríguez Carlos F CF Daday Csaba C Biyani Nikhil N Llorca Oscar O Byron Adam A Chami Mohamed M Gräter Frauke F Boskovic Jasminka J Frame Margaret C MC Stahlberg Henning H Lietha Daniel D
The EMBO journal 20200811 19
Focal adhesion kinase (FAK) is a key component of the membrane proximal signaling layer in focal adhesion complexes, regulating important cellular processes, including cell migration, proliferation, and survival. In the cytosol, FAK adopts an autoinhibited state but is activated upon recruitment into focal adhesions, yet how this occurs or what induces structural changes is unknown. Here, we employ cryo-electron microscopy to reveal how FAK associates with lipid membranes and how membrane intera ...[more]
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