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A FAK conundrum is solved: activation and organization of focal adhesion kinase at the plasma membrane
Author(s) -
Brod Florian,
Fässler Reinhard
Publication year - 2020
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.15252/embj.2020106234
Subject(s) - focal adhesion , biology , microbiology and biotechnology , membrane , kinase , adhesion , biophysics , signal transduction , biochemistry , materials science , composite material
Focal adhesion kinase ( FAK ) is a central mediator of cell adhesion, acting both as a scaffold and as catalytically active kinase. Acebrón et al (2020) use cryo‐electron microscopy (cryo‐ EM ) to visualize the dramatic structural changes that occur upon FAK recruitment to the plasma membrane, which releases FAK autoinhibition and induces its oligomerization. Since activity control via autoinhibition and protein clustering are features also utilized by other focal adhesion ( FA ) proteins, they have moved center stage in the endeavor to understand the complex process of cell adhesion regulation.