Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/232869
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | FAK structure and regulation by membrane interactions and force in focal adhesions |
Autor: | Tapial Martínez, Paula CSIC; López-Navajas, Pilar CSIC ; Lietha, Daniel CSIC ORCID | Palabras clave: | Cell adhesion Cell signalling Focal adhesion kinase Mechanobiology Membrane interactions Structural biology |
Fecha de publicación: | 24-ene-2020 | Editor: | Multidisciplinary Digital Publishing Institute | Citación: | Biomolecules 10 (2) 179 (2020) | Resumen: | Focal adhesion kinase (FAK) is a non-receptor tyrosine kinase with key roles in the regulation of cell adhesion migration, proliferation and survival. In cancer FAK is a major driver of invasion and metastasis and its upregulation is associated with poor patient prognosis. FAK is autoinhibited in the cytosol, but activated upon localisation into a protein complex, known as focal adhesion complex. This complex forms upon cell adhesion to the extracellular matrix (ECM) at the cytoplasmic side of the plasma membrane at sites of ECM attachment. FAK is anchored to the complex via multiple sites, including direct interactions with specific membrane lipids and connector proteins that attach focal adhesions to the actin cytoskeleton. In migrating cells, the contraction of actomyosin stress fibres attached to the focal adhesion complex apply a force to the complex, which is likely transmitted to the FAK protein, causing stretching of the FAK molecule. In this review we discuss the current knowledge of the FAK structure and how specific structural features are involved in the regulation of FAK signalling. We focus on two major regulatory mechanisms known to contribute to FAK activation, namely interactions with membrane lipids and stretching forces applied to FAK, and discuss how they might induce structural changes that facilitate FAK activation. | Descripción: | 16 p.-2 fig. | Versión del editor: | https://doi.org/10.3390/biom10020179 | URI: | http://hdl.handle.net/10261/232869 | DOI: | 10.3390/biom10020179 | E-ISSN: | 2218-273X |
Aparece en las colecciones: | (CIB) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
biomolecules_tapial-martínez_2020.pdf | Artículo principal | 1,86 MB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
PubMed Central
Citations
63
checked on 09-abr-2024
SCOPUSTM
Citations
108
checked on 23-abr-2024
WEB OF SCIENCETM
Citations
95
checked on 23-feb-2024
Page view(s)
91
checked on 23-abr-2024
Download(s)
80
checked on 23-abr-2024