scholarly journals Food for thought: How cell adhesion coordinates nutrient sensing

2021 ◽  
Vol 220 (5) ◽  
Author(s):  
Hellyeh Hamidi ◽  
Johanna Ivaska

Cell adhesion controls cell survival and proliferation via multiple mechanisms. Rabanal-Ruiz et al. (2021. J. Cell Biol.https://doi.org/10.1083/jcb.202004010) demonstrate that focal adhesions are key signaling hubs for cellular nutrient sensing and signaling.

Genetics ◽  
2000 ◽  
Vol 155 (4) ◽  
pp. 1725-1740
Author(s):  
Rachel T Cox ◽  
Donald G McEwen ◽  
Denise L Myster ◽  
Robert J Duronio ◽  
Joseph Loureiro ◽  
...  

Abstract During development signaling pathways coordinate cell fates and regulate the choice between cell survival or programmed cell death. The well-conserved Wingless/Wnt pathway is required for many developmental decisions in all animals. One transducer of the Wingless/Wnt signal is Armadillo/β-catenin. Drosophila Armadillo not only transduces Wingless signal, but also acts in cell-cell adhesion via its role in the epithelial adherens junction. While many components of both the Wingless/Wnt signaling pathway and adherens junctions are known, both processes are complex, suggesting that unknown components influence signaling and junctions. We carried out a genetic modifier screen to identify some of these components by screening for mutations that can suppress the armadillo mutant phenotype. We identified 12 regions of the genome that have this property. From these regions and from additional candidate genes tested we identified four genes that suppress arm: dTCF, puckered, head involution defective (hid), and Dpresenilin. We further investigated the interaction with hid, a known regulator of programmed cell death. Our data suggest that Wg signaling modulates Hid activity and that Hid regulates programmed cell death in a dose-sensitive fashion.


Cytokine ◽  
1994 ◽  
Vol 6 (5) ◽  
pp. 561
Author(s):  
Anne-Marie O'Farrell ◽  
Masatoshi Ichihara ◽  
Atsushi Miyajima

2011 ◽  
Vol 109 (5) ◽  
pp. 1305-1313 ◽  
Author(s):  
Andriy Shkilnyy ◽  
Justin Dubois ◽  
Georges Sabra ◽  
Jamie Sharp ◽  
Serge Gagnon ◽  
...  

2013 ◽  
Vol 10 (8) ◽  
pp. 706-713 ◽  
Author(s):  
Sander Bekeschus ◽  
Kai Masur ◽  
Julia Kolata ◽  
Kristian Wende ◽  
Anke Schmidt ◽  
...  

2011 ◽  
pp. P2-488-P2-488
Author(s):  
Nagesha Guthalu Kondegowda ◽  
Anthony Otero ◽  
Anais Mozar ◽  
Connie Chin ◽  
Rupangi C Vasavada

2021 ◽  
Author(s):  
Koichi Fukuda ◽  
Fan Lu ◽  
Jun Qin

AbstractRas suppressor-1 (Rsu-1) is a leucine-rich repeat (LRR)-containing protein that is crucial for regulating fundamental cell adhesion processes and tumor development. Rsu-1 interacts with a zinc-finger type multi LIM domain-containing adaptor protein PINCH-1 involved in the integrin-mediated consensus adhesome but not with highly homologous isoform PINCH-2. However, the structural basis for such specific interaction and regulatory mechanism remains unclear. Here, we determined the crystal structures of Rsu-1 and its complex with the PINCH-1 LIM4-5 domains. Rsu-1 displays an arc-shaped solenoid architecture with eight LRRs shielded by the N- and C-terminal capping modules. We show that a large conserved concave surface of the Rsu-1 LRR domain recognizes the PINCH-1 LIM5 domain, and that the C-terminal non-LIM region of PINCH-2 but not PINCH-1 sterically disfavors the Rsu-1 binding. We further show that Rsu-1 can be assembled, via PINCH-1-binding, into a tight hetero-pentamer complex comprising Rsu-1, PINCH-1, ILK, Parvin, and Kindlin-2 that constitute a major consensus integrin adhesome crucial for focal adhesion assembly. Consistently, our mutagenesis and cell biological data consolidate the significance of the Rsu-1/PINCH-1 interaction in focal adhesion assembly and cell spreading. Our results provide a crucial molecular insight into Rsu-1-mediated cell adhesion with implication on how it may regulate tumorigenic growth.


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