Deletion of the cell adhesion adaptor protein vinculin disturbs the localization of GFAP in Bergmann glial cells

Glia ◽  
2013 ◽  
Vol 61 (7) ◽  
pp. 1067-1083 ◽  
Author(s):  
Ulrike Winkler ◽  
Petra G. Hirrlinger ◽  
Marcello Sestu ◽  
Franziska Wilhelm ◽  
Stefanie Besser ◽  
...  
2002 ◽  
Vol 68 (2) ◽  
pp. 138-149 ◽  
Author(s):  
Jens Grosche ◽  
Helmut Kettenmann ◽  
Andreas Reichenbach

2007 ◽  
Vol 311 (1) ◽  
pp. 238-250 ◽  
Author(s):  
Okiru Komine ◽  
Mai Nagaoka ◽  
Kei Watase ◽  
David H. Gutmann ◽  
Kenji Tanigaki ◽  
...  

2017 ◽  
Vol 10 (491) ◽  
pp. eaal2880 ◽  
Author(s):  
Inbar Azoulay-Alfaguter ◽  
Marianne Strazza ◽  
Michael Peled ◽  
Hila K. Novak ◽  
James Muller ◽  
...  

1994 ◽  
Vol 14 (5) ◽  
pp. 2503-2514 ◽  
Author(s):  
T Muller ◽  
JM Fritschy ◽  
J Grosche ◽  
GD Pratt ◽  
H Mohler ◽  
...  

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.


2017 ◽  
Vol 216 (11) ◽  
pp. 3785-3798 ◽  
Author(s):  
Ralph T. Böttcher ◽  
Maik Veelders ◽  
Pascaline Rombaut ◽  
Jan Faix ◽  
Marina Theodosiou ◽  
...  

Cell spreading requires the coupling of actin-driven membrane protrusion and integrin-mediated adhesion to the extracellular matrix. The integrin-activating adaptor protein kindlin-2 plays a central role for cell adhesion and membrane protrusion by directly binding and recruiting paxillin to nascent adhesions. Here, we report that kindlin-2 has a dual role during initial cell spreading: it binds paxillin via the pleckstrin homology and F0 domains to activate Rac1, and it directly associates with the Arp2/3 complex to induce Rac1-mediated membrane protrusions. Consistently, abrogation of kindlin-2 binding to Arp2/3 impairs lamellipodia formation and cell spreading. Our findings identify kindlin-2 as a key protein that couples cell adhesion by activating integrins and the induction of membrane protrusions by activating Rac1 and supplying Rac1 with the Arp2/3 complex.


2009 ◽  
pp. 161-171 ◽  
Author(s):  
A. Verkhratsky ◽  
A. Reichenbach

2019 ◽  
Vol 45 (6) ◽  
pp. 1365-1374 ◽  
Author(s):  
Miguel Escalante ◽  
Jazmín Soto-Verdugo ◽  
Luisa C. Hernández-Kelly ◽  
Dinorah Hernández-Melchor ◽  
Esther López-Bayghen ◽  
...  

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