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.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 J+Cell+Biol
2017 ; 216
(11
): 3785-3798
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Kindlin-2 recruits paxillin and Arp2/3 to promote membrane protrusions during
initial cell spreading
#MMPMID28912124
Böttcher RT
; Veelders M
; Rombaut P
; Faix J
; Theodosiou M
; Stradal TE
; Rottner K
; Zent R
; Herzog F
; Fässler R
J Cell Biol
2017[Nov]; 216
(11
): 3785-3798
PMID28912124
show ga
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.
|*Cell Adhesion
[MESH]
|*Cell Shape
[MESH]
|Actin-Related Protein 2-3 Complex/genetics/*metabolism
[MESH]