scholarly journals SLK-mediated phosphorylation of paxillin is required for focal adhesion turnover and cell migration

Oncogene ◽  
2012 ◽  
Vol 32 (39) ◽  
pp. 4656-4663 ◽  
Author(s):  
J L Quizi ◽  
K Baron ◽  
K N Al-Zahrani ◽  
P O'Reilly ◽  
R K Sriram ◽  
...  
Keyword(s):  
Cell Migration ◽  
Focal Adhesion ◽  
Focal Adhesion Turnover

scholarly journals FAK/src-Family Dependent Activation of the Ste20-Like Kinase SLK Is Required for Microtubule-Dependent Focal Adhesion Turnover and Cell Migration

PLoS ONE ◽  
2008 ◽  
Vol 3 (4) ◽  
pp. e1868 ◽  
Author(s):  
Simona Wagner ◽  
Chris J. Storbeck ◽  
Kristin Roovers ◽  
Ziad Y. Chaar ◽  
Piotr Kolodziej ◽  
...  
Keyword(s):  
Cell Migration ◽  
Focal Adhesion ◽  
Focal Adhesion Turnover

scholarly journals Interaction of Paxillin with Poly(A)-Binding Protein 1 and Its Role in Focal Adhesion Turnover and Cell Migration

2005 ◽  
Vol 25 (9) ◽  
pp. 3763-3773 ◽  
Author(s):  
Alison J. Woods ◽  
Theodoros Kantidakis ◽  
Hisataka Sabe ◽  
David R. Critchley ◽  
Jim C. Norman
Keyword(s):  
Cell Migration ◽  
Rna Interference ◽  
Focal Adhesion ◽  
Nuclear Export ◽  
Binding Protein ◽  
Focal Adhesions ◽  
Nuclear Accumulation ◽  
Two Dimensional ◽  
Nucleocytoplasmic Shuttling ◽  
Focal Adhesion Turnover

ABSTRACT We have previously identified poly(A)-binding protein 1 (PABP1) as a ligand for paxillin and shown that the paxillin-PABP1 complex undergoes nucleocytoplasmic shuttling. By targeting the paxillin-binding subdomain sequences in PABP1, we have generated mutants of PABP1 that do not bind to cellular paxillin. Here we report that paxillin association is necessary for efficient nuclear export of PABP1 and that RNA interference of paxillin drives the nuclear accumulation of PABP1. Furthermore, ablation of paxillin-PABP1 association impeded a number of indices of cell motility including spreading on fibronectin, cell migration on two-dimensional matrices, and transmigration in Boyden chambers. These data indicate that PABP1 must associate with paxillin in order to be efficiently transported from the nucleus to the cytoplasm and that this event is necessary for cells to remodel their focal adhesions during cell migration.

scholarly journals Microtubule acetylation but not detyrosination promotes focal adhesion dynamics and cell migration

2018 ◽  
Author(s):  
Bertille Bance ◽  
Shailaja Seetharaman ◽  
Cécile Leduc ◽  
Batiste Boëda ◽  
Sandrine Etienne-Manneville
Keyword(s):  
Cell Migration ◽  
Focal Adhesion ◽  
Focal Adhesions ◽  
Cell Polarization ◽  
Post Translational Modifications ◽  
Tubulin Acetylation ◽  
Focal Adhesion Turnover ◽  
Regulatory Functions ◽  
Insight Into

AbstractMicrotubules play a crucial role in mesenchymal migration by controlling cell polarity and the turnover of cell adhesive structures on the extracellular matrix. The polarized functions of microtubules imply that microtubules are locally regulated. Here, we investigated the regulation and role of two major tubulin post-translational modifications, acetylation and detyrosination, which have been associated with stable microtubules. Using primary astrocytes in a wound healing assay, we show that these tubulin modifications are independently regulated during cell polarization and differently affect cell migration. In contrast to microtubule detyrosination, αTAT1-mediated microtubule acetylation increases in the vicinity of focal adhesions and promotes cell migration. We further demonstrate that αTAT1 increases focal adhesion turnover by promoting Rab6-positive vesicle fusion at focal adhesions. Our results highlight the specificity of microtubule post-translational modifications and bring new insight into the regulatory functions of tubulin acetylation.

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