Bipartite mechanism for laminin-integrin interactions: Identification of the integrin-binding site in LG domains of the laminin α chain

2020 ◽  
Vol 87 ◽  
pp. 66-76 ◽  
Author(s):  
Yukimasa Taniguchi ◽  
Mamoru Takizawa ◽  
Shaoliang Li ◽  
Kiyotoshi Sekiguchi
1994 ◽  
Vol 269 (14) ◽  
pp. 10856-10863 ◽  
Author(s):  
R.D. Bowditch ◽  
M. Hariharan ◽  
E.F. Tominna ◽  
J.W. Smith ◽  
K.M. Yamada ◽  
...  

2019 ◽  
Vol 81 ◽  
pp. 34-49 ◽  
Author(s):  
Alessandra Capuano ◽  
Eliana Pivetta ◽  
Francesca Baldissera ◽  
Giulia Bosisio ◽  
Bruna Wassermann ◽  
...  

2014 ◽  
Vol 30 (S1) ◽  
pp. A18-A19
Author(s):  
Ruimin Pan ◽  
Miroslaw K. Gorny ◽  
Susan Zolla-Pazner ◽  
Xiang-Peng Kong

2004 ◽  
Vol 15 (10) ◽  
pp. 4416-4425 ◽  
Author(s):  
Andrea Dorfleutner ◽  
Edith Hintermann ◽  
Takehiko Tarui ◽  
Yoshikazu Takada ◽  
Wolfram Ruf

In cancer and angiogenesis, coagulation-independent roles of tissue factor (TF) in cell migration are incompletely understood. Immobilized anti-TF extracellular domain antibodies induce cell spreading, but this phenomenon is epitope specific and is not induced by anti-TF 5G9. Spreading on anti-TF is β1 integrin–dependent, indicating functional interactions of the TF extracellular domain 5G9 epitope (a presumed integrin-binding site) and integrins. Recombinant TF extracellular domain supports adhesion of cells expressing αvβ3 or certain β1 integrin heterodimers (α3β1, α4β1, α5β1, α6β1, α9β1) and adhesion is blocked by specific anti-integrin antibodies or mutations in the integrin ligand-binding site. Although several studies have linked TF to cell migration, we here demonstrate that TF specifically regulates α3β1-dependent migration on laminin 5. Expression of TF suppresses α3β1-dependent migration, but only when the TF cytoplasmic domain is not phosphorylated. Suppression of migration can be reversed by 5G9, presumably by disrupting integrin interaction, or by the protease ligand VIIa, known to induce PAR-2–dependent phosphorylation of TF. In both cases, release of α3β1 inhibition is prevented by mutation of critical phosphorylation sites in the TF cytoplasmic domain. Thus, TF influences integrin-mediated migration through cooperative intra- and extracellular interactions and phosphorylation regulates TF's function in cell motility.


Blood ◽  
2018 ◽  
Vol 131 (6) ◽  
pp. 674-685 ◽  
Author(s):  
Andrea S. Rothmeier ◽  
Enbo Liu ◽  
Sagarika Chakrabarty ◽  
Jennifer Disse ◽  
Barbara M. Mueller ◽  
...  

Key Points The FVIIa integrin-binding motif is required for TF-FVIIa complex formation with integrin β1 and proangiogenic signaling. The arf6 integrin recycling pathway controls TF-FVIIa signaling and cell surface availability for procoagulant activity.


2012 ◽  
Vol 12 (7) ◽  
pp. 1501-1507 ◽  
Author(s):  
Mirela Darc ◽  
Carlos G. Schrago ◽  
Esmeralda A. Soares ◽  
Alcides Pissinatti ◽  
Albert N. Menezes ◽  
...  

2012 ◽  
Vol 21 (4) ◽  
pp. 583-588 ◽  
Author(s):  
S. D. Yogesha ◽  
Erumbi S. Rangarajan ◽  
Clemens Vonrhein ◽  
Gerard Bricogne ◽  
Tina Izard

2008 ◽  
Vol 283 (44) ◽  
pp. 30341-30350 ◽  
Author(s):  
François Rousseau ◽  
Sylvie Chevalier ◽  
Catherine Guillet ◽  
Elisa Ravon ◽  
Caroline Diveu ◽  
...  

2007 ◽  
Vol 282 (23) ◽  
pp. 17280-17288 ◽  
Author(s):  
Michèle Moes ◽  
Sophie Rodius ◽  
Stacey J. Coleman ◽  
Susan J. Monkley ◽  
Erik Goormaghtigh ◽  
...  

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