scholarly journals Identification and Characterization of the Actin-Binding Motif of Phostensin

2012 ◽  
Vol 13 (12) ◽  
pp. 15967-15982 ◽  
Author(s):  
Tzu-Fan Wang ◽  
Ning-Sheng Lai ◽  
Kuang-Yung Huang ◽  
Hsien-Lu Huang ◽  
Ming-Chi Lu ◽  
...  
Keyword(s):  
Actin Binding ◽  
Binding Motif ◽  
Identification And Characterization

Characterization of the human nebulette gene: a polymorphism in an actin-binding motif is associated with nonfamilial idiopathic dilated cardiomyopathy

2000 ◽  
Vol 107 (5) ◽  
pp. 440-451 ◽  
Author(s):  
Takuro Arimura ◽  
Takeyuki Nakamura ◽  
Shitoshi Hiroi ◽  
Manatsu Satoh ◽  
Megumi Takahashi ◽  
...  
Keyword(s):  
Dilated Cardiomyopathy ◽  
Idiopathic Dilated Cardiomyopathy ◽  
Actin Binding ◽  
Binding Motif

scholarly journals Contribution of Ena/VASP Proteins to Intracellular Motility ofListeriaRequires Phosphorylation and Proline-rich Core but Not F-Actin Binding or Multimerization

2002 ◽  
Vol 13 (7) ◽  
pp. 2383-2396 ◽  
Author(s):  
Marcus Geese ◽  
Joseph J. Loureiro ◽  
James E. Bear ◽  
Jürgen Wehland ◽  
Frank B. Gertler ◽  
...  
Keyword(s):  
Bacterial Motility ◽  
Actin Binding ◽  
Rich Region ◽  
Bacterial Surface ◽  
Identification And Characterization ◽  
Actin Binding Site ◽  
Intracellular Motility ◽  
Proline Rich Region

The Listeria model system has been essential for the identification and characterization of key regulators of the actin cytoskeleton such as the Arp2/3 complex and Ena/vasodilator-stimulated phosphoprotein (VASP) proteins. Although the role of Ena/VASP proteins in Listeria motility has been extensively studied, little is known about the contributions of their domains and phosphorylation state to bacterial motility. To address these issues, we have generated a panel of Ena/VASP mutants and, upon expression in Ena/VASP-deficient cells, evaluated their contribution to Ena/VASP function in Listeria motility. The proline-rich region, the putative G-actin binding site, and the Ser/Thr phosphorylation of Ena/VASP proteins are all required for efficientListeria motility. Surprisingly, the interaction of Ena/VASP proteins with F-actin and their potential ability to form multimers are both dispensable for their involvement in this process. Our data suggest that Ena/VASP proteins contribute toListeria motility by regulating both the nucleation and elongation of actin filaments at the bacterial surface.

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