Identification and cellular localization of the actin‐binding protein ABP‐120 from Entamoeba histolytica

1996 ◽  
Vol 22 (5) ◽  
pp. 849-857 ◽  
Author(s):  
Miguel Vargas ◽  
Philippe Sansonetti ◽  
Nancy Guillén
Keyword(s):  
Entamoeba Histolytica ◽  
Cellular Localization ◽  
Binding Protein ◽  
Actin Binding ◽  
Actin Binding Protein

EhNCABP166: A nucleocytoplasmic actin-binding protein from Entamoeba histolytica

2010 ◽  
Vol 172 (1) ◽  
pp. 19-30 ◽  
Author(s):  
A.D. Campos-Parra ◽  
N.A. Hernández-Cuevas ◽  
R. Hernandez-Rivas ◽  
M. Vargas
Keyword(s):  
Entamoeba Histolytica ◽  
Binding Protein ◽  
Actin Binding ◽  
Actin Binding Protein

IRSp53 is a novel interactor of SHIP2: A role of the actin binding protein Mena in their cellular localization in breast cancer cells

2020 ◽  
Vol 73 ◽  
pp. 109692
Author(s):  
Mathieu Antoine ◽  
Isabelle Vandenbroere ◽  
Somadri Ghosh ◽  
Christophe Erneux ◽  
Isabelle Pirson
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Cellular Localization ◽  
Binding Protein ◽  
Actin Binding ◽  
Actin Binding Protein

Clathrin Hub Expression Dissociates the Actin-Binding Protein Hip1R from Coated Pits and Disrupts Their Alignment with the Actin Cytoskeleton

Traffic ◽  
2001 ◽  
Vol 2 (11) ◽  
pp. 851-858 ◽  
Author(s):  
Elizabeth M. Bennett ◽  
Chih-Ying Chen ◽  
Asa E. Y. Engqvist-Goldstein ◽  
David G. Drubin ◽  
Frances M. Brodsky
Keyword(s):  
Actin Cytoskeleton ◽  
Binding Protein ◽  
Actin Binding ◽  
Coated Pits ◽  
Actin Binding Protein

Binding of Human Platelet Glycoprotein lb and Actin to Fragments of Actin-Binding Protein

1992 ◽  
Vol 67 (02) ◽  
pp. 252-257 ◽  
Author(s):  
Anne M Aakhus ◽  
J Michael Wilkinson ◽  
Nils Olav Solum
Keyword(s):  
Actin Filaments ◽  
High Speed ◽  
Binding Protein ◽  
Protein A ◽  
Actin Binding ◽  
Platelet Glycoprotein ◽  
Actin Binding Protein ◽  
Crossed Immunoelectrophoresis ◽  
Triton X ◽  
Calpain Inhibitors

SummaryActin-binding protein (ABP) is degraded into fragments of 190 and 90 kDa by calpain. A monoclonal antibody (MAb TI10) against the 90 kDa fragment of ABP coprecipitated with the glycoprotein lb (GP lb) peak observed on crossed immunoelectrophoresis of Triton X-100 extracts of platelets prepared without calpain inhibitors. MAb PM6/317 against the 190 kDa fragment was not coprecipitated with the GP lb peak under such conditions. The 90 kDa fragment was adsorbed on protein A agarose from extracts that had been preincubated with antibodies to GP lb. This supports the idea that the GP Ib-ABP interaction resides in the 90 kDa region of ABP. GP lb was sedimented with the Triton-insoluble actin filaments in trace amounts only, and only after high speed centrifugation (100,000 × g, 3 h). Both the 190 kDa and the 90 kDa fragments of ABP were sedimented with the Triton-insoluble actin filaments.

Sign in / Sign up

Export Citation Format

Share Document